Cloning, sequencing, expression and function of a cDNA encoding a receptor for the opioid growth factor, [Met5]enkephalin

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)147-154
Number of pages8
JournalBrain research
Volume849
Issue number1-2
DOIs
StatePublished - Dec 4 1999

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Enkephalins
Opioid Analgesics
Organism Cloning
Intercellular Signaling Peptides and Proteins
Complementary DNA
Biomedical Enhancement
Amino Acids
Opioid Receptors
Growth
Wound Healing
Open Reading Frames
Proteins
Cell Proliferation
Pharmacology
Peptides
methionine-enkephalin receptor
Neoplasms

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

Cite this

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title = "Cloning, sequencing, expression and function of a cDNA encoding a receptor for the opioid growth factor, [Met5]enkephalin",
abstract = "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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AU - Zagon, Ian

AU - Verderame, Michael

AU - Allen, Sandra S.

AU - McLaughlin, Patricia

PY - 1999/12/4

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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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