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. 1987 Jun 1;244(2):465–469. doi: 10.1042/bj2440465

Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C.

N M Hooper 1, M G Low 1, A J Turner 1
PMCID: PMC1148013  PMID: 2822007

Abstract

Renal dipeptidase (dehydropeptidase-I, EC 3.4.13.11) was released from pig kidney membrane preparations by treatment with phosphatidylinositol-specific phospholipase C from Staphylococcus aureus and Bacillus thuringiensis and a phospholipase C preparation from Bacillus cereus to a similar extent as alkaline phosphatase. Endopeptidase-24.11 and aminopeptidase N were not released by this treatment. After treatment of the membrane fraction with the S. aureus phospholipase C the dipeptidase was converted from an amphipathic to a hydrophilic form, as deduced from phase-separation experiments in Triton X-114. It is concluded that renal dipeptidase is anchored to the microvillar membrane by covalently attached phosphatidylinositol.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem. 1981 Feb 25;256(4):1604–1607. [PubMed] [Google Scholar]
  2. Ferguson M. A., Low M. G., Cross G. A. Glycosyl-sn-1,2-dimyristylphosphatidylinositol is covalently linked to Trypanosoma brucei variant surface glycoprotein. J Biol Chem. 1985 Nov 25;260(27):14547–14555. [PubMed] [Google Scholar]
  3. Fulcher I. S., Pappin D. J., Kenny A. J. The N-terminal amino acid sequence of pig kidney endopeptidase-24.11 shows homology with pro-sucrase-isomaltase. Biochem J. 1986 Nov 15;240(1):305–308. doi: 10.1042/bj2400305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Futerman A. H., Low M. G., Michaelson D. M., Silman I. Solubilization of membrane-bound acetylcholinesterase by a phosphatidylinositol-specific phospholipase C. J Neurochem. 1985 Nov;45(5):1487–1494. doi: 10.1111/j.1471-4159.1985.tb07217.x. [DOI] [PubMed] [Google Scholar]
  5. He H. T., Barbet J., Chaix J. C., Goridis C. Phosphatidylinositol is involved in the membrane attachment of NCAM-120, the smallest component of the neural cell adhesion molecule. EMBO J. 1986 Oct;5(10):2489–2494. doi: 10.1002/j.1460-2075.1986.tb04526.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kahan F. M., Kropp H., Sundelof J. G., Birnbaum J. Thienamycin: development of imipenen-cilastatin. J Antimicrob Chemother. 1983 Dec;12 (Suppl 500):1–35. doi: 10.1093/jac/12.suppl_d.1. [DOI] [PubMed] [Google Scholar]
  7. Kenny A. J., Maroux S. Topology of microvillar membrance hydrolases of kidney and intestine. Physiol Rev. 1982 Jan;62(1):91–128. doi: 10.1152/physrev.1982.62.1.91. [DOI] [PubMed] [Google Scholar]
  8. Kim H. S., Campbell B. J. Association of renal dipeptidase with the Triton-insoluble fraction of kidney microvilli. J Membr Biol. 1983;75(2):115–122. doi: 10.1007/BF01995631. [DOI] [PubMed] [Google Scholar]
  9. Kropp H., Sundelof J. G., Hajdu R., Kahan F. M. Metabolism of thienamycin and related carbapenem antibiotics by the renal dipeptidase, dehydropeptidase. Antimicrob Agents Chemother. 1982 Jul;22(1):62–70. doi: 10.1128/aac.22.1.62. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Low M. G. Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors. Biochem J. 1987 May 15;244(1):1–13. doi: 10.1042/bj2440001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Low M. G., Finean J. B. Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C. Biochem J. 1977 Oct 1;167(1):281–284. doi: 10.1042/bj1670281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Low M. G., Kincade P. W. Phosphatidylinositol is the membrane-anchoring domain of the Thy-1 glycoprotein. Nature. 1985 Nov 7;318(6041):62–64. doi: 10.1038/318062a0. [DOI] [PubMed] [Google Scholar]
  14. Malik A. S., Low M. G. Conversion of human placental alkaline phosphatase from a high Mr form to a low Mr form during butanol extraction. An investigation of the role of endogenous phosphoinositide-specific phospholipases. Biochem J. 1986 Dec 1;240(2):519–527. doi: 10.1042/bj2400519. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Matsas R., Stephenson S. L., Hryszko J., Kenny A. J., Turner A. J. The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N. Biochem J. 1985 Oct 15;231(2):445–449. doi: 10.1042/bj2310445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Medof M. E., Walter E. I., Roberts W. L., Haas R., Rosenberry T. L. Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid. Biochemistry. 1986 Nov 4;25(22):6740–6747. doi: 10.1021/bi00370a003. [DOI] [PubMed] [Google Scholar]
  17. Stieger A., Cardoso de Almeida M. L., Blatter M. C., Brodbeck U., Bordier C. The membrane-anchoring systems of vertebrate acetylcholinesterase and variant surface glycoproteins of African trypanosomes share a common antigenic determinant. FEBS Lett. 1986 Apr 21;199(2):182–186. doi: 10.1016/0014-5793(86)80476-8. [DOI] [PubMed] [Google Scholar]
  18. Taguchi R., Asahi Y., Ikezawa H. Purification and properties of phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis. Biochim Biophys Acta. 1980 Jul 14;619(1):48–57. [PubMed] [Google Scholar]
  19. Takesue Y., Yokota K., Nishi Y., Taguchi R., Ikezawa H. Solubilization of trehalase from rabbit renal and intestinal brush-border membranes by a phosphatidylinositol-specific phospholipase C. FEBS Lett. 1986 May 26;201(1):5–8. doi: 10.1016/0014-5793(86)80560-9. [DOI] [PubMed] [Google Scholar]

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