Alterations in CD45 glycosylation pattern accompanying different cell proliferation states.
CD45 is a leukocyte-specific transmembrane glycoprotein whose intracellular domain exhibits protein tyrosine phosphatase activity and plays a critical role in signal transduction. CD45 derived from stationary lymphocytes migrated faster in SDS-PAGE than that derived from exponentially growing cells. A change in N-linked saccharide structure other than the neuraminidase-sensitive terminal sialic acid portion was found to be responsible for the molecular size change in CD45. The differential glycosylation appeared to occur during late-stage posttranslational processing of CD45. We speculate that the N-glycosylation difference affects the interaction between CD45 and other factors involved in signal transduction leading to modulation of leukocyte proliferation.
Ohta
T
T
Department of Pathology, Roger Williams Medical/Cancer Center-Brown University, Providence, Rhode Island 02908.
Kitamura
K
K
Maizel
A L
AL
Takeda
A
A
D000581:Amidohydrolases / Q000494:pharmacology; D002455:Cell Division; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D017493:Leukocyte Common Antigens / Q000378:metabolism*; D009439:Neuraminidase / Q000494:pharmacology; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D011499:Protein Processing, Post-Translational
D017493:Leukocyte Common Antigens; D009439:Neuraminidase; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase