PMID: 9160964Apr 24, 1997Paper

Ontogeny of prohormone convertases in rat prenatal development

Annals of the New York Academy of Sciences
M Zheng, J E Pintar

Abstract

It has been well established that peptide precursors usually undergo limited proteolysis at pairs or single basic amino acids during their biosynthetic process. This posttranslational modification paradigm is common for numerous membrane-spanning and secreted proteins, neuropeptides, and peptide hormones of physiological significance, in which endoproteolytic cleavage is invariably essential for the accurate biosynthesis and full activity of the mature products. Establishment of an effective peptide profile is dependent on not only the presence of peptide precursor, but also the presence and the enzymatic specificities of cleavage enzymes. We have, therefore, characterized the spatial and temporal patterns of six subtilisin-like serine endoproteases known to be involved in proprotein processing, including furin, PC1, PC2, PC4, PC5, and PACE4, in rat prenatal development and related the results to the expression patterns of several peptide precursors. We have observed largely distinct and sometimes complementary expression patterns of individual PCs in various embryonic structures, suggesting PCs may be functionally distinct in processing different sets of proprotein substrates in development. From these studies, numerous tentat...Continue Reading

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Citations

Apr 1, 2009·General and Comparative Endocrinology·Michael G MorashYounes Anini
Nov 5, 2003·Journal of Neuroscience Research·Traci A CzyzykJohn E Pintar
Mar 30, 2001·The Journal of Biological Chemistry·L UlloaS Tabibzadeh

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