Linked Life Data

9374491

Source:http://linkedlifedata.com/resource/pubmed/id/9374491

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
48
pubmed:dateCreated
1997-12-22
pubmed:databankReference
pubmed:abstractText
We have cloned and characterized a new member of the p38 group of mitogen-activated protein kinases here termed p38delta. Sequence comparisons revealed that p38delta is approximately 60% identical to the other three p38 isoforms but only 40-45% to the other mitogen-activated protein kinase family members. It contains the TGY dual phosphorylation site present in all p38 group members and is activated by a group of extracellular stimuli including cytokines and environmental stresses that also activate the other three known p38 isoforms. However, unlike the other p38 isoforms, the kinase activity of p38delta is not blocked by the pyridinyl imidazole, 4-(4-fluorophenyl)-2-2(4-hydroxyphenyl)-5-(4-pyridyl)-imidazole (identicalto SB202190). p38delta can be activated by MKK3 and MKK6, known activators of the other isoforms. Nonetheless, in-gel kinase assays provide evidence for additional activators. The data presented herein show that p38delta has many properties that are similar to those of other p38 group members. Nonetheless important differences exist among the four members of the p38 group of enzymes, and thus each may have highly specific, individual contributions to biologic events involving activation of the p38 pathways.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30122-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9374491-Amino Acid Sequence, pubmed-meshheading:9374491-Animals, pubmed-meshheading:9374491-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9374491-Cloning, Molecular, pubmed-meshheading:9374491-Enzyme Activation, pubmed-meshheading:9374491-Gene Expression, pubmed-meshheading:9374491-Glomerulonephritis, pubmed-meshheading:9374491-Isoenzymes, pubmed-meshheading:9374491-MAP Kinase Kinase 3, pubmed-meshheading:9374491-MAP Kinase Kinase 6, pubmed-meshheading:9374491-Mitogen-Activated Protein Kinase Kinases, pubmed-meshheading:9374491-Mitogen-Activated Protein Kinases, pubmed-meshheading:9374491-Molecular Sequence Data, pubmed-meshheading:9374491-Phylogeny, pubmed-meshheading:9374491-Protein-Serine-Threonine Kinases, pubmed-meshheading:9374491-Protein-Tyrosine Kinases, pubmed-meshheading:9374491-RNA, Messenger, pubmed-meshheading:9374491-Rabbits, pubmed-meshheading:9374491-Sequence Alignment, pubmed-meshheading:9374491-Sequence Homology, Amino Acid, pubmed-meshheading:9374491-Substrate Specificity, pubmed-meshheading:9374491-Tissue Distribution, pubmed-meshheading:9374491-p38 Mitogen-Activated Protein Kinases
pubmed:year
1997
pubmed:articleTitle
Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta.
pubmed:affiliation
Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA. jhan@scripps.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't