ScienceDirect® Home Skip Main Navigation Links
You have guest access to ScienceDirect. Find out more.
 
Home
Browse
My Settings
Alerts
Help
 Quick Search
 Search tips (Opens new window)
    Clear all fields    
advertisementadvertisement
FEBS Letters
Volume 269, Issue 2, 3 September 1990, Pages 319-323
 
Font Size: Decrease Font Size  Increase Font Size
 Abstract - selected
PDF (546 K)

 
 
 
Related Articles in ScienceDirect
View More Related Articles
 
View Record in Scopus
 
doi:10.1016/0014-5793(90)81184-P    How to Cite or Link Using DOI (Opens New Window)
Copyright © 1990 Published by Elsevier Science B.V. All rights reserved.

Research letters

Isolation and functional expression of pituitary peptidylglycine α-amidating enzyme mRNA A variant lacking the transmembrane domain

Ichiro Kato, Hideto Yonekura, Hiroshi Yamamoto and Hiroshi OkamotoCorresponding Author Contact Information

Department of Biochemistry, Tohoku University School of Medicine. Sendai 980, Miyagi, Japan

Received 12 June 1990. 
Available online 5 November 2001.

Abstract

We demonstrate that, in rat pituitary, peptidylglycine α-amidating enzyme was encoded by at least 5 distinct mRNAs. Southern blot and ribonuclease protection analyses revealed that the mRNAs arose through alternative splicing. A variant lacking the transmembrane domain-coding sequence was a major mRNA species for the enzyme in the pituitary. When the cDNAs were expressed in COS-7 cells, the variant was the most efficient in producing a secretory form (37 kDA) of the enzyme.

Author Keywords: Peptide α-amidating enzyme; Functional expression; Secretory form; Transmembrane domain; Alternative splicing; mRNA

Abbreviations: kbp, kilobase pairs; bp, base pairs; Hepes, 4(2-hydroxyethyl)-1-piperazineethane sulfonic acid

References

1. T.W. Schwartz In: H. Okamoto, Editor, Molecular Biology of the Islets of Langerhans, Cambridge University Press, Cambridge (1990), pp. 153–205.

2. A.F. Bradbury, M.D. Finnie and D.G. Smyth Nature 298 (1982), pp. 686–688. View Record in Scopus | Cited By in Scopus (102)

3. A.S.N. Murthy, R.E. Mains and B.A. Eipper J. Biol. Chem. 261 (1986), pp. 1815–1822. View Record in Scopus | Cited By in Scopus (23)

4. N.M. Mehta, J.P. Gilligan, B.N. Jones, A.H. Bertelsen, B.A. Roos and R.S. Birnbaum Arch. Biochem. Biophys. 261 (1988), pp. 44–54. Abstract | Article | PDF (1089 K) | View Record in Scopus | Cited By in Scopus (9)

5. V. May, E.I. Cullen, K.M. Braas and B.A. Eipper J. Biol. Chem. 263 (1988), pp. 7550–7554. View Record in Scopus | Cited By in Scopus (12)

6. B.A. Eipper, V. May and K.M. Braas J. Biol. Chem. 263 (1988), pp. 8371–8379. View Record in Scopus | Cited By in Scopus (13)

7. H. Yonekura, K. Nata, T. Watanabe, Y. Kurashina, H. Yamamoto and H. Okamoto J. Biol. Chem. 263 (1988), pp. 2990–2997. View Record in Scopus | Cited By in Scopus (11)

8. B.A. Eipper, L.P. Park, I.M. Dickerson, H.T. Keutmann, E.A Thiele, H. Rodriguez, P.R. Schofield and R.E. Mains Mol. Endocrinol. 1 (1987), pp. 777–790. View Record in Scopus | Cited By in Scopus (24)

9. J. Messing Methods Enzymol. 101 (1983), pp. 20–78. Abstract | Article | PDF (3279 K) | View Record in Scopus | Cited By in Scopus (445)

10. C. Inoue, K. Shiga, S. Takasawa, M. Kitagawa, H. Yamamoto and H. Okamoto Natl. Acad. Sci. USA 84 (1987), pp. 6659–6662. View Record in Scopus | Cited By in Scopus (18)

11. F-T. Liu, K. Albrandt and M.W. Robertson Proc. Natl. Acad. Sci. USA 85 (1988), pp. 5639–5643. View Record in Scopus | Cited By in Scopus (3)

12. S. Subramani, R. Mulligan and P. Berg Mol. Cell. Biol. 1 (1981), pp. 854–864. View Record in Scopus | Cited By in Scopus (45)

13. C. Chen and H. Okayama Mol. Cell. Biol. 7 (1987), pp. 2745–2752. View Record in Scopus | Cited By in Scopus (2998)

14. M. Noguchi, K. Takahashi and H. Okamoto Arch. Biochem. Biophys. 275 (1989), pp. 505–513. Abstract | Article | PDF (784 K) | View Record in Scopus | Cited By in Scopus (5)

15. Heijne G. von Nucleic Acids Res. 14 (1986), pp. 4683–4690.

16. D.A. Stoffers, C.B. Green and B.A. Eipper Proc. Natl. Acad. Sci. USA 86 (1989), pp. 735–739. View Record in Scopus | Cited By in Scopus (46)

17. B.A. Eipper, A.C. Myers and R.E. Mains Endocrinology 116 (1985), pp. 2497–2504. View Record in Scopus | Cited By in Scopus (20)

18. M. Tajima, T. Iida, S. Yoshida, K. Komatsu, R. Namba, M. Yanagi, M. Noguchi and H. Okamoto J. Biol. Chem. (1990) in press. .

19. G.S. Wand, R.L. Ney, R.E. Mains and B.A. Eipper Neuroendocrinology 41 (1985), pp. 482–489. View Record in Scopus | Cited By in Scopus (1)

Corresponding Author Contact Information Correspondence address: H. Okamoto, Department of Biochemistry, Tohoku University School of Medicine, Sendai 980, Miyagi, Japan.


FEBS Letters
Volume 269, Issue 2, 3 September 1990, Pages 319-323
 
Home
Browse
My Settings
Alerts
Help
Elsevier.com (Opens new window)
About ScienceDirect  |  Contact Us  |  Information for Advertisers  |  Terms & Conditions  |  Privacy Policy
Copyright © 2008 Elsevier B.V. All rights reserved. ScienceDirect® is a registered trademark of Elsevier B.V.