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Effect of methyl mercaptan on synthesis and degradation of collagen
Author(s) -
Johnson P.,
Yaegaki K.,
Tonzetich J.
Publication year - 1996
Publication title -
journal of periodontal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.31
H-Index - 83
eISSN - 1600-0765
pISSN - 0022-3484
DOI - 10.1111/j.1600-0765.1996.tb00499.x
Subject(s) - procollagen peptidase , hydroxyproline , extracellular , chemistry , proline , intracellular , fibroblast , biochemistry , type i collagen , gel electrophoresis , microbiology and biotechnology , in vitro , amino acid , biology , endocrinology
Measurements of the conversion of [ 14 C]‐proline to [ 14 C]‐hydroxyproline were employed to assess the effect of methyl mercaptan on intra‐ and extracellular metabolism of collagenous proteins in human gingival fibroblast cultures. Following a 30‐min pulse, 10 ng of methyl mercaptan per ml of 95% air/5% CO 2 , headspace suppressed collagen synthesis by 39% and increased the intracellular degradation of newly synthesized collagen from 26% to 42%. Parallel cultures assayed for proline transport demonstrated a 29% inhibition of [ 14 C]‐proline uptake. A similar analysis of cultures exposed to methyl mercaptan for 12 h revealed an increase in intracellular degradation (20% control vs. 30% test) and a marked increase in extracellular collagenolysis (4% control vs. 55% test). While pulsing, collagen synthesis was decreased by 39%. Slab gel electrophoresis also demonstrated that treatment with methyl mercaptan caused reductions both in mature a, and α 2 chains of type I collagen and in type III procollagen. Identities of the procollagen species were confirmed by pepsin digestion. Reverse transcribed polymerase chain reaction was utilized to compare expression of a1 chains of type I procollagen with type III procollagen and indicated suppression of mRNA synthesis for type III procollagen in cultures exposed to methyl mercaptan.