Linked Life Data

2559088

Source:http://linkedlifedata.com/resource/pubmed/id/2559088

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-3-8
pubmed:abstractText
Immunoglobulin heavy chain binding protein (BiP) associates transiently with various proteins destined for the secretory pathway. To investigate the relationship between BiP and the 78K (K = 10(3) Mr) glucose-regulated protein (GRP78), we have determined a partial amino acid sequence of purified mouse BiP and isolated and sequenced a full-length cDNA clone encoding mouse GRP78. The 26 amino-terminal residues of the mature BiP protein are identical to a sequence of amino acids located near the start of the open reading frame encoding GRP78. A polyclonal antiserum raised against mouse GRP78 protein expressed in bacteria from the cloned GRP78 cDNA could immunoprecipitate complexes consisting of BiP and unfolded forms of immunoglobulin heavy chains. Furthermore, a monoclonal antibody raised against mouse BiP immunoprecipitated mouse GRP78 expressed in monkey CV-1 cells from an SV40-GRP78 recombinant vector. Finally, like the endogenous BiP of simian cells, mouse GRP78 associated with malfolded, non-glycosylated forms of influenza hemagglutinin (HA) when GRP78 and HA were co-expressed from SV40 vectors in CV-1 cells. These studies confirm that BiP is identical to GRP78. Comparison of the nucleic acid and deduced amino acid sequence of mouse GRP78 with those of other rodent and human GRP78s revealed an extremely high degree of sequence identity. BiP/GRP78 is closely related (approximately 60% identity) to the cytoplasmic 70K heat-shock proteins. Surprisingly, the carboxy-terminal 29 amino acids of BiP/GRP78, which are not conserved in HSP70 proteins, are almost identical in sequence to the steroidogenesis activator peptide found in the cytoplasm of rat Leydig tumor cells. Possible relationships between these polypeptides are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0269-3518
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-37
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:2559088-Amino Acid Sequence, pubmed-meshheading:2559088-Animals, pubmed-meshheading:2559088-Base Sequence, pubmed-meshheading:2559088-Carrier Proteins, pubmed-meshheading:2559088-Cell Line, pubmed-meshheading:2559088-Chromatography, Agarose, pubmed-meshheading:2559088-Cloning, Molecular, pubmed-meshheading:2559088-Cross Reactions, pubmed-meshheading:2559088-DNA, pubmed-meshheading:2559088-Escherichia coli, pubmed-meshheading:2559088-Fluorescent Antibody Technique, pubmed-meshheading:2559088-Genetic Vectors, pubmed-meshheading:2559088-Heat-Shock Proteins, pubmed-meshheading:2559088-Immunoglobulin Heavy Chains, pubmed-meshheading:2559088-Mice, pubmed-meshheading:2559088-Molecular Chaperones, pubmed-meshheading:2559088-Molecular Sequence Data, pubmed-meshheading:2559088-Precipitin Tests, pubmed-meshheading:2559088-Recombinant Fusion Proteins, pubmed-meshheading:2559088-Simian virus 40
pubmed:year
1989
pubmed:articleTitle
Identification of immunoglobulin heavy chain binding protein as glucose-regulated protein 78 on the basis of amino acid sequence, immunological cross-reactivity, and functional activity.
pubmed:affiliation
Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't