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Originally published In Press as doi:10.1074/jbc.M209075200 on October 16, 2002
J. Biol. Chem., Vol. 277, Issue 52, 50333-50340, December 27, 2002
The Protein-tyrosine Phosphatase CD45 Reaches the Cell Surface
via Golgi-dependent and -independent Pathways*
Troy A.
Baldwin and
Hanne L.
Ostergaard§
From the Department of Medical Microbiology and Immunology,
University of Alberta, Edmonton, Alberta T6G 2S2, Canada
CD45 is a receptor protein-tyrosine phosphatase
essential for T cell development and lymphocyte activation. It is
highly glycosylated, with multiple isoforms and glycoforms expressed on
the cell surface depending on the cell type and stage of
differentiation. Interestingly, we found two pools of newly synthesized
CD45 expressed on plasma membrane, one of which arrived by 5 min
after synthesis. The remaining pool of CD45 was fully glycosylated and
began to arrive at the cell surface at ~15 min. The rapidly expressed
population of CD45 possessed exclusively endoglycosidase H-sensitive
N-linked carbohydrate. Additionally, this rapidly expressed
pool of CD45 appeared on the cell surface in a brefeldin A
(BFA)-insensitive manner, suggesting that it reached the cell surface
independent of the Golgi complex. The remaining CD45 trafficked through
the Golgi complex, and transport proceeded via a BFA-sensitive
mechanism. These data suggest that CD45 is able to reach the cell
surface via two distinct routes. The first is a conventional
Golgi-dependent pathway that allows fully processed CD45 to
be expressed. The second utilizes an ill defined mechanism that is
independent of the Golgi, is BFA-resistant, and allows for the
expression of CD45 with immature carbohydrate on the cell surface.
*
This work was supported in part by an operating grant from
the Canadian Institutes of Health Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a studentship from the Alberta Heritage Foundation
for Medical Research.
§
Alberta Heritage Foundation for Medical Research Senior Scientist.
To whom correspondence should be addressed: Dept. of Medical Microbiology and Immunology, 6-70 HMRC, University of Alberta, Edmonton, Alberta T6G 2S2, Canada. Tel.: 780-492-7710; Fax:
780-492-9828; E-mail: hanne.ostergaard@ualberta.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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