Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1 Pt 1
|
pubmed:dateCreated |
1993-8-26
|
pubmed:abstractText |
Gastric ezrin, a membrane-cytoskeletal linker with sequence homology to talin and erythrocyte band 4.1, has been associated with the remodeling of parietal cell apical membrane that occurs with adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase stimulation. Here we examine the interrelationship between parietal cell ezrin and Ca(2+)-dependent protease activity. Addition of Ca2+ to sonicated gastric gland preparations rendered a relatively selective proteolysis of the 80-kDa ezrin, accompanied by the appearance of a 55-kDa breakdown product. Ca(2+)-dependent proteolysis of ezrin was blocked by E64, a cysteine protease inhibitor, or calpastatin, indicating calpain as the responsible protease. Degradation of ezrin in intact gastric glands was achieved by varying extracellular [Ca2+] and [ionomycin]. Ezrin degradation in situ was rapid and relatively selective, although Ca(2+)-dependent degradation of some spectrin-like bands was also observed. The effect of activated calpain I on parietal cell function was assessed by probing the secretory response to histamine stimulation using [14C]aminopyrine uptake, along with parallel measurements of calpain activity, over a wide range of ionomycin. Activation of calpain, as evidenced by loss of parietal cell ezrin, was correlated with decreased AP uptake by stimulated gastric glands, supporting a role for ezrin in the oxyntic secretory process. The calpain-ezrin interaction established here, and the similarities of calpain with talin and erythrocyte band 4.1, suggest a common feature to this family of ezrin/band 4.1/talin proteins that have been implicated in membrane-cytoskeletal association.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/ezrin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0002-9513
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
265
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
C36-46
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:8393284-Animals,
pubmed-meshheading:8393284-Calcium,
pubmed-meshheading:8393284-Calpain,
pubmed-meshheading:8393284-Cytoskeletal Proteins,
pubmed-meshheading:8393284-Endopeptidases,
pubmed-meshheading:8393284-Osmolar Concentration,
pubmed-meshheading:8393284-Parietal Cells, Gastric,
pubmed-meshheading:8393284-Peptide Hydrolases,
pubmed-meshheading:8393284-Phosphoproteins,
pubmed-meshheading:8393284-Protons,
pubmed-meshheading:8393284-Rabbits,
pubmed-meshheading:8393284-Sonication,
pubmed-meshheading:8393284-Subcellular Fractions
|
pubmed:year |
1993
|
pubmed:articleTitle |
Ezrin-calpain I interactions in gastric parietal cells.
|
pubmed:affiliation |
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|