PMID: 8455028Apr 1, 1993Paper

Deletions of the synenkephalin domain which do not alter cell-specific proteolytic processing or secretory targeting of human proenkephalin

Journal of Neurochemistry
P R Albert, D Liston

Abstract

To identify signals that direct the proteolytic processing and regulated secretion of human proenkephalin (hPE), we have transfected the hPE gene or minigene constructs into pituitary tumor cells, either rat GH4Cl cells or mouse AtT-20 cells. Cells transfected with either the hPE gene or minigene contained similar levels of methionine-enkephalin (ME)-containing peptides and hPE mRNA. In the GH4Cl clones, ME was present predominantly in high-molecular-mass forms (5-25 kDa). In contrast, the AtT-20 clones contained almost exclusively free ME and low-molecular-mass forms (< 5 kDa), with very little high-molecular-mass species present. Thus, among pituitary cells, corticotroph-derived cells appear better equipped to process hPE than lactotroph-derived cells. Despite limited proteolytic processing, GH4Cl clones secreted large amounts of unprocessed (> 20 kDa) hPE into the medium, making up to 10% of endogenous rat prolactin secretion. Both precursor and processed forms of ME were cosecreted acutely (< 1 h) with rat prolactin, and release of both polypeptides was stimulated up to 12-fold by secretagogues. Thus, complete proteolytic processing was not required for accurate targeting of hPE to the regulated secretory pathway. When tran...Continue Reading

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Citations

Jun 4, 2020·Molecular Pharmacology·Lloyd D FrickerLakshmi A Devi
Aug 25, 2020·Journal of Neuroscience Research·Alden Y HuangChristopher J Evans

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