Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.5.1.52 (
PNGase F
)
1,527
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The biochemical nature and relative topographic localization of Ag determinants recognized on
CD45
molecular complex by mAb defining four distinct Ag specificities (conventional
CD45
, CD45R, 180 kDa and 220/205/190 kDa) have been investigated. These Ag specificities display a differential biochemical, cellular, and histochemical distributions and are important in the definition of CD4-positive complementary functional T cell subsets and/or distinct stages of thymic maturation. Protease treatment of either
CD45
-positive cells or purified
CD45
molecules revealed that both conventional
CD45
and 180-kDa (UCHL1 epitope) Ag specificities are defined by epitopes present on a protease-resistant domain which is internal to the protease-sensitive epitopes defining both CD45R and 220/205/190-kDa Ag specificities. In addition, it is shown that carbohydrate moieties are contributing to the epitopes recognized by both the anti-180-kDa UCHL1 and the anti-220/205/190-kDa mAb. Neuraminidase treatment, which cleaves sialic acids either from N- or O-linked oligosaccharides, abrogated the reactivity of both mAb. However,
N-glycanase
treatment, which selectively cleaves N-linked sugars, did not affect the recognition of these two epitopes. Thus, these results demonstrate that the Ag determinants recognized by the UCHL1 and the anti-220/205/190-kDa mAb, which are topographically unrelated, are associated with sialic acids from O-linked-type oligosaccharides, emphasizing the contribution of carbohydrates to the Ag heterogeneity of
CD45
molecular complex.
...
PMID:Biochemical nature and topographic localization of epitopes defining four distinct CD45 antigen specificities. Conventional CD45, CD45R, 180 kDa (UCHL1) and 220/205/190 kDa. 247 88
The serum-mannan binding protein (S-MBP) is a calcium-dependent C-type lectin specific for mannose and N-acetylglucosamine. S-MBP is known as a host defense factor involved in innate immunity, where the target ligands for S-MBP should be on the surface of exogenous microorganisms. In this study, we tried to find endogenous ligands for this endogenous lectin. Among the cells tested, only the lymphocytes from thymus of BALB/c mice expressed ligands for S-MBP on their surface, those from bone marrow, spleen, mesenteric lymph nodes and peripheral blood all being negative. Interestingly, among the thymocytes, only the immature thymocytes with the CD4+CD8+CD3low phenotype expressed ligands for S-MBP, and ligands for S-MBP decreased on their maturation. A major cell surface glycoprotein bearing S-MBP ligands was isolated and identified as CD45RO, which is a transmembrane protein with tyrosine phosphatase activity. Deglycosylation experiments with
N-glycanase
and endoglycosidase H indicated that the S-MBP ligands on thymic
CD45
are high mannose type or hybrid type N-linked oligosaccharides. This unique presentation of S-MBP ligands on this special
CD45
isoform suggested the possibility that the oligosaccharide portion of
CD45
on immature thymocytes is associated with the maturation, development or selection events of thymocytes.
...
PMID:A unique CD45 glycoform recognized by the serum mannan-binding protein in immature thymocytes. 861 14