Title:The Catalytic Activity of GSTM1 In vitro is Independent of MAPK8
Volume: 14
Issue: 3
Author(s): Shannon Robin, Khalil Ben Hassine, Simona Jurkovic Mlakar, Vid Mlakar, Marc Ansari*Chakradhara Rao S. Uppugunduri*
Affiliation:
- CANSEARCH Research Platform in Pediatric Oncology and Hematology, Department of Pediatrics, Gynecology and
Obstetrics, University of Geneva, Geneva, Switzerland
- Division of Pediatric Oncology and Hematology, Department
of Women, Child and Adolescent, University Geneva Hospitals, Geneva, Switzerland
- CANSEARCH Research Platform in Pediatric Oncology and Hematology, Department of Pediatrics, Gynecology and
Obstetrics, University of Geneva, Geneva, Switzerland
Keywords:
Mitogen-activated protein kinase 8 (MAPK8), glutathione s-transferase mu-1 (GSTM1), protein-protein interaction, GST enzyme assay, CDNB, inhibition.
Abstract: Background: Glutathione S-transferases (GSTs) are phase II metabolic enzymes crucial
for the metabolism of electrophilic drugs. Additionally, several GST isoforms are involved in protein-
protein interaction with mitogen-activated protein kinases (MAPKs), modulating apoptosis
pathways.
Methods: To assess the potential change of enzymatic activity, we performed a GST enzyme assay
with human recombinant GSTM1 in the presence and absence of MAPK8. Recently, GSTM1 has
been demonstrated to interact with MAPK8 both in silico and in vitro. The binding interface predicted
in silico comprised amino acid residues present on the surface of the protein and a few were
deep in the active site of the protein.
Results: The experiment demonstrated that the GSTM1 activity was conserved even in the presence
of MAPK8 in the assay.
Conclusion: The possible alteration in the activity of MAPK8 in this interaction needs to be evaluated
in further experiments.
