Conversion of proendothelin-1 into endothelin-1 by aspartylproteases.
The ability of cathepsin D, chymosin, pepsin and renin to produce endothelin-1 (ET-1) from proendothelin-1 (proET-1) was compared. No significant conversion was observed when proET-1 was incubated with up to 1 U of renin for 15 min at 37 degrees C. Cathepsin D generated, as well as degraded, ET-1 rapidly. Net production of ET-1 reached a maximum when 0.003 U of cathepsin D was used, and about 16% of the initial proET-1 was detected as ET-1 by HPLC. Pepsin up to 1 U converted proET-1 into ET-1 dose-dependently with a maximum of 71% conversion. A further increase of the amount of pepsin in the reaction mixture produced nonspecific cleavage of ET-1. Less than 10% of ET-1 remained in the presence of 15 U of pepsin. Chymosin also generated ET-1 dose-dependently, and a complete conversion was obtained at 1 U of enzyme. Greater than 1 U of chymosin only slightly degraded ET-1; at least 80% of ET-1 was still present when 15 U of chymosin was included in the assay. Other properties associated with the conversion of proET-1 into ET-1 by chymosin were investigated. Similar to authentic ET-1, the product of chymosin treatment caused contraction of isolated rabbit aortic rings, and pre-incubation of chymosin with pepstatin A abolished this contractile response.(ABSTRACT TRUNCATED AT 250 WORDS)[1]References
- Conversion of proendothelin-1 into endothelin-1 by aspartylproteases. Savage, P., Shetty, S.S., Martin, L.L., Jeng, A.Y. Int. J. Pept. Protein Res. (1993) [Pubmed]
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