Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1982 Jul;79(14):4295–4297. doi: 10.1073/pnas.79.14.4295

Tissue-specific expression of mRNAs for dipeptidyl carboxypeptidase isoenzymes.

H A El-Dorry, C B Pickett, J S MacGregor, R L Soffer
PMCID: PMC346657  PMID: 6289298

Abstract

The molecular weight of newly synthesized dipeptidyl carboxypeptidase (angiotensin-converting enzyme; peptidyldipeptide hydrolase, EC 3.4.15.1) polypeptide primed in a reticulocyte lysate by poly(A)-containing RNA from mature rabbit testis was only about 65% that of the immunologically related species programmed by pulmonary RNA. Furthermore, in contrast to the pulmonary RNA-dependent product, the synthesis of this testicular protein was not directed by RNA from testes of immature animals. These findings indicate that a shorter polypeptide chain and pubertal expression--the structural and regulatory properties that distinguish the testicular dipeptidyl carboxypeptidase isozyme--are determined pretranslationally.

Full text

PDF
4295

Images in this article

4296Image
on p.4296
4296Image
on p.4296

Selected References

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

  1. Alt F. W., Bothwell A. L., Knapp M., Siden E., Mather E., Koshland M., Baltimore D. Synthesis of secreted and membrane-bound immunoglobulin mu heavy chains is directed by mRNAs that differ at their 3' ends. Cell. 1980 Jun;20(2):293–301. doi: 10.1016/0092-8674(80)90615-7. [DOI] [PubMed] [Google Scholar]
  2. Caldwell P. R., Seegal B. C., Hsu K. C., Das M., Soffer R. L. Angiotensin-converting enzyme: vascular endothelial localization. Science. 1976 Mar 12;191(4231):1050–1051. doi: 10.1126/science.175444. [DOI] [PubMed] [Google Scholar]
  3. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  4. Cushman D. W., Cheung H. S. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem Pharmacol. 1971 Jul;20(7):1637–1648. doi: 10.1016/0006-2952(71)90292-9. [DOI] [PubMed] [Google Scholar]
  5. Das M., Hartley J. L., Soffers R. L. Serum angiotensin-converting enzyme. Isolation and relationship to the pulmonary enzyme. J Biol Chem. 1977 Feb 25;252(4):1316–1319. [PubMed] [Google Scholar]
  6. Das M., Soffer R. L. Pulmonary angiotensin-converting enzyme antienzyme antibody. Biochemistry. 1976 Nov 16;15(23):5088–5094. doi: 10.1021/bi00668a022. [DOI] [PubMed] [Google Scholar]
  7. Early P., Rogers J., Davis M., Calame K., Bond M., Wall R., Hood L. Two mRNAs can be produced from a single immunoglobulin mu gene by alternative RNA processing pathways. Cell. 1980 Jun;20(2):313–319. doi: 10.1016/0092-8674(80)90617-0. [DOI] [PubMed] [Google Scholar]
  8. Hagenbüchle O., Tosi M., Schibler U., Bovey R., Wellauer P. K., Young R. A. Mouse liver and salivary gland alpha-amylase mRNAs differ only in 5' non-translated sequences. Nature. 1981 Feb 19;289(5799):643–646. doi: 10.1038/289643a0. [DOI] [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. MANS R. J., NOVELLI G. D. A convenient, rapid and sensitive method for measuring the incorporation of radioactive amino acids into protein. Biochem Biophys Res Commun. 1960 Nov;3:540–543. doi: 10.1016/0006-291x(60)90171-6. [DOI] [PubMed] [Google Scholar]
  11. Maccecchini M. L., Rudin Y., Blobel G., Schatz G. Import of proteins into mitochondria: precursor forms of the extramitochondrially made F1-ATPase subunits in yeast. Proc Natl Acad Sci U S A. 1979 Jan;76(1):343–347. doi: 10.1073/pnas.76.1.343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ng K. K., Vane J. R. Conversion of angiotensin I to angiotensin II. Nature. 1967 Nov 25;216(5117):762–766. doi: 10.1038/216762a0. [DOI] [PubMed] [Google Scholar]
  13. Patchett A. A., Harris E., Tristram E. W., Wyvratt M. J., Wu M. T., Taub D., Peterson E. R., Ikeler T. J., ten Broeke J., Payne L. G. A new class of angiotensin-converting enzyme inhibitors. Nature. 1980 Nov 20;288(5788):280–283. doi: 10.1038/288280a0. [DOI] [PubMed] [Google Scholar]
  14. Pelham H. R., Jackson R. J. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur J Biochem. 1976 Aug 1;67(1):247–256. doi: 10.1111/j.1432-1033.1976.tb10656.x. [DOI] [PubMed] [Google Scholar]
  15. Polsky-Cynkin R., Fanburg B. L. Immunochemical comparison of angiotensin 1 converting enzymes from different rat organs. Int J Biochem. 1979;10(8):669–674. doi: 10.1016/0020-711x(79)90210-6. [DOI] [PubMed] [Google Scholar]
  16. Rogers J., Early P., Carter C., Calame K., Bond M., Hood L., Wall R. Two mRNAs with different 3' ends encode membrane-bound and secreted forms of immunoglobulin mu chain. Cell. 1980 Jun;20(2):303–312. doi: 10.1016/0092-8674(80)90616-9. [DOI] [PubMed] [Google Scholar]
  17. Ryan J. W., Ryan U. S., Schultz D. R., Whitaker C., Chung A. Subcellular localization of pulmonary antiotensin-converting enzyme (kininase II). Biochem J. 1975 Feb;146(2):497–499. doi: 10.1042/bj1460497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Singer P. A., Singer H. H., Williamson A. R. Different species of messenger RNA encode receptor and secretory IgM mu chains differing at their carboxy termini. Nature. 1980 May 29;285(5763):294–300. doi: 10.1038/285294a0. [DOI] [PubMed] [Google Scholar]
  19. Soffer R. L., Reza R., Caldwell P. R. Angiotensin-converting enzyme from rabbit pulmonary particles. Proc Natl Acad Sci U S A. 1974 May;71(5):1720–1724. doi: 10.1073/pnas.71.5.1720. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Young R. A., Hagenbüchle O., Schibler U. A single mouse alpha-amylase gene specifies two different tissue-specific mRNAs. Cell. 1981 Feb;23(2):451–458. doi: 10.1016/0092-8674(81)90140-9. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES