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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1999-3-11
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pubmed:databankReference |
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pubmed:abstractText |
Beta-adrenergic or cholinergic stimulation of the rat parotid gland was earlier shown to induce dephosphorylation of endogenous destrin- and cofilin-like proteins, which are phosphorylated in resting cells at Ser residues probably present near the N-terminals. The primary structures and phosphorylation sites were determined here. The rat destrin-like protein had a sequence 95% identical to the cDNA-derived sequence of porcine destrin. The rat cofilin-like protein was 98% identical to that of porcine cofilin. Each protein lacked the initiator Met and began with an acetylalanine residue followed by a Ser residue. The N-terminal peptides generated with endoproteinase Asp-N were isolated; they were each phosphorylated at Ser-2. Earlier work had shown that partial cleavage of the phosphorylated destrin- and cofilin-like proteins with cyanogen bromide provides unphosphorylated 16.7- and 18.3-kDa fragments, respectively. It was here confirmed that they contained all the Ser residues other than those present in the N-terminal peptides. From these observations, it was now concluded that the destrin- and cofilin-like proteins are rat parotid destrin and cofilin (non-muscle type), respectively, and that each protein is phosphorylated exclusively at Ser-2 in resting cells and dephosphorylated at this site in response to beta-adrenergic or cholinergic stimulation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
D
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actin Depolymerizing Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Destrin,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, beta,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cholinergic,
http://linkedlifedata.com/resource/pubmed/chemical/Salivary Proteins and Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/endoproteinase Asp-N
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0003-9969
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
955-67
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9877327-Actin Depolymerizing Factors,
pubmed-meshheading:9877327-Alanine,
pubmed-meshheading:9877327-Amino Acid Sequence,
pubmed-meshheading:9877327-Animals,
pubmed-meshheading:9877327-Carrier Proteins,
pubmed-meshheading:9877327-Cyanogen Bromide,
pubmed-meshheading:9877327-Cytoskeletal Proteins,
pubmed-meshheading:9877327-DNA, Complementary,
pubmed-meshheading:9877327-Destrin,
pubmed-meshheading:9877327-Endopeptidases,
pubmed-meshheading:9877327-Male,
pubmed-meshheading:9877327-Mass Spectrometry,
pubmed-meshheading:9877327-Metalloendopeptidases,
pubmed-meshheading:9877327-Methionine,
pubmed-meshheading:9877327-Microfilament Proteins,
pubmed-meshheading:9877327-Molecular Sequence Data,
pubmed-meshheading:9877327-Molecular Weight,
pubmed-meshheading:9877327-Parotid Gland,
pubmed-meshheading:9877327-Phosphorylation,
pubmed-meshheading:9877327-Rats,
pubmed-meshheading:9877327-Rats, Wistar,
pubmed-meshheading:9877327-Receptors, Adrenergic, beta,
pubmed-meshheading:9877327-Receptors, Cholinergic,
pubmed-meshheading:9877327-Salivary Proteins and Peptides,
pubmed-meshheading:9877327-Serine,
pubmed-meshheading:9877327-Swine
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pubmed:year |
1998
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pubmed:articleTitle |
Complete amino acid sequences and phosphorylation sites, determined by Edman degradation and mass spectrometry, of rat parotid 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,
Research Support, Non-U.S. Gov't
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