In vitro translation and processing of rat kidney gamma-glutamyl transpeptidase.

Nash, Barbara; Tate, Suresh S.

doi:10.1016/s0021-9258(17)43715-x

Cited by 77 publications

(8 citation statements)

References 48 publications

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“…It is known that kidney GGT is normally sequestered in the brane. The relatively late cleavage of the transpeptidase precursor in the post-translational processing of the enzyme may therefore serve to prevent degradation of GSH in the cytoplasm [32]. It has been claimed that the catalytic function of GGT is influenced by its inner core structure, which determines the number of branches of peroxidation would in part contribute to lower the renal content of the tripeptide.…”

Section: Discussionmentioning

confidence: 99%

Contribution of γ glutamyl transpeptidase to oxidative damage of ischemic rat kidney

Cutrìn

Zingaro

Camandola

et al. 2000

Kidney International

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Ex vivo data supporting a net pro-oxidant effect of up-regulated GGT during short-term ischemia of rat kidney have been obtained. The enzyme stimulation appears to contribute to the renal morphological damage exerted by a brief hypoxic condition at the level of PT cells. The actual impact on kidney function by GGT-dependent oxidative damage during transient ischemia and the potential protective action of GGT inhibitors require subsequent investigation.

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Section: Discussionmentioning

confidence: 99%

Contribution of γ glutamyl transpeptidase to oxidative damage of ischemic rat kidney

Cutrìn

Zingaro

Camandola

et al. 2000

Kidney International

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“…In the presence of membranes, a major band of Mr ~62 000 was produced, consistent with the full-length propeptide of 568 residues. In vitro translation of yGT from rat renal poly(A+) RNA is totally dependent on the presence of membranes (Nash & Tate, 1984). Apparently, the signal sequence of the nascent yGT binds the endogenous lysate signal recognition particle (SRP) which would specifically arrest yGT translation.…”

Section: Isolation and Characterization Of Cdnas Representing Thementioning

confidence: 99%

“…Bands of slower mobility from M, 65 000-75 000 are consistent with N-linked glycosylation of the propeptide by the membranes. Dog pancreas membranes do exhibit a very low level of the protease activity which cleaves the yGT propeptide (Nash & Tate, 1984). Thus, the bands at lower molecular weight could represent cleavage of the propeptide to the large (40 000-50 000 Da) and small I I (25 000-30 000 Da) subunits, both with and without N-linked glycosylation, respectively.…”

Section: Isolation and Characterization Of Cdnas Representing Thementioning

confidence: 99%

Expression of rat renal .gamma.-glutamyltranspeptidase in LLC-PK1 cells as a model for apical targeting

Altman¹,

Orr²,

Lagenaur³

et al. 1993

Biochemistry

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In the rat, gamma-glutamyltranspeptidase (gamma GT) is transcribed into four unique mRNAs from a single gene by use of at least three different promoters and alternative splicing. For the first time, two distinct full-length cDNAs encoding the protein for rat renal gamma-glutamyltranspeptidase have now been isolated. Characterization by restriction enzyme mapping and nucleotide sequencing indicates that the two cDNAs, corresponding to transcripts I and II, differ only in the 5' noncoding region. However, transcription from promoter I, most proximal to the coding sequence, apparently began 20 bases upstream from the major transcription start previously reported. Since in vitro transcription and translation of these two new gamma GT cDNAs were found to produce a full-length peptide (M(r) approximately 62,000), both cDNAs were used to transfect LLC-PK1 (porcine) cells, a polarized cell line most representative of the renal proximal tubule. Rat gamma GT was expressed in transfected cells as judged by immunofluorescence analysis, direct immunoprecipitation after metabolic labeling with [35S]methionine, and an increase in gamma GT specific enzymatic activity (up to 5-fold). When clonal cell lines (I or II) were grown on Falcon filter inserts, the increased gamma GT activity was found only at the apical surface, consistent with polarized expression of the rat gamma GT. In contrast, transfection of the same cells with cDNA of human growth hormone resulted in both apical (70%) and basal lateral (30%) secretion of the expressed hormone.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…The enzyme γ-glutamyl transpeptidase (GGT; E.C.2.3.3.2) is conserved throughout all three domains of life, ranging from single-celled prokaryotes to multicellular higher eukaryotes (Rawlings et al, 2010). It belongs to the N-terminal nucleophile hydrolase superfamily and exists as a heterodimer of a large and a small subunit (Nash and Tate, 1984;Suzuki et al, 1989;Brannigan et al, 1995). It is a two-substrate enzyme catalyzing the transfer of γ-glutamyl moiety from donor substrates, such as glutathione/glutamine, to an acceptor substrate, which can be water (hydrolysis) or other amino acids/small peptides (transpeptidation) or the donor itself (autotranspeptidation) (Thompson and Meister, 1977;Tate and Meister, 1981).…”

Section: Introductionmentioning

confidence: 99%

Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure–Function Relationship and Its Biotechnological Applications

et al. 2021

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Gamma-glutamyl transpeptidase (GGT) enzyme is ubiquitously present in all life forms and plays a variety of roles in diverse organisms. Higher eukaryotes mainly utilize GGT for glutathione degradation, and mammalian GGTs have implications in many physiological disorders also. GGTs from unicellular prokaryotes serve different physiological functions in Gram-positive and Gram-negative bacteria. In the present review, the physiological significance of bacterial GGTs has been discussed categorizing GGTs from Gram-negative bacteria like Escherichia coli as glutathione degraders and from pathogenic species like Helicobacter pylori as virulence factors. Gram-positive bacilli, however, are considered separately as poly-γ-glutamic acid (PGA) degraders. The structure–function relationship of the GGT is also discussed mainly focusing on the crystallization of bacterial GGTs along with functional characterization of conserved regions by site-directed mutagenesis that unravels molecular aspects of autoprocessing and catalysis. Only a few crystal structures have been deciphered so far. Further, different reports on heterologous expression of bacterial GGTs in E. coli and Bacillus subtilis as hosts have been presented in a table pointing toward the lack of fermentation studies for large-scale production. Physicochemical properties of bacterial GGTs have also been described, followed by a detailed discussion on various applications of bacterial GGTs in different biotechnological sectors. This review emphasizes the potential of bacterial GGTs as an industrial biocatalyst relevant to the current switch toward green chemistry.

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In vitro translation and processing of rat kidney gamma-glutamyl transpeptidase.

Cited by 77 publications

References 48 publications

Contribution of γ glutamyl transpeptidase to oxidative damage of ischemic rat kidney

Contribution of γ glutamyl transpeptidase to oxidative damage of ischemic rat kidney

Expression of rat renal .gamma.-glutamyltranspeptidase in LLC-PK1 cells as a model for apical targeting

Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure–Function Relationship and Its Biotechnological Applications

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