DOI: 10.1242/jcs.1989.supplement_11.10. 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

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

10.1242/jcs.1989.supplement_11.10

Crossref journal-article

The Company of Biologists

Journal of Cell Science (237)

Abstract

ABSTRACT 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=103Mr) 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 (∼60% identity) to the cytoplasmic 70K heat-shock proteins. Surprisingly, the carboxy-terminal 29 amino acids of BÌP/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.

Bibliography

Kozutsumi, Y., Normington, K., Press, E., Slaughter, C., Sambrook, J., & Gething, M.-J. (1989). 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. Journal of Cell Science, 1989(Supplement_11), 115â137.

Authors 6

Yasunori Kozutsumi (first)
Karl Normington (additional)
Eileen Press (additional)
Clive Slaughter (additional)
Joe Sambrook (additional)
Mary-Jane Gething (additional)

References 45 Referenced 34

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Dates

Type	When
Created	12 years, 3 months ago (May 23, 2013, 8:19 a.m.)
Deposited	1 year, 1 month ago (July 10, 2024, 3:49 p.m.)
Indexed	1 year, 1 month ago (July 10, 2024, 4:40 p.m.)
Issued	36 years, 7 months ago (Jan. 1, 1989)
Published	36 years, 7 months ago (Jan. 1, 1989)
Published Online	36 years, 7 months ago (Jan. 1, 1989)
Published Print	36 years, 7 months ago (Jan. 1, 1989)

Funders 0

None

BibTeX

@article{Kozutsumi_1989, title={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}, volume={1989}, ISSN={1477-9137}, url={http://dx.doi.org/10.1242/jcs.1989.supplement_11.10}, DOI={10.1242/jcs.1989.supplement_11.10}, number={Supplement_11}, journal={Journal of Cell Science}, publisher={The Company of Biologists}, author={Kozutsumi, Yasunori and Normington, Karl and Press, Eileen and Slaughter, Clive and Sambrook, Joe and Gething, Mary-Jane}, year={1989}, month=jan, pages={115–137} }

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  "abstract": "<jats:title>ABSTRACT</jats:title>\n               <jats:p>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=103Mr) 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 (\u223c60% identity) to the cytoplasmic 70K heat-shock proteins. Surprisingly, the carboxy-terminal 29 amino acids of B\u00ccP/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.</jats:p>",
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