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167 results on '"Emonds-Alt X"'

7. Comparative effects of nonpeptide tachykinin receptor antagonists on experimental gut inflammation in rats and guinea-pigs

Author

Mazelin, L., Theodorou, Vassilia, Emonds-Alt, X., Fioramonti, Jean, Bueno, Lionel, ProdInra, Migration, Unité de recherche Pharmacologie-Toxicologie (UPT), and Institut National de la Recherche Agronomique (INRA)

Subjects
[SDV] Life Sciences [q-bio], COBAYE, [SDV]Life Sciences [q-bio], RAT, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
1998

14. Biochemical and pharmacological activities of SR 144190, a new potent non-peptide tachykinin NK2 receptor antagonist

Author

Emonds-Alt, X, primary, Advenier, C, additional, Cognon, C, additional, Croci, T, additional, Daoul, S, additional, Ducoux, J.P, additional, Landi, M, additional, Naline, E, additional, Neliat, G, additional, Poncelet, M, additional, Proietto, V, additional, Van Broeck, D, additional, Vilain, P, additional, Soubrié, P, additional, Le Fur, G, additional, Maffrand, J.P, additional, and Brelière, J.C, additional

Published
1997
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45. A direct simultaneous plate assay of proteoglycan and collagen degradation by cells in culture and its application to synovial cells

Author

Peeters-Joris, C, Emonds-Alt, X, and Vaes, G

Abstract

1. A radiochemical plate assay is presented that allows a simultaneous evaluation of the capacity of cells in culture to degrade proteoglycan and collagen. Its principle consists of monitoring the release of soluble radioactive degradation products from Multiwell culture plates coated with dried reconstituted 3H-labelled-proteoglycan/14C-labelled-collagen mixed gels. The plates can also be used for the assay of proteolytic activities within enzyme solutions. 2. When cultured on the plates, rabbit synovial cells degrade collagen and proteoglycan almost simultaneously, owing to the secretion of collagenase and of a proteoglycan-degrading metal-dependent neutral proteinase.

Published
1981
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48. Functional characterization of the nonpeptide neurokinin3 (NK3) receptor antagonist, SR142801 on the human NK3 receptor expressed in Chinese hamster ovary cells.

Author

Oury-Donat, F, Carayon, P, Thurneyssen, O, Pailhon, V, Emonds-Alt, X, Soubrié, P, and Le Fur, G

Abstract

The effects of SR142801, a nonpeptide tachykinin neurokinin (NK3) receptor antagonist, were investigated on the functional events linked to NK3 receptor activation by using Chinese hamster ovary (CHO) cells transfected with the human NK3 receptor. Radioligand binding conducted with [125I]iodohistidyl-[MePhe7]-NKB revealed a competitive inhibition by SR142801 and its (-)-antipode SR142806 with Ki values of 0.21 +/- 0.03 and 32.0 +/- 5.0 nM, respectively. NK3 agonists such as [MePhe7]-NKB and senktide stimulated inositol monophosphate formation with EC50 values of 2.0 +/- 1.4 and 2.1 +/- 0.7 nM, respectively. SR142801 antagonized the stimulatory effect of [MePhe7]-NKB (10(-8) M) with an IC50 of 14.3 +/- 2.6 nM and of senktide (10(-8) M) with an IC50 of 4.8 +/- 1.5 nM. The [3H]arachidonic acid release induced by either [MePhe7]-NKB (EC50 of 2.6 +/- 0.2 nM) or senktide (EC50 of 4.2 +/- 2.9 nM) also was inhibited by SR142801 with IC50 values of 16.1 +/- 0.5 and 8.0 +/- 1.7 nM, respectively. The cyclic AMP accumulation induced by 10(-7) M [MePhe7]-NKB (EC50 of 54 +/- 2 nM) also was antagonized by SR142801 with an IC50 value of 4.0 +/- 0.7 nM. These antagonistic effects were stereospecific and NK3 receptor specific because the (-)-antipode, SR142806, was much less effective than SR142801 in NK3 agonist-evoked responses, whereas the nonpeptide NK1 (SR140333) and NK2 (SR48968) receptor antagonists were almost inactive. The activity of SR142801 also was evaluated on the [Ca++]i increase induced by 10(-9) M [MePhe7]-NKB.(ABSTRACT TRUNCATED AT 250 WORDS)

Published
1995

49. Evidence for a common molecular mode of action for chemically distinct nonpeptide antagonists at the neurokinin-1 (substance P) receptor.

Author

Gether, U, Emonds-Alt, X, Brelière, J C, Fujii, T, Hagiwara, D, Pradier, L, Garret, C, Johansen, T E, and Schwartz, T W

Abstract

The molecular mechanism of action of three chemically distinct nonpeptide antagonists, SR 140,333, FK 888, and RP 67,580, was compared with that of the previously characterized compound CP 96,345, using a series of chimeric constructs between their common target, the rat neurokinin (NK)-1 (substance P) receptor, and the homologous nonresponsive NK-3 (NKB) receptor. The ability of all four nonpeptide compounds to displace radiolabeled substance P from the NK-1 receptor and their ability to inhibit the peptide-induced increase in inositol phosphate turnover were critically dependent on structural elements located in an area from the middle of the second extracellular loop through transmembrane segments V and VI to the middle of the third extracellular loop of the NK-1 receptor. Dissection of the domain around the outer part of transmembrane segments V and VI into smaller segments demonstrated that the individual nonpeptide antagonists, in agreement with their distinct chemical structures, were dependent on different subepitopes within the common putative binding domain. Full NK-1-like susceptibility to SR 140,333, FK 888, and CP 96,345 could be transferred to the NK-3 receptor by exchange of transmembrane segments V and VI and adjacent parts with corresponding segments from the NK-1 receptor. For SR 140,333 and CP 96,345, almost the same effect could be achieved by transfer of two discontinuous segments around the top of transmembrane segments V and VI. RP 67,580 shared interaction sites with the other compounds around the top of transmembrane segment VI but appeared also to be dependent on transmembrane segment VII. It is concluded that four nonpeptide antagonists, despite overt chemical differences, appear to block NK-1 receptor function by interacting in distinct ways with a common site located spatially around the outer part of transmembrane segment VI.

Published
1994

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