High impact information on LOC414915

• Galectin-4 is therefore secreted by a nonclassical pathway, and the brush border enzymes represent a novel class of natural ligands for a member of the galectin family [1].
• This region shares structural features with sugar binding sites of known lectin structures of the leguminous and galectin families [2].
• The detection of galectin-1 (gal-1) in pig granulosa cell lysates by immunoblotting and its cytosolic as well as membrane-associated localization prompted us to study its effects on cell proliferation and regulation of progesterone synthesis [3].
• In the presence of 30 mM lactose, the gal-1-reduced P450(SCC) expression was prevented [3].
• Strongly reduced mRNA levels were recorded for P450(SCC) and 3beta-hydroxysteroid dehydrogenase/isomerase (3beta-HSD) when FSH-stimulated granulosa cells were cultured in the presence of gal-1 [3].

Biological context of LOC414915

• The amino-terminal domain of hamster galectin 3, which is a repetitive sequence rich in glutamine, tyrosine, glycine and proline, is also an excellent substrate [4].
• One of the primary galectins expressed in intestinal epithelium is galectin-4, a tandem-repeat galectin with two carbohydrate-recognition domains in a single polypeptide chain [5].
• Activation of oxidative burst and degranulation of porcine neutrophils by a homologous spleen galectin-1 compared to N-formyl-L-methionyl-L-leucyl-L-phenylalanine and phorbol 12-myristate 13-acetate [6].

Anatomical context of LOC414915

• Effects of galectin-1 on regulation of progesterone production in granulosa cells from pig ovaries in vitro [3].
• Transglutaminase-mediated cross-linking of galectin 3 to itself or to matrix components may be one mechanism for stabilisation of a multivalent binding form of the lectin in cell secretions or in extracellular matrices [4].
• We have extended our previous studies on a porcine spleen galectin-1 in relation to its functional roles such as polymorphonuclear neutrophils (PMNs) stimulation compared to well known PMN activators e.g. N-formyl-L-methionyl-L leucyl-L-phenylalanine (fMLP) and phorbol 12-myristate 13-acetate (PMA) [6].

Associations of LOC414915 with chemical compounds

• Cross-linking of galectin 3, a galactose-binding protein of mammalian cells, by tissue-type transglutaminase [4].
• These galectin-like glycoproteins (binding probably via the N-acetyllactosamine sequences to laminin) could also be detected by labelled F-actin in protein blots [7].

References