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Effects of various chelating agents, quinones, diazoheterocyclic compounds and other substances on proline hydroxylation and synthesis of collagenous and non-collagenous proteins

1967; Elsevier BV; Volume: 140; Issue: 2 Linguagem: Inglês

10.1016/0005-2795(67)90474-6

1878-1454

Miloš Chvapil, J Hurych, E. Ehrlichová, B Cmuchalová,

Prostate Cancer Treatment and Research

The effect of metal chelating agents on [14C]proline hydroxylation and [14C]-proline incorporation into collagenous and non-collagenous proteins in chick embryo skin slices varies according to the substance studied. α,α′-Dipyridyl (0.1–1 mM) and sodium diethyldithiocarbamate (1 mM) block proline hydroxylation and lead to the formation of a typical hydroxyproline-deficient collagen containing approximately twice as much proline as normal collagen. 1,10-Phenanthroline in 0.1–0.05 mM concentrations inhibits the hydroxylation of proline and the proline incorporation into collagen by 50%; it has no effect on the specific activity of proline in non-collagenous proteins. EDTA, d-penicillamine and metopiron in 1 mM concentrations do not affect the three above-mentioned reactions. Glycine, cysteine, methionine and 8-hydroxyquinoline as well as quinones (1,4-benzo-, 1,2-naphtho-) and other oxidation-reduction substances (glutathione, cytochrome c) inhibit all three reactions to the same extent in relation to the dose. An attempt is made to correlate some physicochemical parameters of diazoheterocyclic compounds (e.g. dipyridyl) with their biological reactivity. A hypothesis is proposed for specific inhibition of proline hydroxylation by some agent assuming the intracellular complexing of Fe2+ enzymes. The finding of two differing sensitives, namely of collagenous and non-collagenous proline, to the action of 1,10-phenanthroline favours the concept of differing metabolic pathways in the synthesis of both groups of proteins. This finding could be the basis for selective inhibition of collagen synthesis.