par Dehaye, Jean-Paul 
;Christophe, Jean ;Ernst, Felix ;Poloczek, Piotr ;Van Bogaert, Patrick
Référence Archives of oral biology, 30, 11-12, page (827-832)
Publication Publié, 1985
;Christophe, Jean ;Ernst, Felix ;Poloczek, Piotr ;Van Bogaert, Patrick Référence Archives of oral biology, 30, 11-12, page (827-832)
Publication Publié, 1985
Article révisé par les pairs
| Résumé : | Binding of 125I-labelled vasoactive intestinal peptide (VIP) to rat parotid acini was saturable, temperature-dependent and reversible, and reflected interaction with a single class of binding sites. Parotid glands possessed approx. 400 fmol binding sites per mg protein and binding of the tracer to these sites could be inhibited by VIP [concentration for half-maximal effect (Kd), 24 nM], by the peptide histidine isoleucine (Kd, 140 nM), by secretin (Kd, 470 nM) and by the human pancreatic growth hormone-releasing factor (hpGRF; Kd, 3200 nM). In the same acini preparation, 10μM VIP also stimulated amylase release 4-fold and increased cyclic AMP 11-fold. Thus, VIP might be a neurotransmitter in the rat parotid gland. © 1985. |
