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Biosynthesis of a renin binding protein
K Fukoshi1, H Inoue, S Takahashi
1Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka, Japan.
Biochemical and Biophysical Research Communications
|October 16, 1989
Summary
Porcine renin binding protein (RnBP) is synthesized in kidney tissues and binds to renin, forming an inactive complex. This protein is conserved across mammalian species and doesn't require further processing after synthesis.
Area of Science:
- Biochemistry
- Molecular Biology
- Physiology
Background:
- Renin binding protein (RnBP) forms an inactive complex with renin, influencing its activity.
- Understanding RnBP biosynthesis is crucial for comprehending renin-angiotensin system regulation.
Purpose of the Study:
- To investigate the biosynthesis of porcine renin binding protein (RnBP).
- To determine the tissues responsible for RnBP synthesis and its molecular characteristics.
- To examine the cross-species conservation of RnBP synthesis.
Main Methods:
- In vitro protein synthesis using mRNA from various porcine tissues.
- Immunological detection of RnBP synthesized in vivo.
- Molecular weight determination of synthesized and purified RnBP.
- Cross-species mRNA analysis using human and rat kidney mRNA.
Main Results:
- Porcine kidney mRNA strongly directed RnBP synthesis in vitro.
- Significant levels of RnBP were also synthesized from liver, adrenal, and pituitary gland mRNA.
- In vitro and in vivo synthesized RnBP shared a molecular weight of 42,000 Da.
- Human and rat kidney mRNA also directed the synthesis of a protein recognized by anti-porcine RnBP antibody.
Conclusions:
- RnBP is synthesized in renin-producing tissues, such as the kidney, at its mature size.
- RnBP binds to renin without requiring proteolytic processing.
- The synthesis and structure of RnBP are conserved across mammalian species.