A secreted peptidase involved in T cell β-endorphin metabolism

B. C. Miller; D. Thiele; L. B. Hersh; G. L. Cottam

doi:10.1016/0162-3109(95)00046-1

A secreted peptidase involved in T cell β-endorphin metabolism

B. C. Miller, D. Thiele, L. B. Hersh, G. L. Cottam

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

12 Scopus citations

Abstract

β-endorphin metabolism by CD4⁺ and CD8⁺ T cells, and the thymoma cell line, EL4, was investigated. In all three cell types, extracellular β-endorphin was metabolized exclusively by a secreted, metal-dependent, thiol peptidase. The enzyme activity is expressed constitutively in EL4 cells and following activation of CD4⁺ and CD8⁺ T cells with anti-CD3 antibody. The enzyme is not one of the proteinases associated with cytolytic T cells and does not appear to be identical with any previously described β-endorphin metabolizing enzyme. The enzyme cleaves β-endorphin at approximately equal rates at either of two sites to yield β-endorphin_1-17 (which is γ-endorphin), β-endorphin_1-18, β-endorphin_18-31 and β-endorphin_19-31. Evidence in the literature indicates that these N- and C-terminal peptides which contain, respectively, the opioid and non-opioid receptor binding domains of β-endorphin, are biologically active. Thus, it is likely that this new T cell peptidase has important immunoregulatory activity.

Original language	English
Pages (from-to)	151-161
Number of pages	11
Journal	Immunopharmacology
Volume	31
Issue number	2-3
DOIs	https://doi.org/10.1016/0162-3109(95)00046-1
State	Published - Mar 1996

Bibliographical note

Funding Information:
We would like to thank Carolyn Moomaw and Willa Rollerson of Dr. Clive Slaughter's laboratory at the University of Texas Southwestern Medical Center for performing the peptide microsequencing and amino acid analyses to identify the/3-endorphin metabolites; and Dr. Mike McGuire, also of the University of Texas Southwestern Medical Center, for many helpful discussions. This work was supported in part by U.S. Public Health Service Grant DA07062 (GLC), DA08801 (BCM), and DA02243 (LBH).

Keywords

T cell peptidase
β-Endorphin metabolism
γ-Endorphin

ASJC Scopus subject areas

Pharmacology

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10.1016/0162-3109(95)00046-1

Cite this

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title = "A secreted peptidase involved in T cell β-endorphin metabolism",

abstract = "β-endorphin metabolism by CD4+ and CD8+ T cells, and the thymoma cell line, EL4, was investigated. In all three cell types, extracellular β-endorphin was metabolized exclusively by a secreted, metal-dependent, thiol peptidase. The enzyme activity is expressed constitutively in EL4 cells and following activation of CD4+ and CD8+ T cells with anti-CD3 antibody. The enzyme is not one of the proteinases associated with cytolytic T cells and does not appear to be identical with any previously described β-endorphin metabolizing enzyme. The enzyme cleaves β-endorphin at approximately equal rates at either of two sites to yield β-endorphin1-17 (which is γ-endorphin), β-endorphin1-18, β-endorphin18-31 and β-endorphin19-31. Evidence in the literature indicates that these N- and C-terminal peptides which contain, respectively, the opioid and non-opioid receptor binding domains of β-endorphin, are biologically active. Thus, it is likely that this new T cell peptidase has important immunoregulatory activity.",

keywords = "T cell peptidase, β-Endorphin metabolism, γ-Endorphin",

author = "Miller, {B. C.} and D. Thiele and Hersh, {L. B.} and Cottam, {G. L.}",

note = "Funding Information: We would like to thank Carolyn Moomaw and Willa Rollerson of Dr. Clive Slaughter's laboratory at the University of Texas Southwestern Medical Center for performing the peptide microsequencing and amino acid analyses to identify the/3-endorphin metabolites; and Dr. Mike McGuire, also of the University of Texas Southwestern Medical Center, for many helpful discussions. This work was supported in part by U.S. Public Health Service Grant DA07062 (GLC), DA08801 (BCM), and DA02243 (LBH).",

year = "1996",

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doi = "10.1016/0162-3109(95)00046-1",

language = "English",

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T1 - A secreted peptidase involved in T cell β-endorphin metabolism

AU - Miller, B. C.

AU - Thiele, D.

AU - Hersh, L. B.

AU - Cottam, G. L.

N1 - Funding Information: We would like to thank Carolyn Moomaw and Willa Rollerson of Dr. Clive Slaughter's laboratory at the University of Texas Southwestern Medical Center for performing the peptide microsequencing and amino acid analyses to identify the/3-endorphin metabolites; and Dr. Mike McGuire, also of the University of Texas Southwestern Medical Center, for many helpful discussions. This work was supported in part by U.S. Public Health Service Grant DA07062 (GLC), DA08801 (BCM), and DA02243 (LBH).

PY - 1996/3

Y1 - 1996/3

N2 - β-endorphin metabolism by CD4+ and CD8+ T cells, and the thymoma cell line, EL4, was investigated. In all three cell types, extracellular β-endorphin was metabolized exclusively by a secreted, metal-dependent, thiol peptidase. The enzyme activity is expressed constitutively in EL4 cells and following activation of CD4+ and CD8+ T cells with anti-CD3 antibody. The enzyme is not one of the proteinases associated with cytolytic T cells and does not appear to be identical with any previously described β-endorphin metabolizing enzyme. The enzyme cleaves β-endorphin at approximately equal rates at either of two sites to yield β-endorphin1-17 (which is γ-endorphin), β-endorphin1-18, β-endorphin18-31 and β-endorphin19-31. Evidence in the literature indicates that these N- and C-terminal peptides which contain, respectively, the opioid and non-opioid receptor binding domains of β-endorphin, are biologically active. Thus, it is likely that this new T cell peptidase has important immunoregulatory activity.

AB - β-endorphin metabolism by CD4+ and CD8+ T cells, and the thymoma cell line, EL4, was investigated. In all three cell types, extracellular β-endorphin was metabolized exclusively by a secreted, metal-dependent, thiol peptidase. The enzyme activity is expressed constitutively in EL4 cells and following activation of CD4+ and CD8+ T cells with anti-CD3 antibody. The enzyme is not one of the proteinases associated with cytolytic T cells and does not appear to be identical with any previously described β-endorphin metabolizing enzyme. The enzyme cleaves β-endorphin at approximately equal rates at either of two sites to yield β-endorphin1-17 (which is γ-endorphin), β-endorphin1-18, β-endorphin18-31 and β-endorphin19-31. Evidence in the literature indicates that these N- and C-terminal peptides which contain, respectively, the opioid and non-opioid receptor binding domains of β-endorphin, are biologically active. Thus, it is likely that this new T cell peptidase has important immunoregulatory activity.

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KW - β-Endorphin metabolism

KW - γ-Endorphin

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A secreted peptidase involved in T cell β-endorphin metabolism

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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