An alternatively processed mRNA specific for γ-glutamyl transpeptidase in human tissues

A. Pawlak, E. H. Cohen, J. N. Octave, R. Schweickhardt, S. J. Wu, F. Bulle, N. Chikhi, Ja-Hyun Baik, S. Siegrist, G. Guellaen

Research output: Contribution to journalArticle

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Abstract

Human γ-glutamyl transpeptidase (GGT) is composed of two subunits derived from a single precursor (Nash, B., and Tate, S.S. (1984) J. Biol. Chem. 259, 678-685; Finidori, J., Laperche, Y., Tsapis, R., Barouki, R., Guellaen, G., and Hanoune, J. (1984) J. Biol. Chem. 259, 4687-4690) consisting of 569 amino acids (Laperche, Y., Bulle, F., Aissani, T., Chobert, M.N., Aggerbeck, M., Hanoune, J., and Guellaen, G. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 937-941). In the present study we report the cloning of an altered form of this precursor from human liver. We have isolated two clones, one 2,632 base pairs (bp) long from a fetal liver cDNA library and one 926 bp long from an adult liver cDNA library, each containing a 22-bp insertion that introduces a premature stop codon and shortens the open reading frame to 1,098 bp when compared with known human cDNA sequences specific for GGT. Sequence analysis of a human genomic GGT clone shows that this insertion of 22 bp is generated by a splicing event involving an alternative 3'-acceptor site. By polymerase chain reaction experiments we demonstrate that the alternatively spliced mRNA is present in polysomes from the microsomal fraction of a human hepatoma cell line (Hep G2) and thus could encode an altered GGT molecule of 39,300 Da (366 amino acids) encompassing most of the heavy subunit which is normally 41,500 Da (380 amino acids). The altered mRNA is detected in various human tissues including liver, kidney, brain, intestine, stomach, placenta, and mammary gland. This report is the first demonstration of an alternative primary sequence in the mRNA coding for GGT, a finding that could be related to the presence of some inactive forms of GGT detected in human tissues.

Original languageEnglish
Pages (from-to)3256-3262
Number of pages7
JournalJournal of Biological Chemistry
Volume265
Issue number6
Publication statusPublished - 1990 Mar 23
Externally publishedYes

Fingerprint

gamma-Glutamyltransferase
Liver
Tissue
Base Pairing
Messenger RNA
Gene Library
Amino Acids
Cloning
Polymerase chain reaction
Clone Cells
Brain
Demonstrations
Complementary DNA
Cells
Polyribosomes
Nonsense Codon
Hep G2 Cells
Molecules
Human Mammary Glands
Placenta

ASJC Scopus subject areas

  • Biochemistry

Cite this

Pawlak, A., Cohen, E. H., Octave, J. N., Schweickhardt, R., Wu, S. J., Bulle, F., ... Guellaen, G. (1990). An alternatively processed mRNA specific for γ-glutamyl transpeptidase in human tissues. Journal of Biological Chemistry, 265(6), 3256-3262.

An alternatively processed mRNA specific for γ-glutamyl transpeptidase in human tissues. / Pawlak, A.; Cohen, E. H.; Octave, J. N.; Schweickhardt, R.; Wu, S. J.; Bulle, F.; Chikhi, N.; Baik, Ja-Hyun; Siegrist, S.; Guellaen, G.

In: Journal of Biological Chemistry, Vol. 265, No. 6, 23.03.1990, p. 3256-3262.

Research output: Contribution to journalArticle

Pawlak, A, Cohen, EH, Octave, JN, Schweickhardt, R, Wu, SJ, Bulle, F, Chikhi, N, Baik, J-H, Siegrist, S & Guellaen, G 1990, 'An alternatively processed mRNA specific for γ-glutamyl transpeptidase in human tissues', Journal of Biological Chemistry, vol. 265, no. 6, pp. 3256-3262.
Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F et al. An alternatively processed mRNA specific for γ-glutamyl transpeptidase in human tissues. Journal of Biological Chemistry. 1990 Mar 23;265(6):3256-3262.
Pawlak, A. ; Cohen, E. H. ; Octave, J. N. ; Schweickhardt, R. ; Wu, S. J. ; Bulle, F. ; Chikhi, N. ; Baik, Ja-Hyun ; Siegrist, S. ; Guellaen, G. / An alternatively processed mRNA specific for γ-glutamyl transpeptidase in human tissues. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 6. pp. 3256-3262.
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AU - Bulle, F.

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