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dc.contributorChellan, Bijoy-
dc.contributorNarayani, Jayakumari-
dc.contributorAppukuttan, Padinjaradath S.-
dc.date.accessioned2012-12-04T11:44:10Z-
dc.date.available2012-12-04T11:44:10Z-
dc.date.issued2007-
dc.identifier.citationEXPERIMENTAL AND MOLECULAR PATHOLOGY. 83; 3; 399-404en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.yexmp.2007.04.004-
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/pubmed/17537433-
dc.identifier.urihttp://dspace.sctimst.ac.in/jspui/handle/123456789/531-
dc.description.abstractLipoprotein(a) [Lp(a)], a modified LDL molecule, is implicated in atherogenesis. Mechanisms of the accumulation of [Lp(a)] in atherosclerotic vessels is lacking in literature. We sought to investigate the complementarities of the carbohydrate structures on Lp(a) and LDL with galectin-1 (a carbohydrate binding protein) and whether endogenous galectin-1 binds Lp(a) in situ. We investigated T-antigen structures on Lp(a) and LDL by enzyme-linked lectin assay using T-antigen specific lectins, galectin-1 and jacalin. Both jacalin and galectin-1 bound strongly to Lp(a) and to a much lesser extent, to LDL. Galectin-1 recognition of the lipoproteins was abolished when the O-linked sugars were selectively removed. Localization of endogenous galectin-1 within histological sections of human internal mammary artery and in vitro binding of Lp(a) to the tissues was analyzed by immunohistochemical staining. The Lp(a)-binding pattern was found to overlap with the localization of galectin-1. The poor Lp (a)-binding on inhibiting tissue galectin-1 with lactose, suggested the binding of Lp(a) to galectin-1. This may be suggestive of a mechanism by which Lp(a) accumulates within arterial walls in atherogenesis. (c) 2007 Elsevier Inc. All rights reserved.-
dc.publisherEXPERIMENTAL AND MOLECULAR PATHOLOGY-
dc.subjectBiochemistry-
dc.titleGalectin-1, an endogenous lectin produced by arterial cells, binds lipoprotein(a) [Lp(a)] in situ: Relevance to atherogenesis-
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