{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T10:55:50Z","timestamp":1788260150475,"version":"build-2803163510"},"reference-count":60,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2020,2,2]],"date-time":"2020-02-02T00:00:00Z","timestamp":1580601600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2016\/50127-5; 2014\/26058-8; 2013\/07467-1"],"award-info":[{"award-number":["2016\/50127-5; 2014\/26058-8; 2013\/07467-1"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["303958\/2018-9; 308133\/2015-3"],"award-info":[{"award-number":["303958\/2018-9; 308133\/2015-3"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","award":["063\/2010 Toxinology, AUXPE 1209\/2011"],"award-info":[{"award-number":["063\/2010 Toxinology, AUXPE 1209\/2011"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Snake venom metalloproteinases (SVMPs) play an important role in local tissue damage of snakebite patients, mostly by hydrolysis of basement membrane (BM) components. We evaluated the proinflammatory activity of SVMPs Atroxlysin-Ia (ATXL) and Batroxrhagin (BATXH) from Bothrops atrox venom and their hydrolysis products of Matrigel. BALB\/c mice were injected with SVMPs (2 \u03bcg), for assessment of paw edema and peritoneal leukocyte accumulation. Both SVMPs induced edema, representing an increase of ~70% of the paw size. Leukocyte infiltrates reached levels of 6 \u00d7 106 with ATXL and 5 \u00d7 106 with BATXH. TNF-\u03b1 was identified in the supernatant of BATXH\u2014or venom-stimulated MPAC cells. Incubation of Matrigel with the SVMPs generated fragments, including peptides from Laminin, identified by LC\u2013MS\/MS. The Matrigel hydrolysis peptides caused edema that increased 30% the paw size and promoted leukocyte accumulation (4\u20135 \u00d7 106) to the peritoneal cavity, significantly higher than Matrigel control peptides 1 and 4 h after injection. Our findings suggest that ATXL and BATXH are involved in the inflammatory reaction observed in B. atrox envenomings by direct action on inflammatory cells or by releasing proinflammatory peptides from BM proteins that may amplify the direct action of SVMPs through activation of endogenous signaling pathways.<\/jats:p>","DOI":"10.3390\/toxins12020096","type":"journal-article","created":{"date-parts":[[2020,2,3]],"date-time":"2020-02-03T01:25:51Z","timestamp":1580693151000},"page":"96","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":31,"title":["Inflammatory Reaction Induced by Two Metalloproteinases Isolated from Bothrops atrox Venom and by Fragments Generated from the Hydrolysis of Basement Membrane Components"],"prefix":"10.3390","volume":"12","author":[{"given":"Michelle Teixeira de","family":"Almeida","sequence":"first","affiliation":[{"name":"Programa de P\u00f3s-Gradua\u00e7\u00e3o em Ci\u00eancias-Toxinologia, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"},{"name":"Laborat\u00f3rio de Imunopatologia, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4426-0731","authenticated-orcid":false,"given":"Luciana Aparecida","family":"Freitas-de-Sousa","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Imunopatologia, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monica","family":"Colombini","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Imunopatologia, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah N. C.","family":"Gimenes","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Imunopatologia, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eduardo S.","family":"Kitano","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signalig, CeTICS, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8083-4272","authenticated-orcid":false,"given":"Eliana L.","family":"Faquim-Mauro","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Imunopatologia, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Solange M. T.","family":"Serrano","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signalig, CeTICS, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1787-6634","authenticated-orcid":false,"given":"Ana Maria","family":"Moura-da-Silva","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Imunopatologia, Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,2,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Williams, D.J., Faiz, M.A., Abela-Ridder, B., Ainsworth, S., Bulfone, T.C., Nickerson, A.D., Habib, A.G., Junghanss, T., Fan, H.W., and Turner, M. (2019). Strategy for a globally coordinated response to a priority neglected tropical disease: Snakebite envenoming. PloS Negl. Trop. Dis., 13.","DOI":"10.1371\/journal.pntd.0007059"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1590\/S0074-02762005000900031","article-title":"Inflammatory effects of snake venom metalloproteinases","volume":"100","author":"Teixeira","year":"2005","journal-title":"Mem Inst. Oswaldo Cruz"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1080\/0962935021000051548","article-title":"Cell adhesion molecules involved in the leukocyte recruitment induced by venom of the snake Bothrops jararaca","volume":"11","author":"Zamuner","year":"2002","journal-title":"Mediat. Inflamm."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/j.jprot.2009.01.015","article-title":"Timeline of key events in snake venom metalloproteinase research","volume":"72","author":"Fox","year":"2009","journal-title":"J. Proteom."