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J Biol Chem, Vol. 275, Issue 17, 12806-12812, April 28, 2000
From the To study potential roles of plasma
membrane-associated extracellular cathepsin B in tumor cell invasion
and metastasis, we used the yeast two-hybrid system to screen for
proteins that interact with human procathepsin B. The annexin II light
chain (p11), one of the two subunits of the annexin II tetramer, was
one of the proteins identified. We have confirmed that recombinant
human procathepsin B interacts with p11 as well as with the annexin II
tetramer in vitro. Furthermore, procathepsin B could
interact with the annexin II tetramer in vivo as
demonstrated by coimmunoprecipitation. Cathepsin B and the annexin II
tetramer were shown by immunofluorescent staining to colocalize on the
surface of human breast carcinoma and glioma cells. Taken together, our
results indicate that the annexin II tetramer can serve as a binding
protein for procathepsin B on the surface of tumor cells, an
interaction that may facilitate tumor invasion and metastasis.
Human Procathepsin B Interacts with the Annexin II Tetramer on
the Surface of Tumor Cells*
,
, and¶**
Department of Pharmacology,
§ Center for Molecular Medicine and Genetics and
¶ Barbara Ann Karmanos Cancer Institute, Wayne State University,
School of Medicine, Detroit, Michigan 48201 and Cancer Biology
Research Group, Department of Biochemistry and Molecular Biology,
University of Calgary, Calgary, Alberta, Canada T2N 4N1
*
This work was supported by United States Public Health
Service Grants CA36481 and CA56586. The Zeiss LSM-310 confocal
microscope was supported in part by National Institutes of Health
Grants P30ES06639 (NIEHS) and P30CA22453 (NCI).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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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