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Biomedical subjects

R Michelot

Publications and source records attributed to R Michelot.

25 records · Page 2Linked to original sources
PubMed1979

In vivo release of substance P in the cat substantia nigra.

Push-pull cannuale were implanted into the substantia nigra (SN) and the caudate nucleus (CN) of the cat to study the in vivo release of substance P (SP), using a radioimmunoassay and high pressure liquid chromatography (HPLC) analysis. The spontaneous release of SP could be detected in the SN and the CN. Potassium (50 mM) locally applied stimulated SP release in both structures. Furthermore an important evoked release of SP was observed in the SN during depolarization of striato-nigral SP fibers with potassium (50 mM) applied in the CN.

Animals↗
PubMed1976

[New studies on inhibition of tRNA N2 guanine methyltransferase by S-adenosyl-homocysteine and S-adenosyl-methionine analogs].

New structural analogs of S-adenosyl homocysteine (SAH) 1-9, 11-14, 19-21) and of S-adenosyl methionine (15-18) have been tested as inhibitors of a N-2 guanine methyltransferase extract from rabbit liver with E. coli B tRNA as substrate. The sulfonium compounds (mixture of +/- diastereoisomers) are more inhibitory than the sulfide derivatives but less inhibitory than SAH itself. The replacement of the aminoacid chain in SAH by various alphatic radicals leads to a correlation between their bulk and the size of the enzymatic site. The monosubstitution of N-6 amino group does not affect significantly the inhibitory effect, which is completely canceled by the disubstitution of N-6.

Animals↗
PubMed1976

[New syntheses of S-adenosylhomocysteine and S-adenosylmethionine analogs].

With the aim of studying analogues of S adenosyl homocysteine and S adenosyl methionine as potential inhibitors of methyl-transferases, we describe the syntheses of such analogues, in which either the amino-acid chain is replaced by various aliphatic radicals of the N 6 amino group of adenine is substituted.

Homocysteine↗
PubMedDate not supplied

Design of potent and selective dynorphin A related peptides devoid of supraspinal motor effects in mice.

Dynorphin A-(1-13)-Tyr-Leu-Phe-Asn-Gly-Pro (Dyn Ia) was previously shown to be a highly potent and selective kappa opioid peptide. Four analogs of Dyn Ia are synthesized by the solid-phase procedure, introducing pseudo CH2NH linkage between positions 6 and 7 as follows: analog 1, [6 psi 7 (CH2NH)]Dyn Ia; analog 2, [6 psi 7 (CH2NH), D-Leu8]Dyn Ia; analog 3, [N(Me)-Tyr1, 6 psi 7 (CH2NH)]Dyn Ia; and analog 4, [N(Me)-Tyr1, 6 psi 7 (CH2NH), D-Leu8]Dyn Ia. The purified peptides are compared in vitro with Dyn Ia for their ability to compete with the binding of selective kappa, mu, and delta opioid ligands using membrane preparations of guinea pig cerebellum (kappa) and rat brain (mu and delta). The synthetic compounds are also compared in vivo in mice (intracerebroventricularly administered) for their analgesic activity against acetic acid induced writhing and their ability to produce motor dysfunction. All compounds display a high affinity (Ki = 0.5-1.8 nM) and a good selectivity for the kappa opioid receptor, and their rank order of potency on the kappa site (analog 2 > analog 1 > analog 3 > analog 4) closely parallels their potency (AD50 = 1.57-5 nmol/mouse) in inhibiting acetic acid induced writhing in mice (analog 2 > analog 1 > analog 4 > analog 3). On the other hand, all the synthetic analogs are less potent than Dyn Ia in producing motor effects, analog 2 being the least potent (CD50 = 15.4 nM as compared with 2.9 nM for Dyn Ia).(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