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/S0006-2952(00)00302-6","article-title":"Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake bothrops asper","volume":"60","author":"Escalante","year":"2000","journal-title":"Biochem. Pharm."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.toxicon.2005.06.019","article-title":"Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom","volume":"46","author":"Gay","year":"2005","journal-title":"Toxicon"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0003-9861(89)90350-0","article-title":"Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases","volume":"275","author":"Baramova","year":"1989","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1023\/A:1014465611487","article-title":"Importance of metalloproteinases and macrophages in viper snake envenomation-induced local inflammation","volume":"26","author":"Costa","year":"2002","journal-title":"Inflammation"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1016\/j.bbrc.2004.08.012","article-title":"Activation of alpha(M)beta(2)-mediated phagocytosis by HF3, a P-III class metalloproteinase isolated from the venom of Bothrops jararaca","volume":"322","author":"Silva","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_10","first-page":"245","article-title":"Blister formation and skin damage induced by BaP1, a haemorrhagic metalloproteinase from the venom of the snake Bothrops asper","volume":"79","author":"Rucavado","year":"1998","journal-title":"Int. J. Exp. Pathol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2000","DOI":"10.1002\/eji.1830260905","article-title":"Processing of pro-tumor necrosis factor-alpha by venom metalloproteinases: A hypothesis explaining local tissue damage following snake bite","volume":"26","author":"Laing","year":"1996","journal-title":"Eur. J. Immunol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1016\/S0041-0101(01)00131-3","article-title":"The effect of jararhagin, a metalloproteinase from Bothrops jararaca venom, on pro-inflammatory cytokines released by murine peritoneal adherent cells","volume":"39","author":"Clissa","year":"2001","journal-title":"Toxicon"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.toxicon.2006.02.001","article-title":"Importance of jararhagin disintegrin-like and cysteine-rich domains in the early events of local inflammatory response","volume":"47","author":"Clissa","year":"2006","journal-title":"Toxicon"},{"key":"ref_14","first-page":"637","article-title":"[Epidemiological and clinical aspects of snake bites in the municipalities of the state of Amazonas, Brazil]","volume":"32","author":"Sadahiro","year":"1999","journal-title":"Rev. Soc. Bras. Med. Trop."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.toxicon.2012.03.004","article-title":"Local inflammatory events induced by Bothrops atrox snake venom and the release of distinct classes of inflammatory mediators","volume":"60","author":"Moreira","year":"2012","journal-title":"Toxicon"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/j.molimm.2003.11.032","article-title":"The complement system is involved in acute inflammation but not in the hemorrhage produced by a Bothrops atrox snake venom low molecular mass proteinase","volume":"40","author":"Rodrigues","year":"2004","journal-title":"Mol. Immunol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.molimm.2017.03.008","article-title":"Immune cells and mediators involved in the inflammatory responses induced by a P-I metalloprotease and a phospholipase A","volume":"85","author":"Menaldo","year":"2017","journal-title":"Mol. Immunol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"22869","DOI":"10.1016\/S0021-9258(18)50027-2","article-title":"Purification, cloning, and molecular characterization of a high-molecular-weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family","volume":"267","author":"Paine","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.toxicon.2012.03.026","article-title":"Jararhagin, A hemorrhagic snake venom metalloproteinase from Bothrops jararaca","volume":"60","author":"Baldo","year":"2012","journal-title":"Toxicon"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Freitas-de-Sousa, L.A., Colombini, M., Lopes-Ferreira, M., Serrano, S.M.T., and Moura-da-Silva, A.M. (2017). Insights into the Mechanisms Involved in Strong Hemorrhage and Dermonecrosis Induced by Atroxlysin-Ia, a PI-Class Snake Venom Metalloproteinase. Toxins, 9.","DOI":"10.3390\/toxins9080239"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.biochi.2015.08.006","article-title":"Comparison of venoms from wild and long-term captive Bothrops atrox snakes and characterization of Batroxrhagin, the predominant class PIII metalloproteinase from the venom of this species","volume":"118","author":"Amazonas","year":"2015","journal-title":"Biochimie"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.abb.2010.01.010","article-title":"The novel metalloproteinase atroxlysin-I from Peruvian Bothrops atrox (Jerg\u00f3n) snake venom acts both on blood vessel ECM and platelets","volume":"496","author":"Sanchez","year":"2010","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.toxicon.2012.03.018","article-title":"Batroxase, a new metalloproteinase from B. atrox snake venom with strong fibrinolytic activity","volume":"60","author":"Cintra","year":"2012","journal-title":"Toxicon"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1016\/1357-2725(96)00042-8","article-title":"The laminins","volume":"28","author":"Malinda","year":"1996","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1007\/s00428-002-0678-x","article-title":"The effect of laminin and its peptide SIKVAV on a human salivary gland adenoid cystic carcinoma cell line","volume":"441","author":"Freitas","year":"2002","journal-title":"Virchows Arch."