Abstract
Since the discovery of proinsulin, post-translational modification of proteins by limited intracellular proteolysis has been recognized increasingly as a normal biosynthetic mechanism in the production of a wide variety of secretory, along with some viral, proteins. Little is known about the processing mechanisms involved, aside, in a few instances, from their tentative intracellular localization to the Golgi area, and some elements of their cleavage specificity. This chapter presents several interesting recent examples of pro-proteins and discusses the general significance of these formsMost small polypeptide hormones are derived via cleavage of larger precursor molecules. A number of examples are summarized; however, additional suggestive evidence of the existence of larger forms of somatostatin, pancreatic polypeptide, calcitonin, and vasopressin, as well as others is accumulating. These larger forms may fulfill a number of important functions in biosynthesis and secretion; however, a requirement for a minimum chain length of 65–70 residues for successful vectorial discharge and sequestration in the rough endoplasmic reticulum may provide an explanation for the existence of many of them.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Regulatory Proteolytic Enzymes and their Inhibitors
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
