Linked Life Data

11563879

Source:http://linkedlifedata.com/resource/pubmed/id/11563879

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-9-20
pubmed:abstractText
Stem cell factor (SCF) initiates its biological effects by binding to its receptor Kit. Cell surface Kit is proteolytically cleaved to generate soluble Kit. Structure-function analysis of the extracellular region of Kit has implicated the first three immunoglobulin-like domains in SCF binding, and the fourth immunoglobulin-like domain in receptor dimerization. However, the role of the fifth immunoglobulin-like domain is unknown. To test the hypothesis that the fifth immunoglobulin-like domain is important for proteolytic cleavage of Kit from the cell surface, we constructed a mutant form of Kit in which the first four immunoglobulin-like domains are linked to the transmembrane and cytoplasmic domains (designated Kit-Del5). Kit-wild type (Kit-WT) and Kit-Del5 were expressed in the murine mast cell line IC2. Flow cytometry demonstrated that both Kit-WT and Kit-Del5 are displayed on the IC2 cell surface, and immunoblotting confirmed the presence of Kit proteins of the expected molecular weights, 154 kDa and 134 kDa, respectively. Although IC2-Kit-WT cells proteolytically cleave cell surface Kit, generating a 98 kDa soluble form of Kit, IC2-Kit-Del5 cells do not. These findings demonstrate that the fifth immunoglobulin-like domain of Kit is required for proteolytic cleavage of Kit from the cell surface.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1043-4666
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
188-95
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
The fifth immunoglobulin-like domain of the Kit receptor is required for proteolytic cleavage from the cell surface.
pubmed:affiliation
Division of Hematology, University of Washington, Seattle, WA, USA. vcbroudy@u.washington.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.