Recombinant Human Renin Produced in Different Expression Systems: Biochemical Properties and 3D Structure

Mathews, Salima; Döbeli, Heinz; Pruschy, Martin; Bosser, Ramon; D’Arcy, Allan; Oefner, Christian; Zulauf, M.; Gentz, Reiner; Breu, Volker; Matile, Hugues; Schlaeger, Jürgen; Fischli, Walter

doi:10.1006/prep.1996.0012

Cited by 23 publications

(13 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, we used transgenic rats with a high overexpression of human Aogen 22 to study the formation of Ang peptides at the level of the vascular wall and in the circulation. We infused human recombinant renin and prorenin generated by Chinese hamster ovary cells, 23 which show similar properties with respect to molecular weight, kinetic activity, activation and immunological characteristics, and binding to a Cibacron blue affinity column compared with human plasma and renal inactive renin. 24 Our study focused on acute effects.…”

Section: Discussionmentioning

confidence: 99%

“…Enzyme-kinetic renin measurements were performed without remikiren. Purified human recombinant renin and prorenin produced in a Chinese hamster ovary expression system 23 were infused for 15 and 20 minutes, respectively. Human recombinant prorenin always exhibited a small active renin contamination; therefore, we used the term "total renin."…”

Section: Hindlimb Perfusionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of Human Prorenin in Rats Transgenic for Human Angiotensinogen

Müller

Hilgers²,

Mathews³

et al. 1999

Hypertension

Self Cite

View full text Add to dashboard Cite

Abstract-The physiological role of prorenin is unknown; however, the possibility that prorenin inhibits renin locally has been suggested. We tested the hypothesis that prorenin may be an endogenous competitor for renin uptake in the tissue. We also investigated whether prorenin can be activated to active renin and affect mean arterial pressure (MAP). Isolated perfused hindquarters of rats transgenic for human angiotensinogen were infused with human renin and/or prorenin. The plateau phase of angiotensin (Ang) I release 15 minutes after cessation of infusions was used as a parameter for renin uptake. Renin (10 ng/mL for 15 minutes) caused sustained release of Ang I (153Ϯ16 fmol/mL). Coinfusion with a 15-fold excess of prorenin did not affect local Ang I formation (153Ϯ19 fmol/mL). Prorenin infusion alone showed no activation to active renin. In addition, we investigated MAP and plasma Ang II levels after injection of saline (⌬MAP, Ϫ1Ϯ2 mm Hg; 40Ϯ5 fmol/mL Ang II), 9 ng renin (⌬MAP, ϩ37Ϯ3 mm Hg; 378Ϯ39 fmol/mL), and 144 ng prorenin (⌬MAP, ϩ10Ϯ5 mm Hg; 61Ϯ5 fmol/mL) and the coinjection of renin and prorenin (⌬MAP, ϩ41Ϯ4 mm Hg; 305Ϯ23 fmol/mL) in anesthetized rats. The data show that prorenin was not activated to active renin and did not affect MAP in short-term experiments. Renin-induced Ang formation was not affected by prorenin. Renin may have been taken up specifically because of its physical and chemical properties or because of nonspecific sequestration in the extravascular space. We conclude that prorenin does not act as an endogenous antagonist for the long-lasting effects of renin in the vascular wall. Moreover, prorenin does not affect acute renin-related effects on blood pressure.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Hindlimb Perfusionmentioning

confidence: 99%

Effects of Human Prorenin in Rats Transgenic for Human Angiotensinogen

Müller

Hilgers²,

Mathews³

et al. 1999

Hypertension

Self Cite

View full text Add to dashboard Cite

show abstract

“…6) Production and purification of recombinant human prorenin and renin in mammal and insect cells has been reported by several groups. [7][8][9][10][11] The purification strategies that they undertook either include many complicated chromatographic steps or require special affinity chromatography using a specific antibody for prorenin or a specific inhibitor for renin. This might have prevented other researchers from working in detail with the enzyme.…”

Section: Efficient Production Of Recombinant Human (Pro)renin Utilizimentioning

confidence: 99%

Efficient Production of Recombinant Human (Pro)renin Utilizing a Decahistidine Tag Attached at the C-Terminus

Nakagawa

Nishiuchi

Akaki

et al. 2007

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

“…Human recombinant renin, prorenin (27), and the polyclonal Ab to human renin were a gift of Walter Fischli (Hoffmann-La Roche Ltd., Basel, Switzerland). The polyclonal Ab to Ang I was a gift from Jean-Baptiste Michel (INSERM U460, Paris, France).…”

Section: Methodsmentioning

confidence: 99%