{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T12:01:14Z","timestamp":1773662474282,"version":"3.50.1"},"reference-count":69,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["ATVB"],"published-print":{"date-parts":[[1998,4]]},"abstract":"<jats:p>\n            <jats:italic>Abstract<\/jats:italic>\n            \u2014Macrophage binding sites for oxidized LDL (Ox-LDL) include class A scavenger receptors (SR-As), the CD-36 molecule, and an additional but hitherto unidentified binding site. Because cell-surface glycosaminoglycans (GAGs) were previously shown to be involved in the cellular uptake of native LDL and lipoprotein(a), several strategies to assess the participation of heparan sulfate (HS) and chondroitin sulfate (CS) in macrophage catabolism of Ox-LDL were used. First, incubation of J-774 A.1 macrophage-like cells with either heparinase or chondroitinase, or with both enzymes together, reduced the binding, uptake, and degradation of\n            <jats:sup>125<\/jats:sup>\n            I\u2013Ox-LDL by 20% to 45%, in comparison with control nontreated cells, while catabolism of\n            <jats:sup>125<\/jats:sup>\n            I-labeled acetylated LDL (Ac-LDL) and native LDL were unaffected. Second, the proteoglycan (PG) cellular content was increased by cell enrichment with exogenous GAGs or by using human monocyte-derived macrophages from two patients with Sanfilippo mucopolysaccharidosis, which are characterized by cellular HS accumulation. In these macrophages, cellular uptake of\n            <jats:sup>125<\/jats:sup>\n            I\u2013Ox-LDL increased, while catabolism of\n            <jats:sup>125<\/jats:sup>\n            I\u2013Ac-LDL and native LDL were unaffected. Experiments using conditioned media from control, heparinase-digested, or chondroitinase-digested macrophages indicated that neither secreted GAGs nor released digestion products played any role in Ox-LDL catabolism. To evaluate potential interactions between cell-surface GAGs and known receptors for Ox-LDL, we used excess unlabeled Ac-LDL to block SR-As or anti\u2013CD-36 antibodies to block CD-36, and then examined the catabolism of\n            <jats:sup>125<\/jats:sup>\n            I\u2013Ox-LDL by GAG-enriched or -depleted macrophages. Both excess unlabeled Ac-LDL and anti\u2013CD-36 antibodies reduced\n            <jats:sup>125<\/jats:sup>\n            I\u2013Ox-LDL catabolism, but only excess unlabeled Ac-LDL completely abolished the increase in\n            <jats:sup>125<\/jats:sup>\n            I\u2013Ox-LDL catabolism on GAG enrichment of the cells, indicating a cooperation between exogenous GAGs and cell-surface SR-As in the catabolism of OX-LDL. Moreover, the addition of GAGases to macrophages that were preincubated with anti\u2013CD-36 antibodies and excess Ac-LDL further reduced macrophage degradation of Ox-LDL in comparison with cells that were pretreated only with anti\u2013CD-36 antibodies and Ac-LDL, indicating a more complex role for endogenous GAGs. Overall, these studies demonstrate a substantial contribution of macrophage-associated GAGs in the catabolism of Ox-LDL, which is mediated in part by a cooperation between GAGs and cell-surface SR-As.\n          <\/jats:p>","DOI":"10.1161\/01.atv.18.4.542","type":"journal-article","created":{"date-parts":[[2011,6,17]],"date-time":"2011-06-17T19:44:19Z","timestamp":1308339859000},"page":"542-553","source":"Crossref","is-referenced-by-count":25,"title":["Role of Macrophage Glycosaminoglycans in the Cellular Catabolism of Oxidized LDL by Macrophages"],"prefix":"10.1161","volume":"18","author":[{"given":"Marielle","family":"Kaplan","sequence":"first","affiliation":[{"name":"From the Lipid Research Laboratory, The Bruce Rappaport Faculty of Medicine, Technion, the Rappaport Family Institute for Research in the Medical Sciences, and Rambam Medical Center, Haifa, Israel (M.K., H.M., M.A.); and the Dorrance Hamilton Research Laboratories, Division of Endocrinology, Diabetes &amp; Metabolic Diseases, Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, Pa (K.J.W.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kevin Jon","family":"Williams","sequence":"additional","affiliation":[{"name":"From the Lipid Research Laboratory, The Bruce Rappaport Faculty of Medicine, Technion, the Rappaport Family Institute for Research in the Medical Sciences, and Rambam Medical Center, Haifa, Israel (M.K., H.M., M.A.); and the Dorrance Hamilton Research Laboratories, Division of Endocrinology, Diabetes &amp; Metabolic Diseases, Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, Pa (K.J.W.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hanna","family":"Mandel","sequence":"additional","affiliation":[{"name":"From the Lipid Research Laboratory, The Bruce Rappaport Faculty of Medicine, Technion, the Rappaport Family Institute for Research in the Medical Sciences, and Rambam Medical Center, Haifa, Israel (M.K., H.M., M.A.); and the Dorrance Hamilton Research Laboratories, Division of Endocrinology, Diabetes &amp; Metabolic Diseases, Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, Pa (K.J.W.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Aviram","sequence":"additional","affiliation":[{"name":"From the Lipid Research Laboratory, The Bruce Rappaport Faculty of Medicine, Technion, the Rappaport Family Institute for Research in the Medical Sciences, and Rambam Medical Center, Haifa, Israel (M.K., H.M., M.A.); and the Dorrance Hamilton Research Laboratories, Division of Endocrinology, Diabetes &amp; Metabolic Diseases, Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, Pa (K.J.W.)."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"276","reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI114271"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.86.4.1372"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.82.9.3000"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI115932"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1161\/atvb.15.9.1378"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/S0022-2275(20)41507-X","volume":"33","year":"1992","journal-title":"J Lipid Res"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.52.070183.001255"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.81.12.3883"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.ATV.7.2.135"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/0021-9150(93)90217-I"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM198904063201407"},{"key":"e_1_3_2_12_2","first-page":"599","volume":"34","year":"1936","journal-title":"Eur J Clin Chem Clin Biochem"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.78.10.6499"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(91)91378-P"},{"key":"e_1_3_2_15_2","first-page":"149","volume":"3","year":"1983","journal-title":"Atherosclerosis"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)81655-1"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1038\/343531a0"},{"key":"e_1_3_2_18_2","doi-asserted-by":"crossref","first-page":"11811","DOI":"10.1016\/S0021-9258(19)50272-1","volume":"268","year":"1993","journal-title":"J Biol Chem"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.27.16221"},{"key":"e_1_3_2_20_2","first-page":"11738","volume":"271","year":"1996","journal-title":"J Biol Chem"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI116081"},{"key":"e_1_3_2_22_2","doi-asserted-by":"crossref","first-page":"10160","DOI":"10.1016\/S0021-9258(18)82186-X","volume":"268","year":"1993","journal-title":"J Biol Chem"},{"key":"e_1_3_2_23_2","doi-asserted-by":"crossref","first-page":"13284","DOI":"10.1016\/S0021-9258(18)42208-9","volume":"267","year":"1992","journal-title":"J Biol Chem"},{"key":"e_1_3_2_24_2","doi-asserted-by":"crossref","first-page":"2764","DOI":"10.1016\/S0021-9258(17)42009-6","volume":"269","year":"1994","journal-title":"J Biol Chem"},{"key":"e_1_3_2_25_2","unstructured":"Fuki IV Kuhn KM Lomazov IR Williams KJ. 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