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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
1995-5-15
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pubmed:abstractText |
We previously reported that when 32Pi-loaded rat parotid slices are incubated with the beta-adrenergic agonist isoproterenol, the level of a soluble 32P-labeled 17-kDa protein (pp17) decreases rapidly (Kanamori, T., and Hayakawa, T. (1982) Biochem. Int. 4, 517-523). Here we show that pp17 consists of two distinct phosphoproteins (pp17a and pp17b), identify their unphosphorylated forms (p17a and p17b, respectively), and provide evidence for their beta-adrenergic stimulation-induced dephosphorylation. Since p17a and p17b were predominant forms even in nonstimulated cells, peptides were generated from them with Staphylococcus aureus V8 protease or cyanogen bromide; subsequent sequencing of these peptides and homology search allowed identification of p17a and p17b as destrin- and cofilin-like proteins, respectively. Interestingly, they were also dephosphorylated in response to cholinergic stimulation. Because destrin and cofilin are actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation, the two parotid proteins reported here might be involved in cortical F-actin disruption observed in parallel with exocytotic amylase secretion.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actin Depolymerizing Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Amylases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Destrin,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, beta
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8061-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7536193-Actin Depolymerizing Factors,
pubmed-meshheading:7536193-Amino Acid Sequence,
pubmed-meshheading:7536193-Amylases,
pubmed-meshheading:7536193-Animals,
pubmed-meshheading:7536193-Carrier Proteins,
pubmed-meshheading:7536193-Cytoskeletal Proteins,
pubmed-meshheading:7536193-Destrin,
pubmed-meshheading:7536193-Microfilament Proteins,
pubmed-meshheading:7536193-Molecular Sequence Data,
pubmed-meshheading:7536193-Nerve Tissue Proteins,
pubmed-meshheading:7536193-Parotid Gland,
pubmed-meshheading:7536193-Phosphoproteins,
pubmed-meshheading:7536193-Phosphorylation,
pubmed-meshheading:7536193-Rats,
pubmed-meshheading:7536193-Receptors, Adrenergic, beta,
pubmed-meshheading:7536193-Sequence Alignment
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pubmed:year |
1995
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pubmed:articleTitle |
Identification of two 17-kDa rat parotid gland phosphoproteins, subjects for dephosphorylation upon beta-adrenergic stimulation, as destrin- and cofilin-like proteins.
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pubmed:affiliation |
Department of Biochemistry, School of Dentistry, Aichi-Gakuin University, Nagoya, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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