|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0037083,
umls-concept:C0060369,
umls-concept:C0205314,
umls-concept:C0332197,
umls-concept:C0332307,
umls-concept:C0679622,
umls-concept:C1333578,
umls-concept:C1515877,
umls-concept:C1519726,
umls-concept:C1710082,
umls-concept:C1879547
|
|
pubmed:issue |
21
|
|
pubmed:dateCreated |
2000-6-30
|
|
pubmed:abstractText |
A novel variant of the fibroblast growth factor receptor type 1 (FGFR-1) was identified in human placental RNA. In this receptor (FGFR-1L) portions of the second and third immunoglobulin-like (Ig-like) domains are deleted. To determine whether FGFR-1L was functional, full-length variant (pSV/FGFR-1L) and wild-type (pSV/FGFR-1) receptors were stably transfected into rat L6 myoblasts cells. Transfected L6 clones expressed respective proteins and bound (125)I-labeled FGF-2 with K(d) values of 99 pm (FGFR-1) and 26 pm (FGFR-1L). FGF-1 and FGF-2 competed efficiently with (125)I-FGF-2 for binding to FGFR-1 and FGFR-1L, whereas FGF-4 was less efficient. FGF-1, FGF-2, and FGF-4 enhanced mitogen-activated protein kinase (MAPK) activity, increased steady-state c-fos mRNA levels, and stimulated proliferation through either receptor, whereas KGF was without effect. FGFR-1 expressing clones exhibited ligand-induced tyrosine phosphorylation of fibroblast growth factor receptor substrate 2 (FRS2), a 90-kDa adaptor protein that links FGFR-1 activation to the MAPK cascade. In contrast, tyrosine phosphorylation of FRS2 was not evident with FGFR-1L. In addition, phospholipase C-gamma was not tyrosine phosphorylated via activated FGFR-1L. These findings indicate that FGFR-1L binds FGF-1 and FGF-2 with high affinity and is capable of mitogenic signaling, but may activate MAPK to occur via non-classical signaling intermediates.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/FGFR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/FGFR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fgfr1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Fgfr2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fos,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Fibroblast Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Fibroblast Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibroblast Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
26
|
|
pubmed:volume |
275
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
15933-9
|
|
pubmed:dateRevised |
2010-5-26
|
|
pubmed:meshHeading |
pubmed-meshheading:10748122-Amino Acid Sequence,
pubmed-meshheading:10748122-Animals,
pubmed-meshheading:10748122-Base Sequence,
pubmed-meshheading:10748122-Cell Division,
pubmed-meshheading:10748122-Cell Line,
pubmed-meshheading:10748122-Cloning, Molecular,
pubmed-meshheading:10748122-Fibroblast Growth Factors,
pubmed-meshheading:10748122-Humans,
pubmed-meshheading:10748122-Isoenzymes,
pubmed-meshheading:10748122-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10748122-Molecular Sequence Data,
pubmed-meshheading:10748122-Phospholipase C gamma,
pubmed-meshheading:10748122-Phosphorylation,
pubmed-meshheading:10748122-Placenta,
pubmed-meshheading:10748122-Protein Binding,
pubmed-meshheading:10748122-Proto-Oncogene Proteins c-fos,
pubmed-meshheading:10748122-RNA, Messenger,
pubmed-meshheading:10748122-Rats,
pubmed-meshheading:10748122-Receptor, Fibroblast Growth Factor, Type 1,
pubmed-meshheading:10748122-Receptor, Fibroblast Growth Factor, Type 2,
pubmed-meshheading:10748122-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:10748122-Receptors, Fibroblast Growth Factor,
pubmed-meshheading:10748122-Sequence Alignment,
pubmed-meshheading:10748122-Signal Transduction,
pubmed-meshheading:10748122-Transfection,
pubmed-meshheading:10748122-Type C Phospholipases
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
A novel type I fibroblast growth factor receptor activates mitogenic signaling in the absence of detectable tyrosine phosphorylation of FRS2.
|
|
pubmed:affiliation |
Division of Endocrinology, Diabetes and Metabolism, Departments of Medicine, Biological Chemistry, and Pharmacology, University of California, Irvine, California 92697, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
