[125I]-[D-Ala2]-beta EP*) binding to Epstein-Barr Virus (EBV) transformed B lymphocytes or to freshly isolated lymphocytes was characterized. The binding was time-, temperature- and pH-dependent; furthermore, it was reversible and cell concentration dependent. Maximum binding appeared at 15C in Tris buffer (pH 7.6) containing both BSA 0.5% and Bacitracin 0.1 mg/ml. beta EP inhibited BEP* binding to transformed lymphocytes and to freshly isolated lymphocytes by 50% at approximately 4 x 10(-8) M and 8 x 10(-9) M, respectively. Peptides representing amino-acid sequences 1-5, 1-16 and 1-17 of beta EP did not inhibit beta EP binding, neither did the opiates compounds Naloxone, Morphine, Bremazocine and Ethylketocyclazocine. On the contrary, beta EPd (6-31) inhibited beta EP* binding as effectively as beta EP, thus indicating that beta EP* binding to lymphocytes does not involve the N-terminal region of beta EP. 2 x 10(7)/ml freshly isolated lymphocytes bound 1.53 +/- 75%, whereas 2 x 10(6)/ml transformed lymphocytes bound 1.64 +/- 0.75% (mean +/- SD) beta EP* at tracer concentration. EBV transformed lymphocytes and freshly isolated lymphocytes may be useful to study beta EP receptors in humans.

Borboni, P., DI COLA, G., Sesti, G., Marini, M.a., Del Porto, P., Gilardini Montani, M., et al. (1989). Beta-endorphin receptors on cultured and freshly isolated lymphocytes from normal subjects. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 163(1), 642-8.

Beta-endorphin receptors on cultured and freshly isolated lymphocytes from normal subjects

BORBONI, PATRIZIA;DI COLA, GIOVANNI;MARINI, MARIA ADELAIDE;LAURO, RENATO;
1989-08-30

Abstract

[125I]-[D-Ala2]-beta EP*) binding to Epstein-Barr Virus (EBV) transformed B lymphocytes or to freshly isolated lymphocytes was characterized. The binding was time-, temperature- and pH-dependent; furthermore, it was reversible and cell concentration dependent. Maximum binding appeared at 15C in Tris buffer (pH 7.6) containing both BSA 0.5% and Bacitracin 0.1 mg/ml. beta EP inhibited BEP* binding to transformed lymphocytes and to freshly isolated lymphocytes by 50% at approximately 4 x 10(-8) M and 8 x 10(-9) M, respectively. Peptides representing amino-acid sequences 1-5, 1-16 and 1-17 of beta EP did not inhibit beta EP binding, neither did the opiates compounds Naloxone, Morphine, Bremazocine and Ethylketocyclazocine. On the contrary, beta EPd (6-31) inhibited beta EP* binding as effectively as beta EP, thus indicating that beta EP* binding to lymphocytes does not involve the N-terminal region of beta EP. 2 x 10(7)/ml freshly isolated lymphocytes bound 1.53 +/- 75%, whereas 2 x 10(6)/ml transformed lymphocytes bound 1.64 +/- 0.75% (mean +/- SD) beta EP* at tracer concentration. EBV transformed lymphocytes and freshly isolated lymphocytes may be useful to study beta EP receptors in humans.
30-ago-1989
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore MED/09 - MEDICINA INTERNA
English
Con Impact Factor ISI
Receptors, Opioid; Adrenocorticotropic Hormone; Time Factors; Cells, Cultured; Temperature; Herpesvirus 4, Human; Binding, Competitive; beta-Endorphin; Cell Transformation, Viral; Lymphocytes; Humans
Borboni, P., DI COLA, G., Sesti, G., Marini, M.a., Del Porto, P., Gilardini Montani, M., et al. (1989). Beta-endorphin receptors on cultured and freshly isolated lymphocytes from normal subjects. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 163(1), 642-8.
Borboni, P; DI COLA, G; Sesti, G; Marini, Ma; Del Porto, P; Gilardini Montani, M; Lauro, R; De Pirro, R
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/53393
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