{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T07:25:36Z","timestamp":1790839536203,"version":"4.1.0"},"reference-count":155,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,9,5]],"date-time":"2022-09-05T00:00:00Z","timestamp":1662336000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100011531","name":"University of Alabama","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011531","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM137958-02"],"award-info":[{"award-number":["GM137958-02"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["K08 GM144788-01"],"award-info":[{"award-number":["K08 GM144788-01"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM146859-01"],"award-info":[{"award-number":["GM146859-01"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Matrix Biology Plus"],"published-print":{"date-parts":[[2022,12]]},"DOI":"10.1016\/j.mbplus.2022.100121","type":"journal-article","created":{"date-parts":[[2022,9,7]],"date-time":"2022-09-07T13:25:47Z","timestamp":1662557147000},"page":"100121","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":54,"special_numbering":"C","title":["Alterations in heparan sulfate proteoglycan synthesis and sulfation and the impact on vascular endothelial function"],"prefix":"10.1016","volume":"16","author":[{"given":"Danielle","family":"Pretorius","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert P.","family":"Richter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanya","family":"Anand","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jessica C.","family":"Cardenas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jillian R.","family":"Richter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0005","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1006\/mvre.1999.2177","article-title":"A new view of Starling's hypothesis at the microstructural level","volume":"58","author":"Hu","year":"1999","journal-title":"Microvasc. Res."},{"issue":"9","key":"10.1016\/j.mbplus.2022.100121_b0010","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1161\/01.ATV.0000085630.24353.3D","article-title":"Endothelial cell glycocalyx modulates immobilization of leukocytes at the endothelial surface","volume":"23","author":"Constantinescu","year":"2003","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0015","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1146\/annurev.cb.08.110192.002053","article-title":"Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans","volume":"8","author":"Bernfield","year":"1992","journal-title":"Annu. Rev. Cell. Biol."},{"issue":"9","key":"10.1016\/j.mbplus.2022.100121_b0020","doi-asserted-by":"crossref","first-page":"2062","DOI":"10.1172\/JCI119377","article-title":"Heparan sulfate proteoglycans of the cardiovascular system. Specific structures emerge but how is synthesis regulated?","volume":"99","author":"Rosenberg","year":"1997","journal-title":"J. Clin. Invest."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0025","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1146\/annurev.bioeng.9.060906.151959","article-title":"The structure and function of the endothelial glycocalyx layer","volume":"9","author":"Weinbaum","year":"2007","journal-title":"Annu. Rev. Biomed. Eng."},{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0030","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1039\/C3IB40199E","article-title":"Shear-induced endothelial NOS activation and remodeling via heparan sulfate, glypican-1, and syndecan-1","volume":"6","author":"Ebong","year":"2014","journal-title":"Integr. Biol. (Camb.)"},{"issue":"Pt 2","key":"10.1016\/j.mbplus.2022.100121_b0035","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1042\/bj20030729","article-title":"Interleukin-8 binds to syndecan-2 on human endothelial cells","volume":"377","author":"Halden","year":"2004","journal-title":"Biochem. J."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0040","doi-asserted-by":"crossref","first-page":"e0214737","DOI":"10.1371\/journal.pone.0214737","article-title":"Thrombin-cleaved syndecan-3\/-4 ectodomain fragments mediate endothelial barrier dysfunction","volume":"14","author":"Jannaway","year":"2019","journal-title":"PLoS One"},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0045","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1161\/01.RES.0000159708.71142.c8","article-title":"Syndecans: new kids on the signaling block","volume":"96","author":"Tkachenko","year":"2005","journal-title":"Circ. Res."},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0050","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/S0962-8924(02)00039-9","article-title":"Caveolae: anchored, multifunctional platforms in the lipid ocean","volume":"13","author":"van Deurs","year":"2003","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.mbplus.2022.100121_b0055","doi-asserted-by":"crossref","unstructured":"Zeng, Y., Waters, M., Andrews, A., Honarmandi, P., Ebong, E.E., Rizzo, V., et al., (2013). Fluid shear stress induces the clustering of heparan sulfate via mobility of glypican-1 in lipid rafts. Am. J. Physiol. Heart Circ. Physiol., 305 (6), H811-820.","DOI":"10.1152\/ajpheart.00764.2012"},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0060","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1038\/nrm.2017.16","article-title":"The mystery of membrane organization: composition, regulation and roles of lipid rafts","volume":"18","author":"Sezgin","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0065","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.yjmcc.2011.07.007","article-title":"Caveolae create local signalling domains through their distinct protein content, lipid profile and morphology","volume":"52","author":"Harvey","year":"2012","journal-title":"J. Mol. Cell. Cardiol."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0070","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1146\/annurev.biochem.68.1.729","article-title":"Functions of cell surface heparan sulfate proteoglycans","volume":"68","author":"Bernfield","year":"1999","journal-title":"Annu. Rev. Biochem."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0075","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1186\/gb-2008-9-5-224","article-title":"Glypicans","volume":"9","author":"Filmus","year":"2008","journal-title":"Genome Biol."},{"issue":"Pt 2","key":"10.1016\/j.mbplus.2022.100121_b0080","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1242\/jcs.113.2.193","article-title":"Synthesis and sorting of proteoglycans","volume":"113","author":"Prydz","year":"2000","journal-title":"J. Cell Sci."