Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
23
|
| pubmed:dateCreated |
1992-9-10
|
| pubmed:abstractText |
Phosphophoryns are the major non-collagenous proteins of the mineralized matrix of rat incisor dentin. Nearly half the phosphophoryn residues are serines, and 85-90% of these are phosphorylated. Since phosphorylation may be important for phosphophoryn function, it was of interest to identify the kinase(s) responsible for catalyzing their phosphophorylation. Rat osteosarcoma (ROS) 17/2.8 osteoblast-like cells were selected as the enzyme source. Native rat incisor phosphophoryns (RIPP-I, II, III) were not substrates for any of the ROS 17/2.8 messenger-dependent kinases but were phosphorylated by membrane-associated endogenous messenger-independent kinases. These were resolved chromatographically and identified as casein kinase (CK) I and II by elution properties and immunoblotting with a CKII antibody. The CKI preferentially used RIPP-III as substrate, while CKII preferred RIPP-I and II. Heparin at 100 and 500 ng/assay and NaCl at 0.25-0.4 M inhibited phosphorylation of the RIPP by CKI and CKII in parallel. At 10 mM spermine, phosphorylation of RIPP-I and II by CKII, and of RIPP-III by CKI were inhibited, but phosphorylation of RIPP-III by CKII was enhanced. Purified sea star oocyte CKII demonstrated the same substrate specificity and spermine concentration shift as the ROS 17/2.8 CKII. These data show that osteoblast-like cells are a rich source of membrane-bound CKI and CKII activity. The different patterns of phosphorylation of RIPP-I, II, and III further show that they are distinct synthetic products of the odontoblast.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Spermine,
http://linkedlifedata.com/resource/pubmed/chemical/phosphophoryn
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
16588-94
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:1644838-Adenosine Triphosphate,
pubmed-meshheading:1644838-Amino Acid Sequence,
pubmed-meshheading:1644838-Animals,
pubmed-meshheading:1644838-Casein Kinases,
pubmed-meshheading:1644838-Caseins,
pubmed-meshheading:1644838-Cell Line,
pubmed-meshheading:1644838-Chromatography, Gel,
pubmed-meshheading:1644838-Chromatography, Ion Exchange,
pubmed-meshheading:1644838-Dentin,
pubmed-meshheading:1644838-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1644838-Guanosine Triphosphate,
pubmed-meshheading:1644838-Heparin,
pubmed-meshheading:1644838-Incisor,
pubmed-meshheading:1644838-Molecular Sequence Data,
pubmed-meshheading:1644838-Osteosarcoma,
pubmed-meshheading:1644838-Peptides,
pubmed-meshheading:1644838-Phosphoproteins,
pubmed-meshheading:1644838-Phosphorylation,
pubmed-meshheading:1644838-Protein Kinases,
pubmed-meshheading:1644838-Rats,
pubmed-meshheading:1644838-Spermine
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
The in vitro phosphorylation of the native rat incisor dentin phosphophoryns.
|
| pubmed:affiliation |
Connective Tissue Research Laboratory, Northwestern University, Chicago, Illinois 60611.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|