Search PubMed⌕ Search

Biomedical subjects

V Zappia

Publications and source records attributed to V Zappia.

At least 109 records · Page 6Linked to original sources
PubMed1972

S-adenosylmethionine decarboxylase from human prostate. Activation by putrescine.

1. The presence of S-adenosylmethionine decarboxylase in human prostate gland is reported. A satisfactory radiochemical enzymic assay was developed and the enzyme was partially characterized. 2. Putrescine stimulates the reaction rate by up to 6-fold at pH7.5: the apparent activation constant was estimated to be 0.13mm. The stimulation is pH-dependent and a maximal effect is observed at acid pH values. 3. Putrescine activation is rather specific: other polyamines, such as spermidine and spermine, did not show any appreciable effect. 4. The apparent K(m) for the substrate is 4x10(-5)m. The calculated S-adenosylmethionine content of human prostate (0.18mumol/g wet wt. of tissue) demonstrates that the cellular amounts of sulphonium compound are saturating with respect to the enzyme. 5. The enzyme is moderately stable at 0 degrees C and is rapidly inactivated at 40 degrees C. The optimum pH is about 7.5, with one-half of the maximal activity occurring at pH6.6. 6. Several carboxy-(14)C-labelled analogues and derivatives of S-adenosylmethionine were tested as substrates. The enzyme appears to be highly specific: the replacement of the 6'-amino group of the sulphonium compound alone results in a complete loss of activity. 7. Inhibition of the enzyme activity by several carbonyl reagents suggests an involvement of either pyridoxal phosphate or pyruvate in the catalytic process. 8. The inhibitory effect of thiol reagents indicates the presence of ;essential' thiol groups.

Adenosine↗
PubMedDate not supplied

Effect of an oxidative stress on methionine and S-adenosylmethionine metabolism in cultured bovine eye lens.

The sulphonium compound [Formula: see text] (AdoMet) plays a central role in many metabolic reactions of cellular metabolism, acting both as a propylamine donor in the biosynthesis of polyamines as well as a methyl donor in the transmethylation reactions. Moreover, AdoMet is a key intermediate of the transsulphuration pathway by which methionine is converted into cysteine, a precursor of glutathione. The aim of this study was to investigate the methionine and AdoMet metabolism in bovine lenses cultured in the presence of labelled methionine, upon treatment with H(2)O(2), as the experimental model for studying the molecular mechanisms responsible for the onset of senile cataract. The results reveal that one of the earliest changes following an oxidative stress is a severe impairment of protein synthesis. As far as the synthesis of AdoMet is concerned, a small but significant decrease in the conversion of labelled methionine into AdoMet occurs in treated lenses compared to the controls. In order to verify if the decreased AdoMet synthesis would lead in turn to alterations of methyl transfer reactions, we examined changes in the levels of various macromolecular methylations, such as protein methyl esterification and phospholipid methylation. The data clearly indicate that both the synthesis of AdoMet and the methyl transfer reactions could be significantly affected in eye lens upon an oxidative stress, suggesting that these alterations could be one of the biochemical events related to the ethiology of senile cataract. Finally, the question of whether or not H(2)O(2)-induced alterations of methionine and AdoMet metabolism could, in turn, affect some closely related metabolism, such as glutathione-associated reactions, is also discussed.

Journal Article↗