Publication | Closed Access
Inhibition of procollagen cell-free synthesis by amino-terminal extension peptides
117
Citations
27
References
1979
Year
Peptide EngineeringCytoskeletonAmino-terminal Extension PeptidesCellular PhysiologyProtein SynthesisProtein ExpressionCollagen ChainsProteomicsCollagen ProductionProtein FunctionBiochemistryEndocrinologyCell BiologyProtein BiosynthesisDevelopmental BiologyNatural SciencesPeptide TherapeuticPeptide SynthesisProtein EngineeringCollagen SynthesisCellular BiochemistryMedicineExtracellular Matrix
Peptides prepared from the amino termini of pro alpha 1(I) and pro alpha 1(III) collagen chains inhibit the production of pro alpha 1(I) and pro alpha 2 by rat calvaria rna in a reticulocyte cell-free system. The synthesis of other proteins was not altered, suggesting a specific effect on collagen production. Various peptides from the helical region of the alpha 1(I) chain did not alter translation. These studies, taken together with earlier studies showing inhibition of collagen synthesis by cells in culture receiving the amino-terminal peptides, are consistent with a regulatory function in collagen synthesis for the amino-terminal peptides from procollagen.
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