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Csobán-Szabó Z, Bécsi B, El Alaoui S, et al. Biochemical Characterisation of Human Transglutaminase 4. Int J Mol Sci. 2021;22(22)doi: 10.3390/ijms222212448.
Csobán-Szabó, Z., Bécsi, B., El Alaoui, S., Fésüs, L., Korponay-Szabó, I. R., & Király, R. (2021). Biochemical Characterisation of Human Transglutaminase 4. International journal of molecular sciences, 22(22), . https://doi.org/10.3390/ijms222212448
Csobán-Szabó, Zsuzsa, et al. "Biochemical Characterisation of Human Transglutaminase 4." International journal of molecular sciences vol. 22,22 (2021). doi: https://doi.org/10.3390/ijms222212448
Csobán-Szabó Z, Bécsi B, El Alaoui S, Fésüs L, Korponay-Szabó IR, Király R. Biochemical Characterisation of Human Transglutaminase 4. Int J Mol Sci. 2021 Nov 18;22(22). doi: 10.3390/ijms222212448. PMID: 34830327; PMCID: PMC8619550.
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Int J Mol Sci. 2021 Nov 18;22(22). doi: 10.3390/ijms222212448.

Biochemical Characterisation of Human Transglutaminase 4.

International journal of molecular sciences

Zsuzsa Csobán-Szabó, Bálint Bécsi, Saïd El Alaoui, László Fésüs, Ilma Rita Korponay-Szabó, Róbert Király

Affiliations

  1. Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
  2. Molecular Cell and Immunobiology Doctoral School, University of Debrecen, 4032 Debrecen, Hungary.
  3. Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
  4. Research Department, Covalab S.A.S., 69500 Bron, France.
  5. Department of Pediatrics, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

PMID: 34830327 PMCID: PMC8619550 DOI: 10.3390/ijms222212448

Abstract

Transglutaminases are protein-modifying enzymes involved in physiological and pathological processes with potent therapeutic possibilities. Human TG4, also called prostate transglutaminase, is involved in the development of autoimmune and tumour diseases. Although rodent TG4 is well characterised, biochemical characteristics of human TG4 that could help th e understanding of its way of action are not published. First, we analysed proteomics databases and found that TG4 protein is present in human tissues beyond the prostate. Then, we studied in vitro the transamidase activity of human TG4 and its regulation using the microtitre plate method. Human TG4 has low transamidase activity which prefers slightly acidic pH and a reducing environment. It is enhanced by submicellar concentrations of SDS suggesting that membrane proximity is an important regulatory event. Human TG4 does not bind GTP as tested by GTP-agarose and BODIPY-FL-GTPγS binding, and its proteolytic activation by dispase or when expressed in AD-293 cells was not observed either. We identified several potential human TG4 glutamine donor substrates in the AD-293 cell extract by biotin-pentylamine incorporation and mass spectrometry. Several of these potential substrates are involved in cell-cell interaction, adhesion and proliferation, suggesting that human TG4 could become an anticancer therapeutic target.

Keywords: TG4; TGp; database reanalysis; enzyme activity; prostate cancer; protein crosslinking; proteomic analysis; substrate search; tissue distribution; transglutaminase

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