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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-9-9
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pubmed:abstractText |
Both keratohyalin granules (KHG) and cornified envelopes were stained histochemically in an indirect immunofluorescent study by antiphosphorylated cystatin alpha antibody, indicating that phosphorylated cystatin alpha is a component of the cornified envelope proteins. When phosphorylated cystatin alpha (P-cystatin alpha) was incubated with epidermal transglutaminase (TGase) and Ca2+ ions, polymerized protein was produced by formation of epsilon-(gamma-glutamyl)lysine cross-linking peptide bonds between lysine residues of cystatin alpha and glutamine residues of suitable protein(s) in the enzyme preparation. However, phosphorylated and non-phosphorylated cystatins were polymerized to similar extents by the TGase. Immunofluorescent and immunoelectron microscopic observations revealed that P-cystatin alpha could be detected in vivo in the KHG and cornified envelopes. Treatment of sphingosine, a specific inhibitor of protein kinase C, markedly suppressed the incorporation of cystatin alpha into KHG. Thus phosphorylation of cystatin alpha by protein kinase C may play an important role in targeting cystatin alpha into KHG.
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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/Csta protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cystatins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingosine,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
308
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
79-82
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1353732-Animals,
pubmed-meshheading:1353732-Cystatins,
pubmed-meshheading:1353732-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1353732-Epidermis,
pubmed-meshheading:1353732-Microscopy, Fluorescence,
pubmed-meshheading:1353732-Microscopy, Immunoelectron,
pubmed-meshheading:1353732-Phosphorylation,
pubmed-meshheading:1353732-Protein Kinase C,
pubmed-meshheading:1353732-Rats,
pubmed-meshheading:1353732-Skin,
pubmed-meshheading:1353732-Skin Physiological Phenomena,
pubmed-meshheading:1353732-Sphingosine,
pubmed-meshheading:1353732-Substrate Specificity,
pubmed-meshheading:1353732-Transglutaminases
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pubmed:year |
1992
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pubmed:articleTitle |
Phosphorylated cystatin alpha is a natural substrate of epidermal transglutaminase for formation of skin cornified envelope.
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pubmed:affiliation |
Department of Dermatology, Kinki University School of Medicine, Osaka, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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