|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0010453,
umls-concept:C0017263,
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0085536,
umls-concept:C0227651,
umls-concept:C0332120,
umls-concept:C0597357,
umls-concept:C1416912,
umls-concept:C1417509,
umls-concept:C1419111
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1992-11-19
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Protein tyrosine phosphatases (PTPases) are a family of enzymes that play a crucial role in the regulation of signal transduction mediated by reversible protein tyrosine phosphorylation. To understand the significance of PTPases in physiological and pathophysiological processes in the kidney, we isolated three cDNA segments encoding PTPases (LAR, LRP and a novel PTPase) from rat kidney by polymerase chain reaction (PCR). Using PCR product as a probe, we isolated a full-length cDNA of rat LRP. LRP cDNA encoded a single membrane spanning protein consisted of 796 amino acids, with two tandemly located intracellular PTPase domains. By Northern analysis, a ubiquitous pattern of LRP gene expression in rat tissues was demonstrated. In cultured rat mesangial cells, LRP mRNA was detected and the mRNA level was suppressed by either interleukin-1 or interleukin-6 treatment.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpra protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Like Protein Tyrosine...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0006-291X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
188
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
34-9
|
|
pubmed:dateRevised |
2007-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:1417854-Amino Acid Sequence,
pubmed-meshheading:1417854-Animals,
pubmed-meshheading:1417854-Base Sequence,
pubmed-meshheading:1417854-Cells, Cultured,
pubmed-meshheading:1417854-Cloning, Molecular,
pubmed-meshheading:1417854-DNA,
pubmed-meshheading:1417854-Gene Expression Regulation,
pubmed-meshheading:1417854-Glomerular Mesangium,
pubmed-meshheading:1417854-Glycoproteins,
pubmed-meshheading:1417854-Kidney,
pubmed-meshheading:1417854-Male,
pubmed-meshheading:1417854-Molecular Sequence Data,
pubmed-meshheading:1417854-Oligodeoxyribonucleotides,
pubmed-meshheading:1417854-Organ Specificity,
pubmed-meshheading:1417854-Polymerase Chain Reaction,
pubmed-meshheading:1417854-Protein Tyrosine Phosphatases,
pubmed-meshheading:1417854-RNA, Messenger,
pubmed-meshheading:1417854-Rats,
pubmed-meshheading:1417854-Rats, Sprague-Dawley,
pubmed-meshheading:1417854-Receptor-Like Protein Tyrosine Phosphatases, Class 4,
pubmed-meshheading:1417854-Receptors, Cell Surface,
pubmed-meshheading:1417854-Restriction Mapping
|
|
pubmed:year |
1992
|
|
pubmed:articleTitle |
cDNA cloning of rat LRP, a receptor like protein tyrosine phosphatase, and evidence for its gene regulation in cultured rat mesangial cells.
|
|
pubmed:affiliation |
1st Department of Medicine, Osaka University Medical School, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
