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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1994-4-15
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pubmed:abstractText |
Lysine-rich phosphorylated cystatin alpha (P-cystatin alpha) from newborn rat epidermis is a good substrate for epidermal transglutaminase (TGase) and also one of the component proteins of cornified envelope in the stratum corneum. Since the filaggrin linker segment peptide was efficiently conjugated with P-cystatin alpha and was mediated by epidermal TGase in the presence of Ca2+ ions, filaggrin is a candidate for the glutamine-rich linkage protein to conjugate with lysine-rich P-cystatin alpha. A conjugated protein was found by epidermal TGase in the activated condition with Ca2+ ions and dithiothreitol. In contrast, the conjugated protein was not formed under chelated conditions with EDTA. The conjugated protein reacted positively with anti-P-cystatin alpha polyclonal antibody (PoAb). The conjugated protein and purified cornified envelope showed an inhibitory effect against papain and cathepsin L, but cathepsin B and H were not inhibited by these P-cystatin alpha conjugates. Although the component protein, P-cystatin alpha itself, inhibited cathepsin H strongly, these conjugated proteins inhibited specifically the cathepsin L family. The amino acid composition of cornified envelope protein and the conjugated protein of P-cystatin alpha and filaggrin linker segment peptide was not completely the same. The conjugated protein of P-cystatin alpha and filaggrin linker segment peptide showed the same inhibitory properties against cysteine proteinases as the cornified envelope. These findings suggest that the linkage protein between P-cystatin alpha and filaggrin linker segment peptide may be considered a model of cornified envelope, although skin cornified envelope may be conjugated with some additional proteins.
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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/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Csta protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsl protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cystatins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Intermediate Filament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases,
http://linkedlifedata.com/resource/pubmed/chemical/filaggrin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
340
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
173-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7907550-Amino Acid Sequence,
pubmed-meshheading:7907550-Animals,
pubmed-meshheading:7907550-Cathepsin L,
pubmed-meshheading:7907550-Cathepsins,
pubmed-meshheading:7907550-Cystatins,
pubmed-meshheading:7907550-Cysteine Endopeptidases,
pubmed-meshheading:7907550-Endopeptidases,
pubmed-meshheading:7907550-Epidermis,
pubmed-meshheading:7907550-Intermediate Filament Proteins,
pubmed-meshheading:7907550-Molecular Sequence Data,
pubmed-meshheading:7907550-Phosphorylation,
pubmed-meshheading:7907550-Rats,
pubmed-meshheading:7907550-Rats, Sprague-Dawley,
pubmed-meshheading:7907550-Transglutaminases
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pubmed:year |
1994
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pubmed:articleTitle |
Linkage between phosphorylated cystatin alpha and filaggrin by epidermal transglutaminase as a model of cornified envelope and inhibition of cathepsin L activity by cornified envelope and the conjugated cystatin alpha.
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pubmed:affiliation |
Department of Dermatology, Kinky 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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