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M Gaudry

Publications and source records attributed to M Gaudry.

46 records · Page 3Linked to original sources
PubMed1982

Biotin transport by a biotin-deficient strain of Escherichia coli.

Biotin uptake has been investigated using an Escherichia coli biotin requiring auxotroph grown under biotin-deficient conditions. This strain accumulated biotin in the free and bound form. In agreement with a previous report by O. Prakash and M.A. Eisenberg (J. Bacteriol. 120 (1974) 785-791), the biotin entry proved to be an active process which depended on an energy source and was inhibited in the presence of uncouplers. The kinetic parameters have been determined (KM = 0.05 microM, Vmax = 7 pmol/min per mg dry weight). The pool of free biotin could be readily exchanged with external biotin and decreased to a very low level in the absence of an energy source. The use of several biotin analogues revealed that this transport system was quite specific for biotin: slight modifications, for instance in the valeric chain, lowered drastically the affinity for the carrier.

Biological Transport, Active↗
PubMed1981

Effect of reduced vitamin K esters on vitamin K-dependent carboxylation.

The hypothesis of a vitamin K hydroquinone hemicarbonate as intermediate of vitamin K-dependent carboxylation of glutamic residues, has been examined, by testing several vitamin K hydroquinone esters as inhibitors of the reaction. Among the esters that have been synthetized, a monoacetate proved to be an inhibitor. Kinetic analysis shows that the inhibition is no competitive with respect to vitamin K.

Animals↗
PubMed1980

Mechanism of the antibiotic action of alpha-dehydrobiotin.

alpha-Dehydrobiotin, a naturally occurring biotin analogue, exhibits antibiotic properties [Hanka, L. J., Reineke, L. M., & Martin, D. G.(1969) J. Bacteriol. 100, 42--46]. It is shown in this paper that in addition to its activity as corepressor of the transcription of the biotin locus [Guha, A., Saturen, Y., & Szybalski, W. (1971) J. Mol. Biol. 56, 53--62] alpha-dehydrobiotin acts at the enzyme level. The synthesis of specifically tritiated alpha-dehydrobiotin has been achieved. By use of this labeled compound and a biotin-department strain of Escherichia coli, it has been demonstrated that alpha-dehydrobiotin can be linked covalently to proteins without further transformation. The fixation of biotin to apocarboxylases is inhibited irreversibly after preincubation with alpha-dehydrobiotin. This strongly supports the hypothesis that alpha-dehydrobiotin can be specifically linked to apocarboxylases in place of biotin and leads to carboxylases that are inactive. Thus, the antibiotic properties of alpha-dehydrobiotin would be partly due to the fact that it compete with biotin for the fixation on the apocarboxylases, producing irreversibly inactive enzymes.

Biological Transport↗
PubMedDate not supplied

A comparison of the priming effect of phorbol myristate acetate and phorbol dibutyrate on fMet-Leu-Phe-induced oxidative burst in human neutrophils.

Phorbol esters such as phorbol myristate acetate (PMA) and phorbol dibutyrate (PDBU) are generally considered to have similar effects through a similar mechanism, i.e. protein kinase C (PKC) activation. We recently suggested that this was not the case in human neutrophils. To identify further differences between the two phorbol esters, we compared their priming effects on fMet-Leu-Phe-induced superoxide anion (O2-) production, cytosolic PKC activity and binding of fMet-Leu-Phe. Priming could be initiated with a low (0.2 nM) concentration of both PDBU and PMA. Their effects on the pattern of fMet-Leu-Phe-induced superoxide production were similar in both Ca2(+)-containing and Ca2(+)-free medium. PDBU, like PMA, abolished the Ca2+ dependency of fMet-Leu-Phe-induced O2- production in a dose-dependent manner. In cytochalasin B-treated cells and in the presence of Ca2+, priming with PDBU or PMA did not alter the enhancing effect of cytochalasin B on fMet-Leu-Phe-induced O2- production. In Ca2(+)-free medium, priming abolished the Ca2+ dependency of fMet-Leu-Phe stimulation in cytochalasin B-treated cells. Cytochalasin B, however, enhanced the effect of PMA but not that of PDBU. Priming with PDBU was not associated under any experimental conditions with a decrease in cytosolic PKC activity, or an increase in PKM activity before or after fMet-Leu-Phe stimulation. Furthermore, priming effects were abolished by cell washing but not by H-7 or staurosporine, which are potent PKC inhibitors. PDBU, in contrast to PMA, increased fMet-Leu-Phe binding to PMNs through a decrease in the dissociation constant and induced degranulation of specific granules as measured by the release of vitamin B12 binding protein. These findings show that the priming effects of PDBU differ in certain respects from those of PMA, namely with regard to its synergism with cytochalasin B and the expression of fMet-Leu-Phe receptors. In addition, priming concentrations of PDBU, like PMA, did not alter cytosolic PKC activity in fMet-Leu-Phe-stimulated neutrophils.

Cells, Cultured↗
PubMedDate not supplied

Dissimilarities in superoxide anion production by human neutrophils stimulated by phorbol myristate acetate or phorbol dibutyrate.

Phorbol 12-myristate 13-acetate (PMA) and phorbol 12,13-dibutyrate (PDBU) are known to translocate protein kinase C (PKC) and to induce superoxide anion (O2-.) production in human neutrophils. They are thus currently used to probe the role of PKC in O2-. production. We show here that under certain conditions, O2-. production induced by PMA is not associated with a decrease in cytosolic PKC activity, whereas these two events are associated after PDBU stimulation. (1) In the presence of extracellular calcium (1 mM), O2-. production was related to the concentration of PMA. PMA induced O2-. production at all the concentrations studied, but this was not associated with a decrease in cytosolic PKC levels up to 5 ng/ml PMA (50% maximum O2-. production). (2) Under PDBU stimulation, even at very low O2-. production levels, cytosolic PKC decreased and the decrease as well as the O2-. production were related to the concentration of PDBU. (3) For a given decrease in cytosolic PKC, O2-. production induced by PMA was much greater than that induced by PDBU. (4) In calcium-free medium, O2-. production induced by low concentrations of PMA (up to 5 ng/ml) was lower than that observed in the presence of 1 mM calcium, whereas modifications of cytosolic PKC activity were similar. (5) Cytochalasin B had no effect on PMA-induced O2-. production, regardless of the calcium content of the medium, and had no effect on the decrease in cytosolic PKC. On the contrary, following PDBU stimulation, cytochalasin B increased O2-. production, regardless of the medium, but induced a larger decrease in cytosolic PKC when Ca2+ was present. (6) Preincubation of PMN with 100 microM H-7 (1-(5-isoquinolinylsulfonyl)-2-methylpiperazine) before stimulation with PMA or PDBU led to similar inhibition of O2-. production whatever the degree of decrease in cytosolic PKC activity. These findings show that, in contrast to PDBU, O2-. production induced by PMA is not always related to cytosolic PKC activity.

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