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A processing enzyme for prorenin in mouse submandibular gland. Purification and characterization
W S Kim1, K Hatsuzawa, Y Ishizuka
1Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
The Journal of Biological Chemistry
|April 15, 1990
Summary
Researchers purified a novel enzyme that converts inactive mouse Ren 2 prorenin into active renin. This specific serine protease, crucial for renin production, differs from other prohormone-processing enzymes.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Renin, a key enzyme in blood pressure regulation, is synthesized as an inactive precursor, prorenin.
- Prorenin activation involves proteolytic cleavage at specific paired basic amino acid residues.
Purpose of the Study:
- To purify and characterize the enzyme responsible for cleaving mouse Ren 2 prorenin.
- To elucidate the enzymatic properties and specificity of this prorenin-converting enzyme.
Main Methods:
- Purification using CM-Toyopearl chromatography, antipain-Sepharose chromatography, and isoelectric focusing.
- Characterization of enzyme structure, isoelectric point, and pH optimum.
- Inhibitor studies to determine enzyme class.
Main Results:
- A novel enzyme, prorenin converting enzyme, was purified from mouse submandibular gland.
- The enzyme consists of 17 and 10 kDa polypeptide chains, with an isoelectric point of 9.5-9.8 and pH optimum of 7.5-8.5.
- It specifically cleaves mouse Ren 2 prorenin at the Lys-Arg site, yielding mature renin, but does not affect mouse Ren 1 or human prorenins. Inhibitor studies suggest it is a serine protease.
Conclusions:
- A unique serine protease specifically processes mouse Ren 2 prorenin.
- This enzyme's distinct substrate specificity differentiates it from other prohormone convertases.
- The findings provide insights into the regulation of renin production and potential therapeutic targets.