Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.53 (sialidase)
 2,694 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mucin-specific lectin from Sambucus sieboldiana (SSA-M) reacts in Western blotting and ELISA with mucins from porcine stomach, bovine and ovine submaxillary glands, the human milk fat globule membrane, in vitro human ovarian, breast and colonic tumor cell lines, and mucins produced in vivo in the ascites of patients with endometrial and ovarian tumors, but not with fetal bovine fetuin or human transferrin. Sialidase treatment of these mucins led to an increase in the binding of SSA-M, suggesting that sialic acid is not part of the binding site for this lectin. Furthermore, sialic acid did not inhibit lectin binding. Treatment of asialomucin with O-glycanase decreased the binding of SSA-M, confirming the reactivity of the lectin with an O-linked carbohydrate. Treatment of mucins with trifluoromethanesulfonic acid, which removes all but core carbohydrate, led to an increase in the binding of SSA-M, suggesting that the lectin reacts with O-linked core glycans. Indeed, the increased reactivity after sialidase treatment of ovine submaxillary mucin suggests the lectin reacts with peptide-linked N-acetylgalactosamine (GalNAc), since more than 98% of the glycan chains attached to this mucin are sialylated GalNAc. The binding of SSA-M to sialidase-treated porcine mucin was inhibited strongly by GalNAc and disaccharides containing galactose (lactose, melibiose, and N-acetyllactosamine) but not by free galactose (Gal), suggesting that the glycan for optimum binding is Gal beta(1-3)GalNAc. This pattern of inhibition was different to other core glycan-reactive lectins tested, indicating that SSA-M is distinct, and should be of use in the isolation and characterisation of mucins and O-linked glycans.
 ...
PMID:Reactivity of mucin-specific lectin from Sambucus sieboldiana with simple sugars, normal mucins and tumor-associated mucins. Comparison with other lectins. 166 64

A new sialic acid-specific lectin from the colonic parasite of squirrel monkeys Tritrichomonas mobilensis (TML) was tested on human and mouse tissues for histochemical staining properties. There were no substantial differences in reactivity between frozen and formalin fixed paraffin sections. TML staining was blocked by preincubation with sialic acid or by sialidase digestion. TML/anti-TML antibody histochemistry was identical with the TML-gold technique. The staining pattern was not blood group dependent. TML stained strongly the luminal membranes of normal vascular endothelium as well as endothelial neoplasms. Lymphatic vessels and capillaries of kidney glomeruli and lung alveolar septi were negative or only slightly positive. In parenchymatous organs luminal membrane positivity was dominant, preferably of cells lining ducts. Weak fine-granular cytoplasmic and basolateral membrane staining was also observed. Umbrella cells in transitional epithelium and basal layers of squamous epithelia showed strong reactivity with cell membranes. Mucin in respiratory epithelium was positive whereas gastrointestinal mucins failed to stain uniformly. Erythrocytes and most white blood cell types showed distinct membrane positivity. Acetylation or alkaline O-deacetylation of tissue sections did not substantially change TML reactivity. Oxidation, however, completely blocked TML staining except for respiratory epithelium and colonic mucin.
 ...
PMID:Histochemical localization of sialylated glycoconjugates with Tritrichomonas mobilensis lectin (TLM). 883 52