},{"issue":"12","key":"10.1016\/j.mbplus.2022.100121_b0085","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1369\/0022155412460056","article-title":"Heparan sulfate biosynthesis: methods for investigation of the heparanosome","volume":"60","author":"Multhaupt","year":"2012","journal-title":"J. Histochem. Cytochem."},{"issue":"12","key":"10.1016\/j.mbplus.2022.100121_b0090","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1369\/0022155412464972","article-title":"Heparan sulfate biosynthesis: regulation and variability","volume":"60","author":"Kreuger","year":"2012","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/j.mbplus.2022.100121_b0095","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.matbio.2013.10.001","article-title":"The exostosin family: proteins with many functions","volume":"35","author":"Busse-Wicher","year":"2014","journal-title":"Matrix Biol."},{"issue":"Pt 3","key":"10.1016\/j.mbplus.2022.100121_b0100","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1042\/bj2930849","article-title":"N.m.r. and molecular-modelling studies of the solution conformation of heparin","volume":"293","author":"Mulloy","year":"1993","journal-title":"Biochem. J."},{"key":"10.1016\/j.mbplus.2022.100121_b0105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1877-1173(10)93001-9","article-title":"Glycosaminoglycan (GAG) biosynthesis and GAG-binding proteins","volume":"93","author":"Zhang","year":"2010","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"10.1016\/j.mbplus.2022.100121_b0110","doi-asserted-by":"crossref","first-page":"507","DOI":"10.3389\/fonc.2019.00507","article-title":"The emerging roles of heparan sulfate 3-o-sulfotransferases in cancer","volume":"9","author":"Denys","year":"2019","journal-title":"Front. Oncol."},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0115","doi-asserted-by":"crossref","first-page":"1670","DOI":"10.1016\/S0006-3495(01)76139-5","article-title":"An electrochemical model of the transport of charged molecules through the capillary glycocalyx","volume":"80","author":"Stace","year":"2001","journal-title":"Biophys. J."},{"key":"10.1016\/j.mbplus.2022.100121_b0120","doi-asserted-by":"crossref","unstructured":"Haaren, P.M.A.v., VanBavel, E., Vink, H., Spaan, J.A.E., (2005). Charge modification of the endothelial surface layer modulates the permeability barrier of isolated rat mesenteric small arteries. Am. J. Physiol. Heart Circ. Physiol., 289 (6), H2503-H2507.","DOI":"10.1152\/ajpheart.00587.2005"},{"key":"10.1016\/j.mbplus.2022.100121_b0125","doi-asserted-by":"crossref","unstructured":"Mulivor, A.W., Lipowsky, H.H., (2002). Role of glycocalyx in leukocyte-endothelial cell adhesion. Am. J. Physiol. Heart Circ. Physiol., 283 (4), H1282-1291.","DOI":"10.1152\/ajpheart.00117.2002"},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0130","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/0092-8674(91)90512-W","article-title":"Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor","volume":"64","author":"Yayon","year":"1991","journal-title":"Cell"},{"issue":"22","key":"10.1016\/j.mbplus.2022.100121_b0135","doi-asserted-by":"crossref","first-page":"15947","DOI":"10.1074\/jbc.274.22.15947","article-title":"Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase","volume":"274","author":"Kan","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0140","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1096\/fasebj.14.1.137","article-title":"Differential ability of heparan sulfate proteoglycans to assemble the fibroblast growth factor receptor complex in situ","volume":"14","author":"Chang","year":"2000","journal-title":"FASEB J."},{"issue":"Pt 5","key":"10.1016\/j.mbplus.2022.100121_b0145","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1242\/jcs.114.5.853","article-title":"The splice variants of vascular endothelial growth factor (VEGF) and their receptors","volume":"114","author":"Robinson","year":"2001","journal-title":"J. Cell Sci."},{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0150","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/j.bbapap.2009.09.002","article-title":"Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling","volume":"1804","author":"Grunewald","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0155","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1074\/jbc.M110.177006","article-title":"Heparan sulfate regulates VEGF165- and VEGF121-mediated vascular hyperpermeability","volume":"286","author":"Xu","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0160","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1114\/1.134","article-title":"1997 Whitaker Distinguished Lecture: Models to solve mysteries in biomechanics at the cellular level; a new view of fiber matrix layers","volume":"26","author":"Weinbaum","year":"1998","journal-title":"Ann. Biomed. Eng."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0165","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1097\/00000542-200405000-00025","article-title":"Endothelial glycocalyx as an additional barrier determining extravasation of 6% hydroxyethyl starch or 5% albumin solutions in the coronary vascular bed","volume":"100","author":"Rehm","year":"2004","journal-title":"Anesthesiology"},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0170","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1097\/00000542-200606000-00018","article-title":"Contrasting effects of colloid and crystalloid resuscitation fluids on cardiac vascular permeability","volume":"104","author":"Jacob","year":"2006","journal-title":"Anesthesiology"},{"issue":"7","key":"10.1016\/j.mbplus.2022.100121_b0175","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1111\/aas.13593","article-title":"The extended starling principle needs clinical validation","volume":"64","author":"Hahn","year":"2020","journal-title":"Acta Anaesthesiol. Scand."},{"issue":"47","key":"10.1016\/j.mbplus.2022.100121_b0180","doi-asserted-by":"crossref","first-page":"16483","DOI":"10.1073\/pnas.0407474101","article-title":"The role of the glycocalyx in reorganization of the actin cytoskeleton under fluid shear stress: a \u201cbumper-car\u201d model","volume":"101","author":"Thi","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"15","key":"10.1016\/j.mbplus.2022.100121_b0185","article-title":"Glycocalyx heparan sulfate cleavage promotes endothelial cell angiopoietin-2 expression by impairing shear stress-related AMPK\/FoxO1 signaling. JCI","volume":"7","author":"Richter","year":"2022","journal-title":"Insight."