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Tetracyclines inhibit intracellular muscle proteolysis in vitro.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1992 Oct 30; Vol. 188 (2), pp. 767-72. - Publication Year :
- 1992
-
Abstract
- Tetracycline antibiotics (TETs) have a recently discovered novel action: inhibition of extracellular metalloproteinase activity, especially that of collagenase and gelatinase. This property, now confirmed in 8 different laboratories using > 40 tissue sources, includes natural and semi-synthetic TETs as well as a chemically modified TET (CMT) devoid of antimicrobial activity. We have used 14C-Tyr biosynthetically labelled intracellular proteins in L-6 myoblast culture as a test system to assess intracellular proteolysis. Starvation accelerates proteolysis, which can be suppressed by agents such as insulin or serum. Minocycline, doxycycline, and CMT all retarded the rate of intracellular protein degradation in a dose dependent manner. These agents also demonstrated marked synergism with insulin. A CMT derivative (pyrazole) stripped of one of its metal chelation sites and lacking anti-collagenase activity, also lost its antiproteolytic effect. CMT at physiologic concentrations (< or = 5 micrograms/ml) had no effect on protein synthesis, but at 15 micrograms/ml (pharmacologic), a suppressive effect was noted. These findings demonstrate that TETs can inhibit protein degradation as well as synthesis in a mammalian muscle-derived cell line.
- Subjects :
- Animals
Carbon Radioisotopes
Cell Line
Doxycycline pharmacology
Insulin pharmacology
Kinetics
Minocycline pharmacology
Muscles drug effects
Radioisotope Dilution Technique
Recombinant Proteins pharmacology
Tetracycline pharmacology
Tyrosine metabolism
Muscles metabolism
Proteins metabolism
Tetracyclines pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 188
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 1445321
- Full Text :
- https://doi.org/10.1016/0006-291x(92)91122-7