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. 1977 Sep;74(9):3647–3651. doi: 10.1073/pnas.74.9.3647

Evidence for pro-β-nerve growth factor, a biosynthetic precursor to β-nerve growth factor

Edward A Berger 1,2,3,*, Eric M Shooter 1,2,3,†
PMCID: PMC431675  PMID: 269420

Abstract

The biosynthesis of β-nerve growth factor (βNGF) was studied in mouse submaxillary glands incubated with L-[35S]cystine. βNGF was isolated from tissue extracts by the addition of antiserum against βNGF and the washed immunoprecipitates were analyzed by sodium dodecyl sulfate gel electrophoresis. With short labeling periods (10 and 25 min) there is a major labeled species with an apparent molecular weight of 22,000 and a smaller peak comigrating with purified βNGF chains (13,260). As time proceeds, the radioactivity in the 22,000 molecular weight peak plateaus, while the label in βNGF continues to increase, until by 4 hr it greatly exceeds the radioactivity of the 22,000 molecular weight species. When glands incubated for 10 min are transferred to medium containing a large excess of unlabeled L-cystine, the 22,000 molecular weight peak gradually declines, and there is a corresponding increase in radioactivity at the βNGF position. The 22,000 molecular weight species isolated from sodium dodecyl sulfate gels possesses all the cystine-containing peptides of βNGF, and possibly two additional ones. When immunoprecipitates from submaxillary glands labeled for 25 min are incubated with the γ subunit (a specific arginyl-esteropeptidase associated with βNGF in the 7S NGF complex), the radioactivity in the 22,000 molecular weight species is converted to the βNGF position. The results suggest that the 22,000 molecular weight species is a biosynthetic precursor to βNGF, and that the γ subunit may function as a specific protease in the processing event.

Keywords: arginyl-esteropeptidase, protein processing, submaxillary gland, gamma subunit, epidermal growth factor

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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