},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0190","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1161\/ATVBAHA.119.313399","article-title":"Shear stress regulation of endothelial glycocalyx structure is determined by glucobiosynthesis","volume":"40","author":"Wang","year":"2020","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.mbplus.2022.100121_b0195","doi-asserted-by":"crossref","unstructured":"Florian, J.A., Kosky, J.R., Ainslie, K., Pang, Z., Dull, R.O., Tarbell, J.M., (2003). Heparan sulfate proteoglycan is a mechanosensor on endothelial cells. Circ. Res., 93 (10), e136-142.","DOI":"10.1161\/01.RES.0000101744.47866.D5"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0200","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.bbrc.2007.01.137","article-title":"The role of endothelial glycocalyx components in mechanotransduction of fluid shear stress","volume":"355","author":"Pahakis","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0205","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1083\/jcb.111.3.1293","article-title":"Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: antithrombin binding on cultured endothelial cells and perfused rat aorta","volume":"111","author":"de Agostini","year":"1990","journal-title":"J. Cell Biol."},{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0210","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.jamcollsurg.2017.05.012","article-title":"Syndecan-1: A quantitative marker for the endotheliopathy of trauma","volume":"225","author":"Rodriguez","year":"2017","journal-title":"J. Am. Coll. Surg."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0215","doi-asserted-by":"crossref","DOI":"10.1186\/s13054-019-2534-2","article-title":"Intravenous fluid resuscitation is associated with septic endothelial glycocalyx degradation","volume":"23","author":"Hippensteel","year":"2019","journal-title":"Crit. Care"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0220","doi-asserted-by":"crossref","DOI":"10.1186\/s10020-021-00412-1","article-title":"Syndecan-1, an indicator of endothelial glycocalyx degradation, predicts outcome of patients admitted to an ICU with COVID-19","volume":"27","author":"Zhang","year":"2021","journal-title":"Mol. Med."},{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0225","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1111\/bcp.12629","article-title":"Degradation of the endothelial glycocalyx in clinical settings: searching for the sheddases","volume":"80","author":"Becker","year":"2015","journal-title":"Br. J. Clin. Pharmacol."},{"key":"10.1016\/j.mbplus.2022.100121_b0230","doi-asserted-by":"crossref","DOI":"10.1016\/j.mbplus.2021.100094","article-title":"Endothelial glycocalyx degradation during sepsis: Causes and consequences","volume":"12","author":"Sullivan","year":"2021","journal-title":"Matrix. Biol. Plus"},{"key":"10.1016\/j.mbplus.2022.100121_b0235","doi-asserted-by":"crossref","DOI":"10.3389\/fmed.2022.898592","article-title":"Endothelial glycocalyx degradation in critical illness and injury","volume":"9","author":"Patterson","year":"2022","journal-title":"Front. Med."},{"issue":"31","key":"10.1016\/j.mbplus.2022.100121_b0240","doi-asserted-by":"crossref","first-page":"18759","DOI":"10.1074\/jbc.271.31.18759","article-title":"Suppression of syndecan-1 expression in endothelial cells by tumor necrosis factor-alpha","volume":"271","author":"Kainulainen","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0245","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1369\/0022155415568995","article-title":"Syndecan-4 is a major syndecan in primary human endothelial cells in vitro, modulated by inflammatory stimuli and involved in wound healing","volume":"63","author":"Vuong","year":"2015","journal-title":"J. Histochem. Cytochem."},{"issue":"10","key":"10.1016\/j.mbplus.2022.100121_b0250","doi-asserted-by":"crossref","first-page":"3698","DOI":"10.3390\/ijms21103698","article-title":"Cell density-dependent fibroblast growth factor-2 signaling regulates syndecan-4 expression in cultured vascular endothelial cells","volume":"21","author":"Hara","year":"2020","journal-title":"Int. J. Mol. Sci."},{"issue":"8","key":"10.1016\/j.mbplus.2022.100121_b0255","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.1002\/jcb.25861","article-title":"Transforming growth factor-beta1 modulates the expression of syndecan-4 in cultured vascular endothelial cells in a biphasic manner","volume":"118","author":"Hara","year":"2017","journal-title":"J. Cell. Biochem."},{"issue":"23","key":"10.1016\/j.mbplus.2022.100121_b0260","doi-asserted-by":"crossref","first-page":"11035","DOI":"10.1073\/pnas.91.23.11035","article-title":"Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds","volume":"91","author":"Gallo","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"24","key":"10.1016\/j.mbplus.2022.100121_b0265","doi-asserted-by":"crossref","first-page":"3103","DOI":"10.1161\/01.CIR.99.24.3103","article-title":"Membrane type 1 matrix metalloproteinase expression in human atherosclerotic plaques: evidence for activation by proinflammatory mediators","volume":"99","author":"Rajavashisth","year":"1999","journal-title":"Circulation"},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0270","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1165\/rcmb.2009-0269OC","article-title":"High-mobility group box 1-mediated matrix metalloproteinase-9 expression in non-small cell lung cancer contributes to tumor cell invasiveness","volume":"43","author":"Liu","year":"2010","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0275","doi-asserted-by":"crossref","first-page":"349","DOI":"10.4049\/jimmunol.1301906","article-title":"IL-6-mediated induction of matrix metalloproteinase-9 is modulated by JAK-dependent IL-10 expression in macrophages","volume":"192","author":"Kothari","year":"2014","journal-title":"J. Immunol."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0280","doi-asserted-by":"crossref","DOI":"10.1186\/s12974-022-02412-2","article-title":"The role of S100B\/RAGE-enhanced ADAM17 activation in endothelial glycocalyx shedding after traumatic brain injury","volume":"19","author":"Zou","year":"2022","journal-title":"J. Neuroinflammation"},{"key":"10.1016\/j.mbplus.2022.100121_b0285","article-title":"Syndecan-1 downregulates syndecan-4 expression by suppressing the ERK1\/2 and p38 MAPK signaling pathways in cultured vascular endothelial cells","volume":"26","author":"Hara","year":"2021","journal-title":"Biochem. Biophys. Rep."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0290","doi-asserted-by":"crossref","first-page":"15811","DOI":"10.1038\/s41598-020-73021-3","article-title":"miR-19b targets pulmonary endothelial syndecan-1 following hemorrhagic shock","volume":"10","author":"Wu","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mbplus.2022.100121_b0295","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.yjmcc.2016.05.007","article-title":"The role of miR-126 in embryonic angiogenesis, adult vascular homeostasis, and vascular repair and its alterations in atherosclerotic disease","volume":"97","author":"Chistiakov","year":"2016","journal-title":"J. Mol. Cell. Cardiol."