Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
31
|
| pubmed:dateCreated |
1993-11-29
|
| pubmed:abstractText |
The major species of voltage-gated potassium channel found on mammalian T lymphocytes is referred to as the type n channel. This potassium channel exhibits unique functional properties which distinguish it from other species of potassium channels, including a potential role in the onset of cellular events associated with T cell activation. As a first step in characterizing specific biochemical properties of the type n channel, we have generated polyclonal antisera against bacterial fusion proteins containing peptide regions unique to the mouse and human type n channel. From membranes of T cell lines derived from both mouse (SAK 8 cell line) and human (Jurkat cell line), the type n channel can be immunoprecipitated following either surface labeling with 125I or metabolic labeling with 32P. The apparent molecular mass of the immunoprecipitated type n channel is approximately 65 kDa, significantly greater than that of the 58-kDa in vitro translated product, and suggestive of post-translational modification events. Phosphoamino acid analysis of the metabolically labeled Jurkat type n channel reveals phosphorylation of serine residues exclusively. In vitro studies also describe the ability of both protein kinase A and protein kinase C to phosphorylate the Jurkat type n channel. The former kinase also appears to phosphorylate a 40-kDa protein which co-immunoprecipitates with the type n channel. These data suggest that direct phosphorylation of the T lymphocyte type n potassium channel or its associated 40-kDa subunit may serve as a means by which channel activity is regulated.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
23720-7
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8226897-Amino Acid Sequence,
pubmed-meshheading:8226897-Animals,
pubmed-meshheading:8226897-Cell Line,
pubmed-meshheading:8226897-Cell Membrane,
pubmed-meshheading:8226897-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:8226897-Humans,
pubmed-meshheading:8226897-Immunologic Techniques,
pubmed-meshheading:8226897-Mice,
pubmed-meshheading:8226897-Molecular Sequence Data,
pubmed-meshheading:8226897-Phosphorylation,
pubmed-meshheading:8226897-Potassium Channels,
pubmed-meshheading:8226897-Precipitin Tests,
pubmed-meshheading:8226897-Protein Kinase C,
pubmed-meshheading:8226897-Protein Processing, Post-Translational,
pubmed-meshheading:8226897-Rats,
pubmed-meshheading:8226897-Recombinant Fusion Proteins,
pubmed-meshheading:8226897-Sequence Alignment,
pubmed-meshheading:8226897-Sequence Homology, Amino Acid,
pubmed-meshheading:8226897-T-Lymphocytes
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
In vivo and in vitro phosphorylation of the T lymphocyte type n (Kv1.3) potassium channel.
|
| pubmed:affiliation |
Vollum Institute, Oregon Health Sciences University, Portland 97201.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
|