Galectin-1, an endogenous lectin produced by arterial cells, binds lipoprotein(a) [Lp(a)] in situ: relevance to atherogenesis

Exp Mol Pathol. 2007 Dec;83(3):399-404. doi: 10.1016/j.yexmp.2007.04.004. Epub 2007 May 3.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Viral, Tumor / chemistry
  • Antigens, Viral, Tumor / metabolism
  • Atherosclerosis*
  • Galectin 1 / genetics
  • Galectin 1 / metabolism*
  • Humans
  • Lipoprotein(a) / metabolism*
  • Lipoproteins, LDL / metabolism
  • Mammary Arteries / cytology*
  • Mammary Arteries / metabolism
  • Plant Lectins / metabolism
  • Protein Binding

Substances

  • Antigens, Viral, Tumor
  • Galectin 1
  • LGALS1 protein, human
  • Lipoprotein(a)
  • Lipoproteins, LDL
  • Plant Lectins
  • jacalin