Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2003-10-27
pubmed:databankReference
pubmed:abstractText
Cell surface retention sequence binding protein-1 (CRSBP-1) is a cell surface binding protein for the cell surface retention sequence (CRS) motif of the v-sis gene product (platelet-derived growth factor-BB). It has been shown to be responsible for cell surface retention of the v-sis gene product in v-sis-transformed cells (fibroblasts) and has been hypothesized to play a role in autocrine growth and transformation of these cells. Here we demonstrate that the CRSBP-1 cDNA cloned from bovine liver libraries encodes a 322-residue type I membrane protein containing a 23-residue signal peptide, a 215-residue cell surface domain, a 21-residue transmembrane domain, and a 63-residue cytoplasmic domain. CRSBP-1 expressed in transfected cells is an approximately 120-kDa disulfide-linked homodimeric glycoprotein and exhibits dual ligand (CRS-containing growth regulators (v-sis gene product and insulin-like growth factor binding protein-3, IGFBP-3) and hyaluronic acid) binding activity. CRSBP-1 overexpression (by stable transfection of cells with CRSBP-1 cDNA) enhances autocrine loop signaling, cell growth, and tumorigenicity (in mice) of v-sis-transformed cells. CRSBP-1 expression also enhances autocrine cell growth mediated by IGFBP-3 in human lung carcinoma cells (H1299 cells), which express very little, if any, endogenous CRSBP-1 and exhibits a mitogenic response to exogenous IGFBP-3, stably transfected with IGFBP-3 cDNA. However, CRSBP-1 overexpression does not affect growth of normal and transformed cells that do not produce these CRS-containing growth regulators. These results suggest that CRSBP-1 plays a role in autocrine regulation of cell growth mediated by growth regulators containing CRS.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43855-69
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12912978-Amino Acid Motifs, pubmed-meshheading:12912978-Amino Acid Sequence, pubmed-meshheading:12912978-Animals, pubmed-meshheading:12912978-Base Sequence, pubmed-meshheading:12912978-Blotting, Western, pubmed-meshheading:12912978-Cattle, pubmed-meshheading:12912978-Cell Division, pubmed-meshheading:12912978-Cell Line, Transformed, pubmed-meshheading:12912978-Cell Line, Tumor, pubmed-meshheading:12912978-Cytoplasm, pubmed-meshheading:12912978-DNA, Complementary, pubmed-meshheading:12912978-Detergents, pubmed-meshheading:12912978-Dimerization, pubmed-meshheading:12912978-Disulfides, pubmed-meshheading:12912978-Fibroblasts, pubmed-meshheading:12912978-Gene Library, pubmed-meshheading:12912978-Glycoproteins, pubmed-meshheading:12912978-Humans, pubmed-meshheading:12912978-Immunoblotting, pubmed-meshheading:12912978-Insulin-Like Growth Factor Binding Protein 3, pubmed-meshheading:12912978-Liver, pubmed-meshheading:12912978-Membrane Proteins, pubmed-meshheading:12912978-Mice, pubmed-meshheading:12912978-Molecular Sequence Data, pubmed-meshheading:12912978-NIH 3T3 Cells, pubmed-meshheading:12912978-Octoxynol, pubmed-meshheading:12912978-Oncogene Proteins v-sis, pubmed-meshheading:12912978-Peptides, pubmed-meshheading:12912978-Protein Binding, pubmed-meshheading:12912978-Protein Sorting Signals, pubmed-meshheading:12912978-Sequence Homology, Amino Acid, pubmed-meshheading:12912978-Time Factors, pubmed-meshheading:12912978-Transfection
pubmed:year
2003
pubmed:articleTitle
Cloning, expression, characterization, and role in autocrine cell growth of cell surface retention sequence binding protein-1.
pubmed:affiliation
Departments of Biochemistry and Molecular Biology, St. Louis University School of Medicine, St. Louis, Missouri 63104, USA. huangjs@slu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't