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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
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The Protein-tyrosine Phosphatase CD45 Reaches the Cell Surface via Golgi-dependent and -independent Pathways*

Troy A. BaldwinDagger 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.

Dagger 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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