Localization of substance P binding sites in submucous plexus of guinea pig ileum, using whole-mount autoradiography

Synapse ◽  
1988 ◽  
Vol 2 (3) ◽  
pp. 232-239 ◽  
Author(s):  
Elizabeth Burcher ◽  
Joel C. Bornstein
1991 ◽  
Vol 560 (1-2) ◽  
pp. 1-11 ◽  
Author(s):  
Christine Tousignant ◽  
Gaétan Guillemette ◽  
Domenico Regoli

1998 ◽  
Vol 30 (4-5) ◽  
pp. 242-245 ◽  
Author(s):  
A. V. Glushakov ◽  
H. Yu. Glushakova ◽  
V. I. Skok

1987 ◽  
Vol 253 (5) ◽  
pp. G666-G672
Author(s):  
J. C. Souquet ◽  
K. N. Bitar ◽  
J. R. Grider ◽  
G. M. Makhlouf

Two radioligands, 125I-labeled substance P (125I-SP) and 125I-labeled substance K (125I-SK), were used to characterize the kinetics and stoichiometry of binding of mammalian tachykinins [substance P (SP), substance K (SK), and neuromedin K (NK)] to smooth muscle cells isolated from the longitudinal muscle layer of guinea pig intestine. Specific binding of 125I-SP and 125I-SK was rapid, saturable, reversible, and temperature dependent. Binding attained 63-70% of steady-state binding within 1 min, coincidentally with the time of optimal contraction. The order of potency with which mammalian tachykinins and the SP antagonist, [D-Pro2, D-Trp7,9]SP, inhibited the binding of both radioligands was identical: SP greater than SK greater than NK greater than [D-Pro2, D-Trp7,9]SP, implying preferential interaction with a site that had highest affinity for SP. SK was 2-3 times, NK 3-4 times, and [D-Pro2, D-Trp7,9]SP 7-23 times less potent than SP (IC50 0.36 nM). Except for NK, the order of potency was similar to that for contraction of isolated muscle cells. The existence of binding sites with even higher affinity was suggested by the ability of muscle cells to contract in response to concentrations as low as 10(-13) M. These binding sites were not detectable at the concentration of radioligands used. It was concluded that a SP receptor is the only tachykinin receptor subtype present on intestinal muscle cells of the guinea pig.


1984 ◽  
Vol 246 (5) ◽  
pp. G509-G514 ◽  
Author(s):  
D. H. Teitelbaum ◽  
T. M. O'Dorisio ◽  
W. E. Perkins ◽  
T. S. Gaginella

The peptides caerulein, neurotensin, somatostatin, and substance P modulate the activity of intestinal neurons and alter gut motility. We examined the effects of these peptides on acetylcholine release from the myenteric plexus and intestinal contractility in vitro. Caerulein (1 X 10(-9) M), neurotensin (1.5 X 10(-6) M), and substance P (1 X 10(-7) M) significantly enhanced the release of [3H]acetylcholine from the myenteric plexus of the guinea pig ileum. This effect was inhibited by tetrodotoxin (1.6 X 10(-6) M). Somatostatin (10(-6) M) inhibited caerulein- and neurotensin-evoked release of acetylcholine but did not inhibit release induced by substance P. Caerulein, neurotensin, and substance P caused contraction of the guinea pig ileal longitudinal muscle. Somatostatin inhibited the contractions induced by caerulein and neurotensin. In contrast, substance P-induced contraction was not inhibited significantly by somatostatin. Thus, in the guinea pig ileum, caerulein-, neurotensin-, and substance P-induced contractility is due, at least in part, to acetylcholine release from the myenteric plexus. The ability of somatostatin to inhibit peptide-induced contractility is selective, and its mechanism may be attributed to inhibition of acetylcholine release.


1987 ◽  
Vol 335 (6) ◽  
pp. 629-635 ◽  
Author(s):  
M. Tonini ◽  
L. Onori ◽  
C. A. Rizzi ◽  
E. Perucca ◽  
L. Manzo ◽  
...  

1984 ◽  
Vol 36 ◽  
pp. 87
Author(s):  
Kohtaro Taniyama ◽  
Yukiko Miki ◽  
Masato Kusunoki ◽  
Naoaki Saito ◽  
Chikako Tanaka

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