TY - JOUR
T1 - Cloning, sequencing, expression and function of a cDNA encoding a receptor for the opioid growth factor, [Met5]enkephalin
AU - Zagon, Ian S.
AU - Verderame, Michael F.
AU - Allen, Sandra S.
AU - McLaughlin, Patricia J.
N1 - Funding Information:
Supported by NIH grants CA66783 and NS20500, and the Laverty Foundation. We thank Jean Copper, Denise Gibo, Mary Haldeman, Jennifer Lehman, Bettina Noel and Yan Wu for technical assistance.
PY - 1999/12/4
Y1 - 1999/12/4
N2 - The native opioid growth factor (OGF), [Met5]enkephalin, is a tonic inhibitory peptide that modulates cell proliferation and tissue organization during development, cancer, cellular renewal, wound healing and angiogenesis. OGF action is mediated by a receptor mechanism. We have cloned and sequenced a 2.1-kilobase (kb) cDNA for a receptor to OGF (OGFr). The open reading frame was found to encode a protein of 580 amino acids, and eight imperfect repeats of nine amino acids each were a prominent feature. The protein encoded by this cDNA exhibited the pharmacological, temporal and spatial characteristics of the OGFr. Functional studies using antisense technology demonstrated an enhancement in cell growth. The molecular organization of the OGFr has no homology to classical opioid receptors. These results provide molecular validity for the interaction of OGF and OGFr in the regulation of growth processes. Copyright (C) 1999 Elsevier Science B.V.
AB - The native opioid growth factor (OGF), [Met5]enkephalin, is a tonic inhibitory peptide that modulates cell proliferation and tissue organization during development, cancer, cellular renewal, wound healing and angiogenesis. OGF action is mediated by a receptor mechanism. We have cloned and sequenced a 2.1-kilobase (kb) cDNA for a receptor to OGF (OGFr). The open reading frame was found to encode a protein of 580 amino acids, and eight imperfect repeats of nine amino acids each were a prominent feature. The protein encoded by this cDNA exhibited the pharmacological, temporal and spatial characteristics of the OGFr. Functional studies using antisense technology demonstrated an enhancement in cell growth. The molecular organization of the OGFr has no homology to classical opioid receptors. These results provide molecular validity for the interaction of OGF and OGFr in the regulation of growth processes. Copyright (C) 1999 Elsevier Science B.V.
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U2 - 10.1016/S0006-8993(99)02046-6
DO - 10.1016/S0006-8993(99)02046-6
M3 - Article
C2 - 10592296
AN - SCOPUS:0032748185
SN - 0006-8993
VL - 849
SP - 147
EP - 154
JO - Brain research
JF - Brain research
IS - 1-2
ER -