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0300","first-page":"2132","article-title":"Influences of up-regulation of miR-126 on septic inflammation and prognosis through AKT\/Rac1 signaling pathway","volume":"23","author":"Wang","year":"2019","journal-title":"Eur. Rev. Med. Pharmacol. Sci."},{"key":"10.1016\/j.mbplus.2022.100121_b0305","doi-asserted-by":"crossref","DOI":"10.1155\/2015\/497280","article-title":"miR-126 is involved in vascular remodeling under laminar shear stress","volume":"2015","author":"Mondadori dos Santos","year":"2015","journal-title":"Biomed. Res. Int."},{"issue":"Pt 6","key":"10.1016\/j.mbplus.2022.100121_b0310","first-page":"1169","article-title":"Autoregulation of glypican-1 by intronic microRNA-149 fine tunes the angiogenic response to FGF2 in human endothelial cells","volume":"127","author":"Chamorro-Jorganes","year":"2014","journal-title":"J. Cell Sci."},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0315","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1165\/rcmb.2016-0338OC","article-title":"Fibroblast growth factor signaling mediates pulmonary endothelial glycocalyx reconstitution","volume":"56","author":"Yang","year":"2017","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0320","doi-asserted-by":"crossref","first-page":"e86249","DOI":"10.1371\/journal.pone.0086249","article-title":"The adaptive remodeling of endothelial glycocalyx in response to fluid shear stress","volume":"9","author":"Zeng","year":"2014","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0325","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1186\/s12967-018-1721-2","article-title":"Pro-atherosclerotic disturbed flow disrupts caveolin-1 expression, localization, and function via glycocalyx degradation","volume":"16","author":"Harding","year":"2018","journal-title":"J. Transl. Med."},{"issue":"11","key":"10.1016\/j.mbplus.2022.100121_b0330","doi-asserted-by":"crossref","first-page":"e0241040","DOI":"10.1371\/journal.pone.0241040","article-title":"Altered shear stress on endothelial cells leads to remodeling of extracellular matrix and induction of angiogenesis","volume":"15","author":"Russo","year":"2020","journal-title":"PLoS One"},{"key":"10.1016\/j.mbplus.2022.100121_b0335","doi-asserted-by":"crossref","unstructured":"Koo, A., Dewey, C.F., Jr., Garcia-Cardena, G., (2013). Hemodynamic shear stress characteristic of atherosclerosis-resistant regions promotes glycocalyx formation in cultured endothelial cells. Am. J. Physiol. Cell Physiol., 304 (2), C137-146.","DOI":"10.1152\/ajpcell.00187.2012"},{"issue":"41","key":"10.1016\/j.mbplus.2022.100121_b0340","doi-asserted-by":"crossref","first-page":"14871","DOI":"10.1073\/pnas.0406073101","article-title":"Distinct endothelial phenotypes evoked by arterial waveforms derived from atherosclerosis-susceptible and -resistant regions of human vasculature","volume":"101","author":"Dai","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.mbplus.2022.100121_b0345","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.coph.2019.04.011","article-title":"The role of the endothelial glycocalyx in advanced age and cardiovascular disease","volume":"45","author":"Machin","year":"2019","journal-title":"Curr. Opin. Pharmacol."},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0350","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1093\/cvr\/cvaa201","article-title":"The glycocalyx core protein Glypican 1 protects vessel wall endothelial cells from stiffness-mediated dysfunction and disease","volume":"117","author":"Mahmoud","year":"2021","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.mbplus.2022.100121_b0355","doi-asserted-by":"crossref","unstructured":"Kang, H., Sun, A., Wu, Q., Yang, J., Zhang, W., Qu, Y., et al., (2020). Atherogenic diet-diminished endothelial glycocalyx contributes to impaired vasomotor properties in rat. Am. J. Physiol. Heart Circ. Physiol., 319 (4), H814-H823.","DOI":"10.1152\/ajpheart.00039.2020"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0360","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1038\/sj.ki.5002573","article-title":"Heparan sulfate domains on cultured activated glomerular endothelial cells mediate leukocyte trafficking","volume":"73","author":"Rops","year":"2008","journal-title":"Kidney Int."},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0365","doi-asserted-by":"crossref","first-page":"809","DOI":"10.3390\/biom11060809","article-title":"HA and HS changes in endothelial inflammatory activation","volume":"11","author":"Carav\u00e0","year":"2021","journal-title":"Biomolecules"},{"issue":"52","key":"10.1016\/j.mbplus.2022.100121_b0370","doi-asserted-by":"crossref","first-page":"41143","DOI":"10.1074\/jbc.M110.153791","article-title":"The heparan sulfate motif (GlcNS6S-IdoA2S)3, common in heparin, has a strict topography and is involved in cell behavior and disease","volume":"285","author":"Smits","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2022.100121_b0375","doi-asserted-by":"crossref","unstructured":"Oshima, K., Han, X., Ouyang, Y., El Masri, R., Yang, Y., Haeger, S.M., et al., (2019). Loss of endothelial sulfatase-1 after experimental sepsis attenuates subsequent pulmonary inflammatory responses. Am. J. Physiol. Lung Cell Mol. Physiol., 317 (5), L667-L677.","DOI":"10.1152\/ajplung.00175.2019"},{"issue":"Pt 9","key":"10.1016\/j.mbplus.2022.100121_b0380","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1242\/jcs.115.9.1951","article-title":"Increased responsiveness of hypoxic endothelial cells to FGF2 is mediated by HIF-1alpha-dependent regulation of enzymes involved in synthesis of heparan sulfate FGF2-binding sites","volume":"115","author":"Li","year":"2002","journal-title":"J. Cell Sci."},{"issue":"9","key":"10.1016\/j.mbplus.2022.100121_b0385","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1161\/CIRCRESAHA.119.315023","article-title":"Heparan sulfate-editing extracellular sulfatases enhance VEGF bioavailability for ischemic heart repair","volume":"125","author":"Korf-Klingebiel","year":"2019","journal-title":"Circ. Res."