Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 71, 2007 - Issue 5
Journal homepage
71
Views
4
CrossRef citations to date
0
Altmetric
Original Articles

Ser84 of Human Renin Contributes to the Biphasic pH Dependence of the Renin-Angiotensinogen Reaction

Hideyuki IWATAUnited Graduate School of Agricultural Science, Gifu University
,
Tsutomu NAKAGAWALaboratory of Applied Biochemistry, Faculty of Applied Biological Science, Gifu University
,
Kazuhiro NISHIUCHILaboratory of Applied Biochemistry, Faculty of Applied Biological Science, Gifu University
,
Tomoaki HIRATSUKALaboratory of Applied Biochemistry, Faculty of Applied Biological Science, Gifu University
,
Ryousuke SATOUUnited Graduate School of Agricultural Science, Gifu University
,
Yuichiro YOSHIOKALaboratory of Applied Biochemistry, Faculty of Applied Biological Science, Gifu University
,
Youko FUKUILaboratory of Applied Biochemistry, Faculty of Applied Biological Science, Gifu University
,
Fumiaki SUZUKILaboratory of Animal Biochemistry, Faculty of Applied Biological Science, Gifu University
&
Yukio NAKAMURALaboratory of Applied Biochemistry, Faculty of Applied Biological Science, Gifu University
 show all
Pages 1279-1285 | Received 04 Dec 2006, Accepted 24 Feb 2007, Published online: 22 May 2014

