Proteins mucin-like glycoproteins

Selectins are transmembrane proteins with membrane-distal Ca +-dependent lectin domains. This family of cell adhesion molecules is involved in the tethering and rolling of leukocytes on the blood vessel endothelium. Nicholson and colleagues [10] published the analysis of leukocyte selectin, CD62L, binding to the mucin-like glycoprotein, Gly-CAM-1. 

Gems, D.H. and Maizels, R.M. (1996) An abundantly expressed mucin-like protein from Toxocara canis infective larvae the precursor of the larval surface coat glycoproteins. Proceedings of the National Academy of Sciences USA 93,1665-1670. 

KIM-1 is a type I cell membrane glycoprotein which contains, in its extracellular portion, a six-cysteine immunoglobulin-like domain, two N-glycosylation sites, and a T/SP-rich domain characteristic of mucin-like O-glycosylated proteins. The ectodomain of KlM-1 is shed from cells in vitro and in vivo into the urine in rodents and humans after proximal tubular kidney injury or in patients with renal cell carcinoma. KlM-1 confers on epithelial cells the ability to recognize and phagocytose dead cells that are present in the postischemic kidney and contribute to the obstmction of the tubule lumen that characterizes acute kidney injiuy. In... 

The reaction of partially purified, lima-bean lectin with hog gastric-mucin type A substance exemplified the precipitin-like curve obtained for lectin-polysaccharide or -glycoprotein reactions.103 Classical precipitin-curves between purified components II and III and type A blood-group substance were also obtained.151,199 Maximal precipitation of component II (equivalence) occurred at a lower ratio of A substance per mole of protein than for component III. Under conditions where type A substance precipitated 90% of the lectin, types A2 and B precipitated151,199 66 and 13%, respectively, of component II, and 21 and 0% of component III. Neither of the lima-bean lectins precipitated with type O blood-group substance. 

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