},{"issue":"12","key":"10.1016\/j.mbplus.2022.100121_b0390","doi-asserted-by":"crossref","first-page":"4751","DOI":"10.1073\/pnas.0705807105","article-title":"Heparan sulfate biosynthesis enzymes EXT1 and EXT2 affect NDST1 expression and heparan sulfate sulfation","volume":"105","author":"Presto","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"14","key":"10.1016\/j.mbplus.2022.100121_b0395","doi-asserted-by":"crossref","first-page":"9547","DOI":"10.1074\/jbc.M113.541573","article-title":"Loss of syndecan-1 induces a pro-inflammatory phenotype in endothelial cells with a dysregulated response to atheroprotective flow","volume":"289","author":"Voyvodic","year":"2014","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0400","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.bpj.2017.05.033","article-title":"Endothelial glycocalyx-mediated nitric oxide production in response to selective AFM pulling","volume":"113","author":"Bartosch","year":"2017","journal-title":"Biophys. J."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0405","doi-asserted-by":"crossref","first-page":"11386","DOI":"10.1038\/s41598-021-90941-w","article-title":"Heparan sulfate proteoglycan glypican-1 and PECAM-1 cooperate in shear-induced endothelial nitric oxide production","volume":"11","author":"Bartosch","year":"2021","journal-title":"Sci. Rep."},{"issue":"9","key":"10.1016\/j.mbplus.2022.100121_b0410","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1038\/ni1233","article-title":"Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses","volume":"6","author":"Wang","year":"2005","journal-title":"Nat. Immunol."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0415","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1038\/ki.2014.115","article-title":"Modulation of heparan sulfate in the glomerular endothelial glycocalyx decreases leukocyte influx during experimental glomerulonephritis","volume":"86","author":"LWMM Rops","year":"2014","journal-title":"Kidney Int."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0420","doi-asserted-by":"crossref","first-page":"13433","DOI":"10.1038\/s41598-018-31779-7","article-title":"Selective deletion of heparan sulfotransferase enzyme, Ndst1, in donor endothelial and myeloid precursor cells significantly decreases acute allograft rejection","volume":"8","author":"Chen","year":"2018","journal-title":"Sci. Rep."},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0425","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1080\/01902148.2018.1451574","article-title":"Regulation of eosinophil recruitment and allergic airway inflammation by heparan sulfate proteoglycan (HSPG) modifying enzymes","volume":"44","author":"Ge","year":"2018","journal-title":"Exp. Lung Res."},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0430","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1038\/s41374-017-0015-2","article-title":"Endothelial heparan sulfate deficiency reduces inflammation and fibrosis in murine diabetic nephropathy","volume":"98","author":"Talsma","year":"2018","journal-title":"Lab. Invest."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0435","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01181-21","article-title":"Endothelial heparan sulfate mediates hepatic neutrophil trafficking and injury during staphylococcus aureus sepsis","volume":"12","author":"Golden","year":"2021","journal-title":"mBio"},{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0440","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1007\/s10719-021-10018-8","article-title":"Structural characteristics of Heparan sulfate required for the binding with the virus processing Enzyme Furin","volume":"39","author":"Zeng","year":"2022","journal-title":"Glycoconj. J."},{"issue":"26","key":"10.1016\/j.mbplus.2022.100121_b0445","doi-asserted-by":"crossref","first-page":"16157","DOI":"10.1074\/jbc.M115.660852","article-title":"2-O-Sulfated domains in syndecan-1 heparan sulfate inhibit neutrophil cathelicidin and promote staphylococcus aureus corneal infection","volume":"290","author":"Hayashida","year":"2015","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.mbplus.2022.100121_b0450","doi-asserted-by":"crossref","first-page":"6551","DOI":"10.1073\/pnas.77.11.6551","article-title":"Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin","volume":"77","author":"Lindahl","year":"1980","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"11","key":"10.1016\/j.mbplus.2022.100121_b0455","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1016\/j.biochi.2010.05.011","article-title":"Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors","volume":"92","author":"Olson","year":"2010","journal-title":"Biochimie"},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0460","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1111\/jth.13920","article-title":"Expression and functional characterization of two natural heparin-binding site variants of antithrombin","volume":"16","author":"Dinarvand","year":"2018","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.mbplus.2022.100121_b0465","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.matbio.2017.01.003","article-title":"HS3ST1 genotype regulates antithrombin's inflammomodulatory tone and associates with atherosclerosis","volume":"63","author":"Smits","year":"2017","journal-title":"Matrix Biol."},{"issue":"40","key":"10.1016\/j.mbplus.2022.100121_b0470","doi-asserted-by":"crossref","first-page":"37912","DOI":"10.1074\/jbc.M204209200","article-title":"Heparan sulfate 3-o-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, Type 1","volume":"277","author":"Xia","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"43","key":"10.1016\/j.mbplus.2022.100121_b0475","doi-asserted-by":"crossref","first-page":"36132","DOI":"10.1074\/jbc.M112.384875","article-title":"Endothelial heparan sulfate 6-O-sulfation levels regulate angiogenic responses of endothelial cells to fibroblast growth factor 2 and vascular endothelial growth factor","volume":"287","author":"Ferreras","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"14","key":"10.1016\/j.mbplus.2022.100121_b0480","doi-asserted-by":"crossref","first-page":"4833","DOI":"10.1073\/pnas.0401028101","article-title":"QSulf1, a heparan sulfate 6-O-endosulfatase, inhibits fibroblast growth factor signaling in mesoderm induction and angiogenesis","volume":"101","author":"Wang","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"8","key":"10.1016\/j.mbplus.2022.100121_b0485","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1038\/nm.2843","article-title":"The pulmonary endothelial glycocalyx regulates neutrophil adhesion and lung injury during experimental sepsis","volume":"18","author":"Schmidt","year":"2012","journal-title":"Nat. Med."},{"issue":"11","key":"10.1016\/j.mbplus.2022.100121_b0490","doi-asserted-by":"crossref","first-page":"2885","DOI":"10.1681\/ASN.2007010119","article-title":"Glomerular endothelial glycocalyx constitutes a barrier to protein permeability","volume":"18","author":"Singh","year":"2007","journal-title":"J. Am. Soc. Nephrol."