  • 1) Auffret, C. A., and Ryle, A. P., The catalytic activity of pig pepsin C towards small synthetic substrates. Biochem. J., 179, 239–246 (1979).
  • 2) Barth, R., and Afting, E. G., Cathepsin D from pig myometrium: characterization of the proteinase. Biochem. J., 219, 899–904 (1984).
  • 3) Meek, D. T., Catalytic mechanisms of the aspartic proteinases. In “Comprehensive Biological Catalysis,” ed. Sinnott, M., Academic Press, New York, pp. 327–344 (1998).
  • 4) Yokosawa, H., Holladay, L. A., Inagami, T., Haas, E., and Murakami, K., Human renal renin. J. Biol. Chem., 255, 3498–3502 (1980).
  • 5) Pilote, L., Mckercher, G., Thibeault, D., and Lamarre, D., Enzymatic characterization of purified recombinant human renin. Biochem. Cell Biol., 73, 163–170 (1995).
  • 6) Dzau, J. V., Brenner, A., and Emmett, L. N., Evidence for renin in rat brain: differentiation from other renin-like enzymes. Am. J. Physiol., 242, E292–297 (1982).
  • 7) Haward, B. R., Pucell, G. A., Merlin Bumpus, F., and Husain, A., Rat ovarian renin: characterization and changes during the estrous cycle. Endocrinology, 123, 2331–2340 (1988).
  • 8) Yukimura, T., Miura, K., Matsushima, Y., Ikemoto, F., and Yamamoto, K., Urinary extraction of renin and its biochemical properties in dogs. Hypertension, 6, 837–842 (1984).
  • 9) Nasir, U. M., Takahashi, K., Nagai, T., Nakagawa, T., Suzuki, F., and Nakamura, Y., Two peaks in pH dependence of renin-angiotensinogen reaction. Biosci. Biotechnol. Biochem., 62, 338–340 (1998).
  • 10) Nasir, U. M., Suzuki, F., Nagai, T., Nakagawa, T., and Nakamura, Y., Tyrosine-83 of human renin contributes to biphasic pH dependence of the renin-angiotensinogen reaction. Biosci. Biotechnol. Biochem., 63, 1143–1145 (1999).
  • 11) Green, D. W., Aykent, S., Gierse, J. K., and Zupec, M. E., Substrate specificity of recombinant human renal renin: effect of histidine in the P2 subsite on pH dependence. Biochemistry, 29, 3126–3133 (1990).
  • 12) Yamauchi, T., Nagahama, M., Hori, H., and Murakami, K., Functional characterization of Asp-317 mutant of human renin expressed in COS cells. FEBS Lett., 230, 205–208 (1988).
  • 13) Dhanaraj, V., Dealwis, C. G., Frazao, C., Badasso, M., Sibanda, B. L., Tickle, I. J., Cooper, J. B., Driessen, H. P. C., Newman, M., Aguilar, C., Wood, S. P., Blundell, T. L., Hobart, P. M., Geoghegan, K. F., Ammirati, M. J., Danley, D. E., O’Connor, B. A., and Hoover, D. J., X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature, 357, 466–472 (1992).
  • 14) Dealwis, C. G., Frazao, C., Badasso, M., Cooper, J. B., Tickle, I. J., Driessen, H., Blundell, T. L., Murakami, K., Miyazaki, H., Sueiras-Diaz, J., Jones, D. M., and Szelke, M., X-ray analysis at 2.0 Å resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4–16 fragment of rat angiotensinogen. J. Mol. Biol., 236, 342–360 (1994).
  • 15) Nakagawa, T., Nishiuchi, K., Akaki, J., Iwata, H., Satou, R., Suzuki, F., and Nakamura, Y., Efficient production of recombinant human (pro)renin utilizing a decahistidine tag attached at the C-terminus. Biosci. Biotechnol. Biochem., 71, 256–260 (2007).
  • 16) Nabi, A. H. M. N., Kageshima, A., Uddin, M. N., Nakagawa, T., Park, E. Y., and Suzuki, F., Binding properties of rat prorenin and renin to the recombinant rat renin/prorenin receptor prepared by a baculovirus expression system. Int. J. Mol. Med., 18, 483–488 (2006).
  • 17) Nagase, M., Suzuki, F., Sawai, Y., Orihashi, T., Inui, Y., Nakagawa, T., and Nakamura, Y., Purification and some properties of recombinant sheep angiotensinogen expressed in Chinese hamster ovary cells. Biomed. Res., 18, 439–443 (1997).
  • 18) Suzuki, F., Yamashita, S., Takahashi, A., Ito, M., Miyazaki, S., Nagata, Y., and Nakamura, Y., Highly sensitive microplate-ELISA for angiotensin I using 3,3′,5,5′-tetramethylbenzidine. Clin. Exp. Hypertens., 12, A83–A95 (1990).
  • 19) Guex, N., and Peitsch, M. C., SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714–2723 (1997).
  • 20) Tong, L., Pav, S., Lamarre, D., Pilote, L., LaPlante, S., Anderson, P. C., and Jung, G., High resolution crystal structures of recombinant human renin in complex with polyhydroxymonoamide inhibitors. J. Mol. Biol., 250, 211–222 (1995).
  • 21) Eisenberg, D., Luthy, R., and Bowie, J. U., VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol., 277, 396–404 (1997).
  • 22) Johnson, W. C., and Lindsey, A. J., An improved universal buffer. Analyst, 64, 490–492 (1939).
  • 23) Andreeva, N. S., and Rumsh, L. D., Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes. Protein Sci., 10, 2439–2450 (2001).
  • 24) Mantafounis, D., and Pitts, J., Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis. Protein Eng., 3, 605–609 (1990).
  • 25) Gimenez-Roqueplo, A. P., Celerier, J., Lucarelli, G., Corvol, P., and Jeunemaitre, X., Role of N-glycosylation in human angiotensinogen. J. Biol. Chem., 273, 21232–21238 (1998).
  • 26) Nabi, A. H. M. N., Uddin, M. N., Nakagawa, T., Orihashi, T., Ebihara, A., Iwasawa, A., Nakamura, Y., and Suzuki, F., Roles of His9 (P2 subsite) and His13 (P3′ subsite) in angiotensinogen for catalytic reaction of renin. Int. J. Mol. Med., 16, 103–107 (2005).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.