Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The structural features of the adult rat hepatocyte (ARH) forms of cell-CAM 105, a Mr 105,000 cell adhesion molecule, were compared using a variety of immunochemical and biochemical techniques with altered forms of more basic pI present on two transplantable hepatocellular carcinomas (THC 1682c and THC AS-30D). Immunoprecipitation analysis with polyclonal (anti-gp 105-2) and monoclonal (MAb) antibodies specific for cell-CAM 105 (MAb 362.50) demonstrated that ARH and THC cell-CAM 105 were indistinguishable in several respects including: (a) binding to wheat germ agglutinin; (b) labeling with NaIO4/NaB3H4; (c) susceptibility to digestion with endoglycosidases (endoglycosidase H and F and peptide N-glycosidase F N-glycanase); (d) rate of turnover on the cell surface; and (e) differential resistance of upper and lower forms to trypsin digestion in the presence or absence of calcium. Digestion with Clostridium perfringens or Vibrio cholerae neuraminidase did not equalize pI but instead decreased the size and increased the pI of both ARH and THC cell-CAM 105. Comparison of two-dimensional tryptic peptide maps, however, revealed five unique peptides in the THC AS-30D map and one peptide in the THC 1682c map, peptides which were only apparent in maps of deglycosylated ARH cell-CAM 105. Based on these results, it was concluded that there were significant differences in the glycosylation of ARH and THC cell-CAM 105. Biosynthetic labeling with 32PO4 and 35SO4 showed that both ARH and THC molecules were phosphorylated but not sulfated. Comparison of 32P-labeled peptides produced by digestion with V-8 protease revealed significant differences in the phosphorylation of the upper and lower forms from ARH and showed that the pattern of phosphorylation on THC cell-CAM 105 most closely resembled ARH upper form. Pulse-chase analysis of ARH cell-CAM 105 further indicated that only a subpopulation of the molecules labeled with [35S]methionine were phosphorylated.
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PMID:Comparison of the structural characteristics of cell-CAM 105 from hepatocytes with those of an altered form expressed by rat transplantable hepatocellular carcinomas. 281 19

Glioma pathogenesis-related 1-like protein1 (GliPr1L1) was identified by liquid chromatography-tandem mass spectrometry analyses of proteins associated to bovine sperm lipid raft membrane domains. This protein belongs to the CAP superfamily including cysteine-rich secretory proteins, Antigen 5 and pathogenesis-related 1 protein. PCR analysis revealed that GliPr1L1 is expressed in testis and, at a much lower level, all along the epididymis. Western blotting showed a similar distribution of GliPr1L1 in testicular and epididymal tissue extracts. In the epididymal lumen, GliPr1L1 was associated with the maturing spermatozoa and epididymosomes all along the excurrent duct but was undetectable in the soluble fraction of epididymal fluid. The protein was detectable as multiple isoforms with a higher MW form in the testis and proximal caput. Treatments with PNGase F revealed that N-glycosylation was responsible of multiple bands detected on Western blots. These results suggest that the N-glycosylation moiety of GliPr1L1 is processed during the transit in the caput. Western blots demonstrated that GliPr1L1 was associated with the sperm plasma membrane preparation. GliPr1L1 is glycosyl phosphatidyl inositol (GPI) anchored to caput and cauda spermatozoa as demonstrated by the ability of phosphatidylinositol specific phospholipase C to release GliPr1L1 from intact sperm cells. Lipid raft membrane domains were separated from caput and cauda epididymal spermatozoa. GliPr1L1 was immunodetectable in the low buoyant density fractions where lipid rafts are distributed. GliPr1L1 was localized on sperm equatorial segment and neck. In vitro fertilization performed in presence of anti-GliPr1L1 showed that this protein is involved in sperm-zona pellucida interaction.
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PMID:Bovine sperm raft membrane associated Glioma Pathogenesis-Related 1-like protein 1 (GliPr1L1) is modified during the epididymal transit and is potentially involved in sperm binding to the zona pellucida. 2255 61