},{"issue":"7","key":"10.1016\/j.mbplus.2022.100121_b0495","doi-asserted-by":"crossref","first-page":"e1005738","DOI":"10.1371\/journal.ppat.1005738","article-title":"Dengue virus NS1 disrupts the endothelial glycocalyx, leading to hyperpermeability","volume":"12","author":"Puerta-Guardo","year":"2016","journal-title":"PLoS Pathog."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0500","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/j.kint.2019.09.035","article-title":"Blocking matrix metalloproteinase-mediated syndecan-4 shedding restores the endothelial glycocalyx and glomerular filtration barrier function in early diabetic kidney disease","volume":"97","author":"Ramnath","year":"2020","journal-title":"Kidney Int."},{"issue":"48","key":"10.1016\/j.mbplus.2022.100121_b0505","doi-asserted-by":"crossref","first-page":"17308","DOI":"10.1073\/pnas.1413725111","article-title":"Syndecan 4 is required for endothelial alignment in flow and atheroprotective signaling","volume":"111","author":"Baeyens","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"12","key":"10.1016\/j.mbplus.2022.100121_b0510","doi-asserted-by":"crossref","first-page":"e12636","DOI":"10.14814\/phy2.12636","article-title":"TNF causes changes in glomerular endothelial permeability and morphology through a Rho and myosin light chain kinase-dependent mechanism","volume":"3","author":"Xu","year":"2015","journal-title":"Physiol. Rep."},{"issue":"12","key":"10.1016\/j.mbplus.2022.100121_b0515","doi-asserted-by":"crossref","first-page":"e0167576","DOI":"10.1371\/journal.pone.0167576","article-title":"Glycocalyx degradation induces a proinflammatory phenotype and increased leukocyte adhesion in cultured endothelial cells under flow","volume":"11","author":"McDonald","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.mbplus.2022.100121_b0520","doi-asserted-by":"crossref","unstructured":"Lipowsky, H.H., Gao, L., Lescanic, A., (2011). Shedding of the endothelial glycocalyx in arterioles, capillaries, and venules and its effect on capillary hemodynamics during inflammation. Am. J. Physiol. Heart Circ. Physiol., 301 (6), H2235-2245.","DOI":"10.1152\/ajpheart.00803.2011"},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0525","doi-asserted-by":"crossref","first-page":"e10510","DOI":"10.1371\/journal.pone.0010510","article-title":"Inhibition of chemokine-glycosaminoglycan interactions in donor tissue reduces mouse allograft vasculopathy and transplant rejection","volume":"5","author":"Dai","year":"2010","journal-title":"PLoS One"},{"issue":"21","key":"10.1016\/j.mbplus.2022.100121_b0530","doi-asserted-by":"crossref","first-page":"11727","DOI":"10.1073\/pnas.2003138117","article-title":"Cell entry mechanisms of SARS-CoV-2","volume":"117","author":"Shang","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0535","doi-asserted-by":"crossref","first-page":"12157","DOI":"10.1038\/s41598-021-91231-1","article-title":"Endothelial glycocalyx shields the interaction of SARS-CoV-2 spike protein with ACE2 receptors","volume":"11","author":"Targosz-Korecka","year":"2021","journal-title":"Sci. Rep."},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0540","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.cell.2020.09.033","article-title":"SARS-CoV-2 infection depends on cellular heparan sulfate and ACE2","volume":"183","author":"Clausen","year":"2020","journal-title":"Cell"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0545","doi-asserted-by":"crossref","first-page":"4263","DOI":"10.1038\/s41598-021-82862-5","article-title":"Causes of death and comorbidities in hospitalized patients with COVID-19","volume":"11","author":"Elezkurtaj","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mbplus.2022.100121_b0550","doi-asserted-by":"crossref","unstructured":"Lee, D.H., Dane, M.J., van den Berg, B.M., Boels, M.G., van Teeffelen, J.W., de Mutsert, R., et al., (2014). Deeper penetration of erythrocytes into the endothelial glycocalyx is associated with impaired microvascular perfusion. PLoS One, 9 (5), e96477.","DOI":"10.1371\/journal.pone.0096477"},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0555","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1111\/jch.13236","article-title":"Association of impaired endothelial glycocalyx with arterial stiffness, coronary microcirculatory dysfunction, and abnormal myocardial deformation in untreated hypertensives","volume":"20","author":"Ikonomidis","year":"2018","journal-title":"J. Clin. Hypertens. (Greenwich)"},{"issue":"5432","key":"10.1016\/j.mbplus.2022.100121_b0560","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1038\/246355a0","article-title":"Anticoagulant action of heparin","volume":"246","author":"Damus","year":"1973","journal-title":"Nature"},{"key":"10.1016\/j.mbplus.2022.100121_b0565","doi-asserted-by":"crossref","unstructured":"Marcum, J.A., Fritze, L., Galli, S.J., Karp, G., Rosenberg, R.D., (1983). Microvascular heparin-like species with anticoagulant activity. Am. J. Physiol. Heart Circ. Physiol., 245 (5 Pt 1), H725-733.","DOI":"10.1152\/ajpheart.1983.245.5.H725"},{"issue":"27","key":"10.1016\/j.mbplus.2022.100121_b0570","doi-asserted-by":"crossref","first-page":"16838","DOI":"10.1074\/jbc.272.27.16838","article-title":"Role of heparan sulfate proteoglycans in the uptake and degradation of tissue factor pathway inhibitor-coagulation factor Xa complexes","volume":"272","author":"Ho","year":"1997","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.mbplus.2022.100121_b0575","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1172\/JCI200315809","article-title":"Normal levels of anticoagulant heparan sulfate are not essential for normal hemostasis","volume":"111","author":"HajMohammadi","year":"2003","journal-title":"J. Clin. Invest."},{"issue":"17","key":"10.1016\/j.mbplus.2022.100121_b0580","doi-asserted-by":"crossref","first-page":"9311","DOI":"10.1073\/pnas.1920880117","article-title":"ZNF263 is a transcriptional regulator of heparin and heparan sulfate biosynthesis","volume":"117","author":"Weiss","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"40","key":"10.1016\/j.mbplus.2022.100121_b0585","doi-asserted-by":"crossref","first-page":"27054","DOI":"10.1074\/jbc.M109.029892","article-title":"The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation","volume":"284","author":"Richard","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"12","key":"10.1016\/j.mbplus.2022.100121_b0590","doi-asserted-by":"crossref","first-page":"3142","DOI":"10.1111\/jth.15052","article-title":"Anticoagulant and signaling functions of antithrombin","volume":"18","author":"Rezaie","year":"2020","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.mbplus.2022.100121_b0595","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S1877-1173(10)93008-1","article-title":"Anticoagulant heparan sulfate to not clot\u2013or not?","volume":"93","author":"Shworak","year":"2010","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"issue":"02","key":"10.1016\/j.mbplus.2022.100121_b0600","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1160\/TH14-04-0360","article-title":"Antithrombin up-regulates AMP-activated protein kinase signalling during myocardial ischaemia\/reperfusion injury","volume":"113","author":"Ma","year":"2015","journal-title":"Thromb. Haemost."