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"47904","DOI":"10.18632\/oncotarget.10062","article-title":"Laminin-111 peptide C16 regulates invadopodia activity of malignant cells through \u03b21 integrin, Src and ERK 1\/2","volume":"7","author":"Siqueira","year":"2016","journal-title":"Oncotarget"},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Rucavado, A., Nicolau, C.A., Escalante, T., Kim, J., Herrera, C., Guti\u00e9rrez, J.M., and Fox, J.W. (2016). Viperid Envenomation Wound Exudate Contributes to Increased Vascular Permeability via a DAMPs\/TLR-4 Mediated Pathway. Toxins, 8.","DOI":"10.3390\/toxins8120349"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.abb.2006.09.018","article-title":"Novel insights into capillary vessel basement membrane damage by snake venom hemorrhagic metalloproteinases: A biochemical and immunohistochemical study","volume":"455","author":"Escalante","year":"2006","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1021\/pr2006439","article-title":"Hemorrhagic activity of HF3, a snake venom metalloproteinase: Insights from the proteomic analysis of mouse skin and blood plasma","volume":"11","author":"Sherman","year":"2012","journal-title":"J. Proteome Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.peptides.2003.12.008","article-title":"The C-terminus of murine S100A9 inhibits hyperalgesia and edema induced by jararhagin","volume":"25","author":"Dale","year":"2004","journal-title":"Peptides"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1016\/j.molimm.2015.09.023","article-title":"Evaluation of the local inflammatory events induced by BpirMP, a metalloproteinase from Bothrops pirajai venom","volume":"68","author":"Bernardes","year":"2015","journal-title":"Mol. Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.toxicon.2015.06.006","article-title":"Mast cells and histamine play an important role in edema and leukocyte recruitment induced by Potamotrygon motoro stingray venom in mice","volume":"103","author":"Kimura","year":"2015","journal-title":"Toxicon"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1161\/ATVBAHA.110.207449","article-title":"Prostaglandins and inflammation","volume":"31","author":"Ricciotti","year":"2011","journal-title":"Arter. Thromb. Vasc. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.intimp.2015.06.001","article-title":"Inflammatory mediators involved in the paw edema and hyperalgesia induced by Batroxase, a metalloproteinase isolated from Bothrops atrox snake venom","volume":"28","author":"Menaldo","year":"2015","journal-title":"Int. Immunopharmacol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.toxicon.2006.01.009","article-title":"Inflammatory effects of BaP1 a metalloproteinase isolated from Bothrops asper snake venom: Leukocyte recruitment and release of cytokines","volume":"47","author":"Fernandes","year":"2006","journal-title":"Toxicon"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1080\/09629350020025728","article-title":"Bothrops asper snake venom and its metalloproteinase BaP-1 activate the complement system. Role in leucocyte recruitment","volume":"9","author":"Farsky","year":"2000","journal-title":"Mediat. Inflamm."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Preciado, L.M., Perea\u00f1ez, J.A., and Comer, J. (2019). Potential of Matrix Metalloproteinase Inhibitors for the Treatment of Local Tissue Damage Induced by a Type P-I Snake Venom Metalloproteinase. Toxins, 12.","DOI":"10.3390\/toxins12010008"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.biochi.2007.11.009","article-title":"Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases","volume":"90","author":"Ramos","year":"2008","journal-title":"Biochimie"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3915","DOI":"10.1016\/j.febslet.2008.10.034","article-title":"Activation of leukocyte rolling by the cysteine-rich domain and the hyper-variable region of HF3, a snake venom hemorrhagic metalloproteinase","volume":"582","author":"Menezes","year":"2008","journal-title":"Febs Lett."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.toxicon.2016.04.042","article-title":"The role of TLR2 in the acute inflammatory response induced by Bothrops atrox snake venom","volume":"118","author":"Moreira","year":"2016","journal-title":"Toxicon"},{"key":"ref_41","first-page":"81","article-title":"Neutrophil Extracellular Traps and Its Implications in Inflammation: An Overview","volume":"8","year":"2017","journal-title":"Front. Immunol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1080\/09629350220131980","article-title":"Increments in cytokines and matrix metalloproteinases in skeletal muscle after injection of tissue-damaging toxins from the venom of the snake Bothrops asper","volume":"11","author":"Rucavado","year":"2002","journal-title":"Mediat. Inflamm"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1055\/s-2003-39075","article-title":"Interleukin (IL)-6 mRNA expression is stimulated by insulin, isoproterenol, tumour necrosis factor alpha, growth hormone, and IL-6 in 3T3-L1 adipocytes","volume":"35","author":"Fasshauer","year":"2003","journal-title":"Horm. Metab. Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"a016295","DOI":"10.1101\/cshperspect.a016295","article-title":"IL-6 in inflammation, immunity, and disease","volume":"6","author":"Tanaka","year":"2014","journal-title":"Cold Spring Harb Perspect. Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.toxicon.2009.03.007","article-title":"Characterization of inflammatory reaction induced by neuwiedase, a P-I metalloproteinase isolated from Bothrops neuwiedi venom","volume":"54","author":"Lopes","year":"2009","journal-title":"Toxicon"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Guti\u00e9rrez, J.M., Escalante, T., Rucavado, A., Herrera, C., and Fox, J.W. (2016). A Comprehensive View of the Structural and Functional Alterations of Extracellular Matrix by Snake Venom Metalloproteinases (SVMPs): Novel Perspectives on the Pathophysiology of Envenoming. Toxins, 8.","DOI":"10.3390\/toxins8100304"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Baldo, C., Jamora, C., Yamanouye, N., Zorn, T.M., and Moura-da-Silva, A.M. (2010). Mechanisms of vascular damage by hemorrhagic snake venom metalloproteinases: Tissue distribution and in situ hydrolysis. PloS Negl. Trop. Dis., 4.","DOI":"10.1371\/journal.pntd.0000727"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.toxicon.2015.10.016","article-title":"Jararhagin disruption of endothelial cell anchorage is enhanced in collagen enriched matrices","volume":"108","author":"Baldo","year":"2015","journal-title":"Toxicon"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1096\/fj.05-4682rev","article-title":"Glycosaminoglycans and their proteoglycans: Host-associated molecular patterns for initiation and modulation of inflammation","volume":"20","author":"Taylor","year":"2006","journal-title":"Faseb. J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1038\/ni0905-861","article-title":"Heparan sulfate and inflammation","volume":"6","author":"Parish","year":"2005","journal-title":"Nat. Immunol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1369\/0022155417740880","article-title":"Danger-Associated Molecular Patterns Derived From the Extracellular Matrix Provide Temporal Control of Innate Immunity","volume":"66","author":"Frevert","year":"2018","journal-title":"J. Histochem. Cytochem."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Newton, K., and Dixit, V.M. (2012). Signaling in innate immunity and inflammation. Cold Spring Harb. Perspect. Biol., 4.","DOI":"10.1101\/cshperspect.a006049"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1681\/ASN.2014010117","article-title":"Beyond tissue injury-damage-associated molecular patterns, toll-like receptors, and inflammasomes also drive regeneration and fibrosis","volume":"25","author":"Anders","year":"2014","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1038\/nri2852","article-title":"The impact of the extracellular matrix on inflammation","volume":"10","author":"Sorokin","year":"2010","journal-title":"Nat. Rev. Immunol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1886","DOI":"10.1002\/pmic.200900758","article-title":"Matrigel: A complex protein mixture required for optimal growth of cell culture","volume":"10","author":"Hughes","year":"2010","journal-title":"Proteomics"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.semcancer.2005.05.004","article-title":"Matrigel: Basement membrane matrix with biological activity","volume":"15","author":"Kleinman","year":"2005","journal-title":"Semin. Cancer Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1007\/s10616-014-9727-y","article-title":"Proteome array identification of bioactive soluble proteins\/peptides in Matrigel: Relevance to stem cell responses","volume":"67","author":"Talbot","year":"2015","journal-title":"Cytotechnology"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Herrera, C., Mac\u00eado, J.K., Feoli, A., Escalante, T., Rucavado, A., Guti\u00e9rrez, J.M., and Fox, J.W. (2016). Muscle Tissue Damage Induced by the Venom of Bothrops asper: Identification of Early and Late Pathological Events through Proteomic Analysis. Plos Negl. Trop. Dis., 10.","DOI":"10.1371\/journal.pntd.0004599"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.toxicon.2016.08.017","article-title":"Involvement of mast cells and histamine in edema induced in mice by Scolopendra viridicornis centipede venom","volume":"121","author":"Kimura","year":"2016","journal-title":"Toxicon"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/12\/2\/96\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T08:53:55Z","timestamp":1760172835000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/12\/2\/96"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,2,2]]},"references-count":60,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2020,2]]}},"alternative-id":["toxins12020096"],"URL":"https:\/\/doi.org\/10.3390\/toxins12020096","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,2,2]]}}}