Please use this identifier to cite or link to this item: http://dspace.sctimst.ac.in/jspui/handle/123456789/531
Title: Galectin-1, an endogenous lectin produced by arterial cells, binds lipoprotein(a) [Lp(a)] in situ: Relevance to atherogenesis
Authors: Chellan, Bijoy
Narayani, Jayakumari
Appukuttan, Padinjaradath S.
Keywords: Biochemistry
Issue Date: 2007
Publisher: EXPERIMENTAL AND MOLECULAR PATHOLOGY
Citation: EXPERIMENTAL AND MOLECULAR PATHOLOGY. 83; 3; 399-404
Abstract: Lipoprotein(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.
URI: http://dx.doi.org/10.1016/j.yexmp.2007.04.004
http://www.ncbi.nlm.nih.gov/pubmed/17537433
http://dspace.sctimst.ac.in/jspui/handle/123456789/531
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