},{"issue":"92","key":"10.1016\/j.mbplus.2022.100121_b0605","doi-asserted-by":"crossref","first-page":"14423","DOI":"10.1039\/D0CC05893A","article-title":"Visualizing antithrombin-binding 3-O-sulfated heparan sulfate motifs on cell surfaces","volume":"56","author":"Kalita","year":"2020","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/j.mbplus.2022.100121_b0610","doi-asserted-by":"crossref","unstructured":"Iwakiri, Y., Tsai, M.H., McCabe, T.J., Gratton, J.P., Fulton, D., Groszmann, R.J., et al., (2002). Phosphorylation of eNOS initiates excessive NO production in early phases of portal hypertension. Am. J. Physiol. Heart Circ. Physiol., 282 (6), H2084-2090.","DOI":"10.1152\/ajpheart.00675.2001"},{"issue":"10","key":"10.1016\/j.mbplus.2022.100121_b0615","doi-asserted-by":"crossref","first-page":"1796","DOI":"10.1161\/01.ATV.0000141133.32496.41","article-title":"PECAM-1 interacts with nitric oxide synthase in human endothelial cells: implication for flow-induced nitric oxide synthase activation","volume":"24","author":"Dusserre","year":"2004","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"Pt 18","key":"10.1016\/j.mbplus.2022.100121_b0620","doi-asserted-by":"crossref","first-page":"4103","DOI":"10.1242\/jcs.02541","article-title":"Role of PECAM-1 in the shear-stress-induced activation of Akt and the endothelial nitric oxide synthase (eNOS) in endothelial cells","volume":"118","author":"Fleming","year":"2005","journal-title":"J. Cell. Sci."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0625","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1161\/01.RES.0000118600.91698.BB","article-title":"Comparative evaluation of FGF-2-, VEGF-A-, and VEGF-C-induced angiogenesis, lymphangiogenesis, vascular fenestrations, and permeability","volume":"94","author":"Cao","year":"2004","journal-title":"Circ. Res."},{"issue":"32","key":"10.1016\/j.mbplus.2022.100121_b0630","doi-asserted-by":"crossref","first-page":"23906","DOI":"10.1016\/S0021-9258(20)80471-2","article-title":"Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4","volume":"268","author":"Guimond","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0635","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1093\/glycob\/cwp031","article-title":"Specific inhibition of FGF-2 signaling with 2-O-sulfated octasaccharides of heparan sulfate","volume":"19","author":"Ashikari-Hada","year":"2009","journal-title":"Glycobiology"},{"issue":"26","key":"10.1016\/j.mbplus.2022.100121_b0640","doi-asserted-by":"crossref","first-page":"16451","DOI":"10.1074\/jbc.M114.627372","article-title":"Synergistic binding of vascular endothelial growth factor-a and its receptors to heparin selectively modulates complex affinity","volume":"290","author":"Teran","year":"2015","journal-title":"J. Biol. Chem."},{"issue":"385","key":"10.1016\/j.mbplus.2022.100121_b0645","doi-asserted-by":"crossref","first-page":"ra70","DOI":"10.1126\/scisignal.aaa0963","article-title":"The interaction of heparan sulfate proteoglycans with endothelial transglutaminase-2 limits VEGF165-induced angiogenesis","volume":"8","author":"Beckouche","year":"2015","journal-title":"Sci. Signal."},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0650","doi-asserted-by":"crossref","first-page":"00652-2021","DOI":"10.1183\/23120541.00652-2021","article-title":"Heparan sulfate mimetic fucoidan restores the endothelial glycocalyx and protects against dysfunction induced by serum of COVID-19 patients in the intensive care unit","volume":"8","author":"Yuan","year":"2022","journal-title":"ERJ Open Res."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0655","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1124\/jpet.116.239509","article-title":"Therapeutic restoration of endothelial glycocalyx in sepsis","volume":"361","author":"Song","year":"2017","journal-title":"J. Pharmacol. Exp. Ther."},{"issue":"53","key":"10.1016\/j.mbplus.2022.100121_b0660","doi-asserted-by":"crossref","first-page":"91350","DOI":"10.18632\/oncotarget.20518","article-title":"Sulodexide recovers endothelial function through reconstructing glycocalyx in the balloon-injury rat carotid artery model","volume":"8","author":"Li","year":"2017","journal-title":"Oncotarget"},{"issue":"12","key":"10.1016\/j.mbplus.2022.100121_b0665","doi-asserted-by":"crossref","first-page":"2646","DOI":"10.1007\/s00125-010-1910-x","article-title":"Effect of sulodexide on endothelial glycocalyx and vascular permeability in patients with type 2 diabetes mellitus","volume":"53","author":"Broekhuizen","year":"2010","journal-title":"Diabetologia"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0670","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/(SICI)1098-1128(199801)18:1<1::AID-MED1>3.0.CO;2-4","article-title":"Review of pharmacodynamics, pharmacokinetics, and therapeutic properties of sulodexide","volume":"18","author":"Harenberg","year":"1998","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.mbplus.2022.100121_b0675","doi-asserted-by":"crossref","first-page":"105","DOI":"10.2147\/JBM.S10558","article-title":"Use of sulodexide in patients with peripheral vascular disease","volume":"1","author":"Lasierra-Cirujeda","year":"2010","journal-title":"J. Blood Med."},{"key":"10.1016\/j.mbplus.2022.100121_b0680","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-3-030-34521-1_1","article-title":"Forty years of basic and translational heparanase research","volume":"1221","author":"Vlodavsky","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"issue":"07","key":"10.1016\/j.mbplus.2022.100121_b0685","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1055\/a-1414-5216","article-title":"Sulodexide in the treatment of patients with early stages of COVID-19: A randomized controlled trial","volume":"121","author":"Gonzalez-Ochoa","year":"2021","journal-title":"Thromb. Haemost."},{"issue":"4","key":"10.1016\/j.mbplus.2022.100121_b0690","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3390\/ph10020036","article-title":"Development of a glycosaminoglycan derived, selectin targeting anti-adhesive coating to treat endothelial cell dysfunction","volume":"10","author":"Wodicka","year":"2017","journal-title":"Pharmaceuticals (Basel)"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0695","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s12195-018-0555-6","article-title":"Selectin-targeting peptide-glycosaminoglycan conjugates modulate neutrophil-endothelial interactions","volume":"12","author":"Wodicka","year":"2019","journal-title":"Cell. Mol. Bioeng."