Enkephalin-hydrolyzing peptidases of rat brain membranes

Are they topographically/functionally coupled to opiate receptors?

László Gráf, András Nagy, Abel Lajtha

Research output: Contribution to journalArticleResearchpeer-review

11 Citations (Scopus)

Abstract

At least four peptidases are involved in the breakdown of Met-enkephalin by rat brain membranes: aminopeptidase(s), angiotensin-converting enzyme (ACE), metalloendopeptidase, and dipeptidyl aminopeptidase. Opiates and some metabolically stable enkephalin analogs used at high concentrations to displace Met-enkephalin from the receptors have no significant effect on the degradation of Met-enkephalin by these peptidases. There is no difference between the dissociation rates of Met-enkephalin from the opiate receptors in membranes, with full and with completely blocked aminopeptidase, ACE, and metalloendopeptidase activities. These data do not imply a close topographical coupling between the opiate receptors and the peptidases studied.

Original languageEnglish
Pages (from-to)1861-1865
Number of pages5
JournalLife Sciences
Volume31
Issue number16-17
DOIs
Publication statusPublished - 1982
Externally publishedYes

Cite this

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title = "Enkephalin-hydrolyzing peptidases of rat brain membranes: Are they topographically/functionally coupled to opiate receptors?",
abstract = "At least four peptidases are involved in the breakdown of Met-enkephalin by rat brain membranes: aminopeptidase(s), angiotensin-converting enzyme (ACE), metalloendopeptidase, and dipeptidyl aminopeptidase. Opiates and some metabolically stable enkephalin analogs used at high concentrations to displace Met-enkephalin from the receptors have no significant effect on the degradation of Met-enkephalin by these peptidases. There is no difference between the dissociation rates of Met-enkephalin from the opiate receptors in membranes, with full and with completely blocked aminopeptidase, ACE, and metalloendopeptidase activities. These data do not imply a close topographical coupling between the opiate receptors and the peptidases studied.",
author = "L{\'a}szl{\'o} Gr{\'a}f and Andr{\'a}s Nagy and Abel Lajtha",
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Enkephalin-hydrolyzing peptidases of rat brain membranes : Are they topographically/functionally coupled to opiate receptors? / Gráf, László; Nagy, András; Lajtha, Abel.

In: Life Sciences, Vol. 31, No. 16-17, 1982, p. 1861-1865.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Enkephalin-hydrolyzing peptidases of rat brain membranes

T2 - Are they topographically/functionally coupled to opiate receptors?

AU - Gráf, László

AU - Nagy, András

AU - Lajtha, Abel

PY - 1982

Y1 - 1982

N2 - At least four peptidases are involved in the breakdown of Met-enkephalin by rat brain membranes: aminopeptidase(s), angiotensin-converting enzyme (ACE), metalloendopeptidase, and dipeptidyl aminopeptidase. Opiates and some metabolically stable enkephalin analogs used at high concentrations to displace Met-enkephalin from the receptors have no significant effect on the degradation of Met-enkephalin by these peptidases. There is no difference between the dissociation rates of Met-enkephalin from the opiate receptors in membranes, with full and with completely blocked aminopeptidase, ACE, and metalloendopeptidase activities. These data do not imply a close topographical coupling between the opiate receptors and the peptidases studied.

AB - At least four peptidases are involved in the breakdown of Met-enkephalin by rat brain membranes: aminopeptidase(s), angiotensin-converting enzyme (ACE), metalloendopeptidase, and dipeptidyl aminopeptidase. Opiates and some metabolically stable enkephalin analogs used at high concentrations to displace Met-enkephalin from the receptors have no significant effect on the degradation of Met-enkephalin by these peptidases. There is no difference between the dissociation rates of Met-enkephalin from the opiate receptors in membranes, with full and with completely blocked aminopeptidase, ACE, and metalloendopeptidase activities. These data do not imply a close topographical coupling between the opiate receptors and the peptidases studied.

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DO - 10.1016/0024-3205(82)90229-6

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JO - Life Sciences

JF - Life Sciences

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