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Proteases and posttranslational processing of prohormones: a review
Canadian Journal of Biochemistry and Cell Biology = Revue Canadienne De Biochimie Et Biologie Cellulaire
|July 1, 1983
Summary
Biologically active peptides, like peptide hormones, originate from larger precursor proteins. This process involves enzymatic cleavage at specific amino acid sites, primarily within secretory granules.
Area of Science:
- Biochemistry
- Molecular Biology
- Endocrinology
Background:
- The 1967 hypothesis proposed that peptide hormones derive from larger precursors via enzymatic cleavage.
- Numerous hormones, active peptides, and neuropeptides are now known to be processed from precursor proteins.
- This posttranslational maturation is established across diverse organisms and tissues, but the responsible enzymes remain unidentified.
Purpose of the Study:
- To review current knowledge on the intracellular processing of precursor molecules.
- To focus on the conversion of prohormones to active hormones.
- To discuss evidence regarding the location, cleavage sites, and potential enzymes involved in this maturation.
Main Methods:
- Review of existing scientific literature and established hypotheses.
- Analysis of evidence concerning the localization of peptide processing.
- Examination of the role of basic amino acid pairs in cleavage.
- Discussion of potential enzyme classes involved in prohormone maturation.
Main Results:
- Peptide hormones and active peptides are derived from larger precursor proteins.
- Cleavage occurs at basic amino acid pairs, predominantly within secretory granules.
- Serine and/or thiol endopeptidases are implicated as potential processing enzymes.
Conclusions:
- The posttranslational processing of precursor molecules into active peptides is a fundamental biological mechanism.
- Secretory granules are key sites for this maturation process.
- Further research is needed to identify the specific enzymes responsible for prohormone conversion.