},{"issue":"8","key":"10.1016\/j.mbplus.2022.100121_b0700","doi-asserted-by":"crossref","first-page":"e23530","DOI":"10.1371\/journal.pone.0023530","article-title":"Modulation of syndecan-1 shedding after hemorrhagic shock and resuscitation","volume":"6","author":"Haywood-Watson","year":"2011","journal-title":"PLoS ONE"},{"issue":"3","key":"10.1016\/j.mbplus.2022.100121_b0705","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1097\/SHK.0b013e31829f91fc","article-title":"Fresh frozen plasma lessens pulmonary endothelial inflammation and hyperpermeability after hemorrhagic shock and is associated with loss of syndecan 1","volume":"40","author":"Peng","year":"2013","journal-title":"Shock"},{"key":"10.1016\/j.mbplus.2022.100121_b0710","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/j.jss.2018.08.027","article-title":"Plasma ameliorates endothelial dysfunction in burn injury","volume":"233","author":"Vigiola Cruz","year":"2019","journal-title":"J. Surg. Res."},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0715","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1213\/ANE.0b013e318210385c","article-title":"Plasma restoration of endothelial glycocalyx in a rodent model of hemorrhagic shock","volume":"112","author":"Kozar","year":"2011","journal-title":"Anesth. Analg."},{"issue":"5","key":"10.1016\/j.mbplus.2022.100121_b0720","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1097\/TA.0b013e3182a92514","article-title":"Evaluation of resuscitation fluids on endothelial glycocalyx, venular blood flow, and coagulation function after hemorrhagic shock in rats","volume":"75","author":"Torres","year":"2013","journal-title":"J. Trauma Acute Care Surg."},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0725","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1097\/SHK.0000000000001432","article-title":"Antithrombin III contributes to the protective effects of fresh frozen plasma following hemorrhagic shock by preventing syndecan-1 shedding and endothelial barrier disruption","volume":"53","author":"Lopez","year":"2020","journal-title":"Shock"},{"issue":"6","key":"10.1016\/j.mbplus.2022.100121_b0730","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1097\/SHK.0000000000001207","article-title":"Fibrinogen protects against barrier dysfunction through maintaining cell surface syndecan-1 in vitro","volume":"51","author":"Wu","year":"2019","journal-title":"Shock"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0735","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1186\/s13613-020-00697-1","article-title":"Role of albumin in the preservation of endothelial glycocalyx integrity and the microcirculation: a review","volume":"10","author":"Aldecoa","year":"2020","journal-title":"Ann. Intensive Care"},{"key":"10.1016\/j.mbplus.2022.100121_b0740","doi-asserted-by":"crossref","unstructured":"Zeng, Y., Adamson, R.H., Curry, F.R., Tarbell, J.M., (2014). Sphingosine-1-phosphate protects endothelial glycocalyx by inhibiting syndecan-1 shedding. Am. J. Physiol. Heart Circ. Physiol., 306 (3), H363-372.","DOI":"10.1152\/ajpheart.00687.2013"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0745","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.yexcr.2015.08.013","article-title":"Sphingosine 1-phosphate induced synthesis of glycocalyx on endothelial cells","volume":"339","author":"Zeng","year":"2015","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.mbplus.2022.100121_b0750","doi-asserted-by":"crossref","unstructured":"Mensah, S.A., Cheng, M.J., Homayoni, H., Plouffe, B.D., Coury, A.J., Ebong, E.E., (2017). Regeneration of glycocalyx by heparan sulfate and sphingosine 1-phosphate restores inter-endothelial communication. PLoS One, 12 (10), e0186116.","DOI":"10.1371\/journal.pone.0186116"},{"key":"10.1016\/j.mbplus.2022.100121_b0755","doi-asserted-by":"crossref","unstructured":"Cancel, L.M., Tarbell, J.M., (2013). Rhamnan sulfate enhances the endothelial glycocalyx and decreases the LDL permeability of human coronary artery endothelial cells in vitro. FASEB J., 27 (S1), 896.893-896.893.","DOI":"10.1096\/fasebj.27.1_supplement.896.3"},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0760","article-title":"Dietary glycocalyx precursor supplementation ameliorates age-related vascular dysfunction","volume":"33","author":"Machin","year":"2019","journal-title":"FASEB J."},{"key":"10.1016\/j.mbplus.2022.100121_b0765","unstructured":"Dietary Interventions on Glycocalyx Dimensions in South Asian Patients With Diabetic Nephropathy. (Glycotreat). [cited 30\/09 2021] Available from: https:\/\/clinicaltrials.gov\/ct2\/show\/NCT03889236."},{"issue":"1","key":"10.1016\/j.mbplus.2022.100121_b0770","doi-asserted-by":"crossref","first-page":"e116","DOI":"10.1097\/AS9.0000000000000116","article-title":"Endotheliopathy is associated with a 24-hour Fibrinolysis phenotype described by low TEG lysis and High D-dimer after trauma: a secondary analysis of the PROPPR study","volume":"3","author":"Richter","year":"2022","journal-title":"Ann. Surg. Open"},{"issue":"2","key":"10.1016\/j.mbplus.2022.100121_b0775","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1083\/jcb.107.2.743","article-title":"Endothelial cell-derived heparan sulfate binds basic fibroblast growth factor and protects it from proteolytic degradation","volume":"107","author":"Saksela","year":"1988","journal-title":"J. Cell Biol."}],"container-title":["Matrix Biology Plus"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2590028522000217?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2590028522000217?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T01:09:59Z","timestamp":1762909799000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2590028522000217"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12]]},"references-count":155,"alternative-id":["S2590028522000217"],"URL":"https:\/\/doi.org\/10.1016\/j.mbplus.2022.100121","relation":{},"ISSN":["2590-0285"],"issn-type":[{"value":"2590-0285","type":"print"}],"subject":[],"published":{"date-parts":[[2022,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Alterations in heparan sulfate proteoglycan synthesis and sulfation and the impact on vascular endothelial function","name":"articletitle","label":"Article Title"},{"value":"Matrix Biology Plus","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mbplus.2022.100121","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"100121"}}