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F. Petitet

Researcher at Collège de France

Publications -  20
Citations -  590

F. Petitet is an academic researcher from Collège de France. The author has contributed to research in topics: Tachykinin receptor & Receptor. The author has an hindex of 14, co-authored 20 publications receiving 586 citations.

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Possible existence of a new tachykinin receptor subtype in the guinea pig ileum.

TL;DR: Results suggest that septide, [Apa9-10]SP, and [Pro9, 10]SP exert their high contracting activity in the guinea pig ileum by acting on a new subtype of tachykinin receptors.
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Selective agonists of NK-2 binding sites highly active on rat portal vein (NK-3 bioassay).

TL;DR: Comparison of the activities of NKA C-terminal analogues on the guinea-pig ileum suggests that 1) only a small population of NK-2 receptors are present in this tissue and 2) beside NK-1,NK-2 and NK-3 receptors, another type of receptor sensitive to C-Terminal sequences might be present in the guineaspig tissue.
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Higher potency of RP 67580, in the mouse and the rat compared with other nonpeptide and peptide tachykinin NK1 antagonists

TL;DR: RP 67580 appears to be a potent NK1 antagonist in the mouse and the rat, and results obtained with (±)‐CP‐96,345 confirm the lower potency of this compound in these two species when compared with reported data obtained in the guinea‐pig or man.
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Selective agonists of tachykinin binding sites

TL;DR: Three types of binding sites for the mammalian tachykinins, ie Substance P (SP) neurokinin A (NKA) and Neurokinin B (NKB), have been found in both the central and peripheral nervous systems, and complementary strategies led to the design of selective agonists of these binding sites.
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Synergistic regulation of cytosolic Ca2+ concentration in mouse astrocytes by NK1 tachykinin and adenosine agonists.

TL;DR: Pinacidil, which hyper‐polarizes the cells by opening K+ channels, prolonged the elevation of cytosolic Ca2+ concentration induced by [L‐Pro9]‐substance P, while Pertussis toxin pretreatment suppressed all the effects induced by 2‐chloroadenosine.