Isolation and identification of a polypeptide in the HSP 70 family that binds substance P

Barry Oblas; Norman D. Boyd; Judith Luber-Narod; Victor E. Reyes; Susan E. Leeman

doi:10.1016/0006-291X(90)90907-5

Isolation and identification of a polypeptide in the HSP 70 family that binds substance P

Barry Oblas, Norman D. Boyd, Judith Luber-Narod, Victor E. Reyes, Susan E. Leeman

Research output: Contribution to journal › Article › peer-review

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Abstract

During the course of an attempt to purify the substance P (SP) receptor from horse salivary glands by substance P-affinity chromatography, a polypeptide of M_r = 78,000 was isolated. The first fifteen amino acid residues at the amino terminus were determined and, unexpectedly, were found to be identical with the amino terminus of a glucose-regulated protein (GRP) of the same molecular weight, a protein that has been identified as a member of the heat shock protein family. This finding raises the intriguing possibility that SP may interact in vivo with GRPs and other members of the heat shock protein family and play a role in modulating their biological activities.

Original language	English (US)
Pages (from-to)	978-983
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	166
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(90)90907-5
State	Published - Jan 30 1990
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(90)90907-5

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title = "Isolation and identification of a polypeptide in the HSP 70 family that binds substance P",

abstract = "During the course of an attempt to purify the substance P (SP) receptor from horse salivary glands by substance P-affinity chromatography, a polypeptide of Mr = 78,000 was isolated. The first fifteen amino acid residues at the amino terminus were determined and, unexpectedly, were found to be identical with the amino terminus of a glucose-regulated protein (GRP) of the same molecular weight, a protein that has been identified as a member of the heat shock protein family. This finding raises the intriguing possibility that SP may interact in vivo with GRPs and other members of the heat shock protein family and play a role in modulating their biological activities.",

author = "Barry Oblas and Boyd, {Norman D.} and Judith Luber-Narod and Reyes, {Victor E.} and Leeman, {Susan E.}",

note = "Funding Information: The authors thank Ms. Janet Hoogasian for her skillful technical assistance and Dr. Robert E. Humphreys for his gift of the NP335-356 peptide fragment. V.E.R. was a fellow of the Jeane B. Kempner Fund. This work was supported by NIH ROlDK 29876.",

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T1 - Isolation and identification of a polypeptide in the HSP 70 family that binds substance P

AU - Oblas, Barry

AU - Boyd, Norman D.

AU - Luber-Narod, Judith

AU - Reyes, Victor E.

AU - Leeman, Susan E.

N1 - Funding Information: The authors thank Ms. Janet Hoogasian for her skillful technical assistance and Dr. Robert E. Humphreys for his gift of the NP335-356 peptide fragment. V.E.R. was a fellow of the Jeane B. Kempner Fund. This work was supported by NIH ROlDK 29876.

PY - 1990/1/30

Y1 - 1990/1/30

N2 - During the course of an attempt to purify the substance P (SP) receptor from horse salivary glands by substance P-affinity chromatography, a polypeptide of Mr = 78,000 was isolated. The first fifteen amino acid residues at the amino terminus were determined and, unexpectedly, were found to be identical with the amino terminus of a glucose-regulated protein (GRP) of the same molecular weight, a protein that has been identified as a member of the heat shock protein family. This finding raises the intriguing possibility that SP may interact in vivo with GRPs and other members of the heat shock protein family and play a role in modulating their biological activities.

AB - During the course of an attempt to purify the substance P (SP) receptor from horse salivary glands by substance P-affinity chromatography, a polypeptide of Mr = 78,000 was isolated. The first fifteen amino acid residues at the amino terminus were determined and, unexpectedly, were found to be identical with the amino terminus of a glucose-regulated protein (GRP) of the same molecular weight, a protein that has been identified as a member of the heat shock protein family. This finding raises the intriguing possibility that SP may interact in vivo with GRPs and other members of the heat shock protein family and play a role in modulating their biological activities.

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JO - Biochemical and Biophysical Research Communications

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Isolation and identification of a polypeptide in the HSP 70 family that binds substance P

Abstract

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