Linked Life Data

7518712

Source:http://linkedlifedata.com/resource/pubmed/id/7518712

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-8-25
pubmed:abstractText
The past few years have seen an explosion in the identification, cloning and characterization of cytokines and their receptors. The pleiotropic effects of many of the growth factors and the considerable redundancy in the actions of growth factors have contributed to a mass of descriptive literature that often seems to defy summary. Only recently have common concepts begun to emerge. First, cytokines mediate their effects through a large family of receptors that have evolved from a common progenitor and retain structural and functional similarities. Within the haematopoietic system, the cytokines are not usually instructive in differentiation, but rather supportive, and may contribute to some differentiation-specific responses. The patterns of expression of cytokine receptors are therefore a product of differentiation and provide for changes in physiological regulation. The second important concept that is emerging is that the cytokines mediate their mitogenic effects through a common signal-transducing pathway involving tyrosine phosphorylation. Thus, although the cytokine receptor superfamily members do not have intrinsic protein tyrosine kinase activity, by coupling to activation of tyrosine phosphorylation they may affect cell growth by pathways that are common with the large family of growth factor receptors that contain intrinsic protein tyrosine kinase activity. The coupling of cytokine binding to tyrosine phosphorylation and mitogenesis requires a relatively small membrane-proximal domain of the receptors. This region has limited sequence similarity which may be required for the association of individual receptors with an appropriate kinase. Activation of kinase activity results from the dimerization or oligomerization of receptor homodimers or heterodimers. Again this requirement is similar to that seen with the growth factor receptors which have intrinsic protein tyrosine kinase activity. The protein tyrosine kinases that couple cytokine binding to tyrosine phosphorylation are members of the Jak family of kinases. The ubiquitous expression of these kinases provides a common cellular background on which the cytokine receptors can function and on which unique functionally distinct receptors have evolved. In particular, tyk2 is required for the responses initiated by IFN-alpha while Jak2 has been implicated in the responses to G-CSF, IL-3, EPO, growth hormone, prolactin and IFN-gamma.(ABSTRACT TRUNCATED AT 400 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0950-3536
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17-48
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Cytokine receptors and signal transduction.
pubmed:affiliation
Department of Biochemistry, St Jude Children's Research Hospital, Memphis, TN 38105.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't