|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
9
|
|
pubmed:dateCreated |
1989-6-9
|
|
pubmed:abstractText |
A 70-kDa protein is phosphorylated in cell-free preparations from rat or mouse fibroblasts by an endogenous protein kinase. This protein is immunologically related to a group of 68-kDa to 87-kDa proteins described in the literature as substrates for protein kinase C (PK-C). Although the phosphorylation of the 70-kDa protein by isolated plasma membranes takes place in the presence of EGTA, we conclude that the reaction is catalyzed by PK-C based on its inhibition by staurosporin. As shown previously, pure PK-C phosphorylates a synthetic random polymer of arginine and serine in the absence of Ca2+ and lipids, a reaction markedly stimulated by an endogenous unidentified activator of PK-C. When the 70-kDa protein from normal fibroblasts was exposed to the cytosol of chemically or ras-transformed fibroblasts, it disappeared as measured by phosphorylation by added PK-C. Cytosol of normal fibroblasts was much less effective (ca. 20%). Cathepsin L purified from rat kidney or from the medium of transformed cells had an effect similar to that of the cytosol of transformed cells. When the 70-kDa protein was phosphorylated by PK-C prior to exposure to cathepsin L or to the cytosol of transformed cells, there was a marked protection of the 70-kDa protein. We conclude that the 70-kDa protein is degraded by cathepsin L as ascertained by both immunological and biochemical assays and that it is protected by prior phosphorylation with PK-C. The possible role of this effect in signal transduction is discussed.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-14069539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-199594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-202261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-2830575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-2836438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-2845402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-2883654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-2928301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3045562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3080427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3160581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3281258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3348781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3352735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3370672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3435459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3438085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3476486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3478678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-351614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3558373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3593703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3680264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3680270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3759937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-3956481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-6296071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-6316349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-6957862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2497461-7053088
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsl protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
86
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
3021-5
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:2497461-Alkaloids,
pubmed-meshheading:2497461-Animals,
pubmed-meshheading:2497461-Blotting, Western,
pubmed-meshheading:2497461-Cathepsin L,
pubmed-meshheading:2497461-Cathepsins,
pubmed-meshheading:2497461-Cell Line,
pubmed-meshheading:2497461-Cell Line, Transformed,
pubmed-meshheading:2497461-Cell Membrane,
pubmed-meshheading:2497461-Cysteine Endopeptidases,
pubmed-meshheading:2497461-Cytosol,
pubmed-meshheading:2497461-Egtazic Acid,
pubmed-meshheading:2497461-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2497461-Endopeptidases,
pubmed-meshheading:2497461-Ethylmaleimide,
pubmed-meshheading:2497461-Fibroblasts,
pubmed-meshheading:2497461-Mice,
pubmed-meshheading:2497461-Molecular Weight,
pubmed-meshheading:2497461-Phosphoproteins,
pubmed-meshheading:2497461-Phosphorylation,
pubmed-meshheading:2497461-Protease Inhibitors,
pubmed-meshheading:2497461-Protein Kinase C,
pubmed-meshheading:2497461-Rats,
pubmed-meshheading:2497461-Staurosporine
|
|
pubmed:year |
1989
|
|
pubmed:articleTitle |
Decreased susceptibility of a 70-kDa protein to cathepsin L after phosphorylation by protein kinase C.
|
|
pubmed:affiliation |
Division of Biological Sciences, Cornell University, Ithaca, NY 14853.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
