Isolation and identification of a polypeptide in the Hsp 70 family that binds substance P.
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.
Department of Physiology, University of Massachusetts Medical Center, Worcester 01655.
B
B
Oblas
N D
ND
Boyd
J
J
Luber-Narod
V E
VE
Reyes
S E
SE
Leeman
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D006360:Heat-Shock Proteins / Q000302:isolation & purification* / Q000378:metabolism; D006736:Horses; D008969:Molecular Sequence Data; D008970:Molecular Weight; D005810:Multigene Family; D013363:Submandibular Gland / Q000032:analysis; D013373:Substance P / Q000378:metabolism*
D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D013373:Substance P