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)

Specific antiserum of human red cells was prepared from rabbit anti-human red cell serum by absorption with red cells of horse, hog, dog and Japanese monkey. This antiserum proved specific for human red cells regardless of blood types ABO and MN as demonstrated by the hemagglutination test. Sialoglycoproteins were extracted with lithium diiodosalicylate and isolated through chromatographic procedures from human red cell membranes, and showed inhibitory activity for the specific antiserum as well as for anti-M and anti-N sera. The isolated glycoproteins corresponded to the sialoglycoproteins on the basis of SDS-PAG electrophoresis. The inhibitory activity of the sialoglycoproteins for the specific antiserum was lost after the substance was treated with sialidase for 24h. A moderate reduction of the inhibitory activity for anti-M and anti-N sera but not for the specific antiserum was seen after treatment for 1h. These results showed that the receptors for the species-specific antiserum were more resistant towards sialidase treatment.
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PMID:Species-specific glycoproteins of the human red cell membrane. 707 95

Spatial regulation is an important feature of signal specificity elicited by cytoplasmic tyrosine kinases of the Src family (SRC family protein tyrosine kinases [SFK]). Cholesterol-enriched membrane domains, such as caveolae, regulate association of SFK with the platelet-derived growth factor receptor (PDGFR), which is needed for kinase activation and mitogenic signaling. PAG, a ubiquitously expressed member of the transmembrane adaptor protein family, is known to negatively regulate SFK signaling though binding to Csk. We report that PAG modulates PDGFR levels in caveolae and SFK mitogenic signaling through a Csk-independent mechanism. Regulation of SFK mitogenic activity by PAG requires the first N-terminal 97 aa (PAG-N), which include the extracellular and transmembrane domains, palmitoylation sites, and a short cytoplasmic sequence. We also show that PAG-N increases ganglioside GM1 levels at the cell surface and, thus, displaces PDGFR from caveolae, a process that requires the ganglioside-specific sialidase Neu-3. In conclusion, PAG regulates PDGFR membrane partitioning and SFK mitogenic signaling by modulating GM1 levels within caveolae independently from Csk.
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PMID:The Csk-binding protein PAG regulates PDGF-induced Src mitogenic signaling via GM1. 1869 48