RGD Reference Report - Identification of annexin VI as a Ca2+-sensitive CRHSP-28-binding protein in pancreatic acinar cells. - Rat Genome Database

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Identification of annexin VI as a Ca2+-sensitive CRHSP-28-binding protein in pancreatic acinar cells.

Authors: Thomas, DD  Kaspar, KM  Taft, WB  Weng, N  Rodenkirch, LA  Groblewski, GE 
Citation: Thomas DD, etal., J Biol Chem 2002 Sep 20;277(38):35496-502.
RGD ID: 724802
Pubmed: PMID:12105190   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M110917200   (Journal Full-text)

CRHSP-28 is a member of the tumor protein D52 protein family that was recently shown to regulate Ca(2+)-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 Ca(2+)-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 Ca(2+), 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 Ca(2+)-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.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
secretion  TAS 724802 RGD 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
apical plasma membrane  IDA 724802 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
calcium-dependent phospholipid binding  IDA 724802 RGD 
calcium-dependent phospholipid binding  TAS 724802 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Anxa6  (annexin A6)


Additional Information