Recombinant human renin produced in different expression systems: biochemical properties and 3D structure

Protein Expression and Purification
S MathewsW Fischli

Abstract

Human renin has been expressed in Sf9 and CHO cells using two different gene constructs. The first construct contained a foreign signal peptide fused directly to the sequence encoding mature renin, whereas the second construct harbors the sequence for preprorenin. Prorenin was produced in significantly higher amounts than the mature enzyme expressed without its propeptide in both expression systems. Both directly expressed mature renin and proteolytically derived active renin have been purified and cocrystallized with the renin inhibitor Ro 42-5892. The 3D structure has been solved for both versions and demonstrates identity despite different glycosylation and different N termini.

Citations

Jun 5, 2002·The Journal of Clinical Investigation·Genevieve NguyenJean-Daniel Sraer
Jan 11, 2007·Bioscience, Biotechnology, and Biochemistry·Tsutomu NakagawaYukio Nakamura
Oct 12, 2007·Bioscience, Biotechnology, and Biochemistry·Saori TakahashiTakeshi Gotoh
Nov 30, 2006·Protein Expression and Purification·Martin J ScottSteve L Martin
Apr 28, 2000·European Journal of Biochemistry·V Schauer-VukasinovicT Giller
Jul 14, 1999·Journal of Hypertension·P J AdmiraalM A Schalekamp
Dec 22, 1999·Journal of Cardiovascular Pharmacology·O ValdenaireW Fischli
Aug 8, 1998·The Journal of Biological Chemistry·A P Gimenez-RoqueploX Jeunemaitre
Dec 14, 2001·The Journal of Biological Chemistry·Fiona Grüninger-LeitchHeinz Döbeli

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