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J. Biol. Chem., Vol. 277, Issue 38, 35496-35502, September 20, 2002
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From the Department of Nutritional Sciences, University of
Wisconsin, Madison, Wisconsin 53706
CRHSP-28 is a member of the tumor protein D52
protein family that was recently shown to regulate
Ca2+-stimulated secretory activity in
streptolysin-O-permeabilized acinar cells (Thomas, D. H., Taft,
W. B., Kaspar, K. M., and Groblewski, G. E. (2001)
J. Biol. Chem. 276, 28866-28872). In the present study, the Ca2+-sensitive phospholipid-binding protein
annexin VI was purified from rat pancreas as a CRHSP-28-binding
protein. The interaction between CRHSP-28 and annexin VI was
demonstrated by coimmunoprecipitation and gel-overlay assays and was
shown to require low micromolar levels of free Ca2+,
indicating these molecules likely interact under physiological conditions. Immunofluorescence microscopy confirmed a dual localization of CRHSP-28 and annexin VI, which appeared in a punctate pattern in the
supranuclear and apical cytoplasm of acini. Stimulation of cells for 5 min with the secretagogue cholecystokinin enhanced the colocalization
of CRHSP-28 and annexin VI within regions of acini immediately below
the apical plasma membrane. Tissue fractionation revealed that CRHSP-28
is a peripheral membrane protein that is highly enriched in smooth
microsomal fractions of pancreas. Further, the content of CRHSP-28 in
microsomes was significantly reduced in pancreatic tissue obtained from
rats that had been infused with a secretory dose of cholecystokinin for
40 min, demonstrating that secretagogue stimulation transiently alters
the association of CRHSP-28 with membranes in cells. Collectively, the
Ca2+-dependent binding of CRHSP-28 and annexin
VI, together with their colocalization in the apical cytoplasm, is
consistent with a role for these molecules in acinar cell
membrane trafficking events that are essential for digestive enzyme secretion.
Identification of Annexin VI as a Ca2+-sensitive
CRHSP-28-binding Protein in Pancreatic Acinar Cells*
*
This work was supported by Grants WISO4221 and WIS04444 from
the United States Department of Agriculture Cooperative State Research
Education and Extension Service Program, by American Cancer Society
Institutional Research Grant IRG-58-011-42-2, and by National Science
Foundation Award MCB-0094154 (to G. E. G.).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.
To whom correspondence should be addressed: Dept. of Nutritional
Sciences, University of Wisconsin, 1415 Linden Dr., Madison, WI
53706. Tel.: 608-262-0884; Fax: 608-262-5860; E-mail: groby@ nutrisci.wisc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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