pubmed-article:19090718 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C0022478 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C1416680 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C1979963 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C2003903 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C0205197 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C2348557 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C1556116 | lld:lifeskim |
pubmed-article:19090718 | lifeskim:mentions | umls-concept:C1556117 | lld:lifeskim |
pubmed-article:19090718 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:19090718 | pubmed:dateCreated | 2009-5-1 | lld:pubmed |
pubmed-article:19090718 | pubmed:abstractText | We previously reported the activation profiles of the human kallikrein-related peptidases (KLKs) as determined from a KLK pro-peptide fusion-protein system. That report described the activity profiles of 12 of the 15 mature KLKs versus the 15 different pro-KLK sequences. The missing profiles in the prior report, involving KLK9, 10, and 15, are now described. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, mass spectrometry, and N-terminal sequence analyses show that KLK9 and 10 exhibit low hydrolytic activities towards all of the 15 pro-KLK sequences, while KLK15 exhibits significant activity towards both Arg- and Lys-containing KLK pro-sequences. The ability of KLK15 to activate pro-KLK8, 12, and 14 is confirmed using recombinant pro-KLK proteins, and shown to be significant for activation of pro-KLK8 and 14, but not 12. These additional data for KLK9, 10, and 15 now permit a completed KLK activome profile, using a KLK pro-peptide fusion-protein system, to be described. The results suggest that KLK15, once activated, can potentially feed back into additional pro-KLK activation pathways. Conversely, KLK9 and 10, once activated, are unlikely to participate in further pro-KLK activation pathways, although similar to KLK1 they may activate other bioactive peptides. | lld:pubmed |
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pubmed-article:19090718 | pubmed:language | eng | lld:pubmed |
pubmed-article:19090718 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19090718 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:19090718 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19090718 | pubmed:month | Apr | lld:pubmed |
pubmed-article:19090718 | pubmed:issn | 1431-6730 | lld:pubmed |
pubmed-article:19090718 | pubmed:author | pubmed-author:BlaberSachiko... | lld:pubmed |
pubmed-article:19090718 | pubmed:author | pubmed-author:ScarisbrickIs... | lld:pubmed |
pubmed-article:19090718 | pubmed:author | pubmed-author:BlaberMichael... | lld:pubmed |
pubmed-article:19090718 | pubmed:author | pubmed-author:GoettigPeterP | lld:pubmed |
pubmed-article:19090718 | pubmed:author | pubmed-author:DebelaMekdesM | lld:pubmed |
pubmed-article:19090718 | pubmed:author | pubmed-author:YoonHyesookH | lld:pubmed |
pubmed-article:19090718 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:19090718 | pubmed:volume | 390 | lld:pubmed |
pubmed-article:19090718 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19090718 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19090718 | pubmed:pagination | 373-7 | lld:pubmed |
pubmed-article:19090718 | pubmed:dateRevised | 2011-2-16 | lld:pubmed |
pubmed-article:19090718 | pubmed:meshHeading | pubmed-meshheading:19090718... | lld:pubmed |
pubmed-article:19090718 | pubmed:meshHeading | pubmed-meshheading:19090718... | lld:pubmed |
pubmed-article:19090718 | pubmed:meshHeading | pubmed-meshheading:19090718... | lld:pubmed |
pubmed-article:19090718 | pubmed:meshHeading | pubmed-meshheading:19090718... | lld:pubmed |
pubmed-article:19090718 | pubmed:meshHeading | pubmed-meshheading:19090718... | lld:pubmed |
pubmed-article:19090718 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19090718 | pubmed:articleTitle | A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15. | lld:pubmed |
pubmed-article:19090718 | pubmed:affiliation | Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306-4300, USA. | lld:pubmed |
pubmed-article:19090718 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19090718 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:19090718 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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