|Author||Chellan, Bijoy ♦ Narayani, Jayakumari ♦ Appukuttan, P. S.|
|Source||Sree Chitra Tirunal Institute for Medical Sciences & Technology|
|Publisher||Experimental and Molecular Pathology|
|Subject Domain (in DDC)||Natural sciences & mathematics ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Technology ♦ Medicine & health|
|Subject Domain (in MeSH)||Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Circulatory and Respiratory Physiological Phenomena ♦ Biological Sciences|
|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.|
|Education Level||UG and PG|
|Learning Resource Type||Article|
|Educational Framework||Medical Council of India (MCI)|
|Journal||EXPERIMENTAL AND MOLECULAR PATHOLOGY|
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