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The Role of Gstπ Isoform in the Cells Signalling and Anticancer Therapy

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The Role of Gstπ Isoform in the Cells Signalling and Anticancer Therapy European Review for Medical and Pharmacological Sciences 2020; 24: 8537-8550 The role of GSTπ isoform in the cells signalling and anticancer therapy M. ŚCISKALSKA, H. MILNEROWICZ Department of Biomedical and Environmental Analyses, Faculty of Pharmacy, Wroclaw Medical University, Wroclaw, Poland Abstract. – OBJECTIVE: The glutathione Abbreviations S-transferases (GSTs) overexpression in hyper- proliferating tumour cells resistant to chemo- 15d-PGJ2 = 15-detoxy-Δ12,14-prostaglandin J2; AP-1 = therapy was demonstrated. An increased GST-π activator protein 1; ARE = antioxidant response ele- activity weakens the efficacy of anti-cancer ments; ASK1 = apoptosis signal-regulating kinase-1; drugs by promoting their efflux from cells. ATP = adenosine-5’-triphosphate; CPIC = p-chlorophe- MATERIALS AND METHODS: This review sum- nyl isocyanate; GSH = reduced glutathione; GST = glu- marises available information on the physiological tathione S-transferase; GSTπ = π izoform of glutathione role of GSTs, in particular the role of GST-π, in reg- S-transferase; JNK = c-Jun N-terminal kinases; Keap1 ulation of signalling pathways mechanisms and = Kelchlike ECH-associated protein 1; MAPK = mito- cellular homeostasis for understanding and ex- gen-activated protein kinases; MRP = multidrug resis- plaining the basis for GST-π application as a tar- tance related proteins; NBDHEX = 6-(7-nitro-2,1,3-ben- get for anticancer therapy and implications for zoxadiazol-4-ylthio) hexanol; NFкB = nuclear factor clinical practice. kappa-light-chain-enhancer of activated B cells; Nrf2 = RESULTS: GST-π can weaken the effect of TNF nuclear factor erythroid 2-related factor 2; PAO = phe- receptor-associated factor 2 (TRAF2) on apop- nylarsine oxide; PPARs = peroxisome proliferator-ac- tosis signal-regulating kinase-1 by inactivation tivated receptors; Prdx6 = peroxiredoxin-6; SN-38 = of MAP kinase pathways (c-Jun N-terminal, p38 irinotecan hydrochloride; STAT3 = signal transducer kinases). GST-π is involved in the metabolism and activator of transcription 3; TLK199 = ezatiostat of endogenous lipids mediators, such as 15-de- hydrochloride; TNF = tumour necrosis factor; TRAF2 = toxy-Δ12,14-prostaglandin J2 (15d-PGJ2). Reduced TNF receptor-associated factor 2. binding of 15d-PGJ2 to peroxisome proliferator-ac- tivated receptors accompanied by GST-π can re- sult in the inhibition of apoptosis. GSTP1 RNA is able to increase the phosphorylation of signal Introduction transducer and activator of transcription 3, what results in negative regulation as regards tran- scriptional activity thereof and affects the growth Glutathione S-transferase (GST, EC 2.5.1.18) is factor signalling. However, the oxidation of GST-π a superfamily of protein enzymes widely distrib- results in inhibition of TRAF2-GST-π complexes uted in nature — from bacteria to animals1,2. So formation and unblocks cell apoptosis. The inhi- far, seven classes of GST have been detected and bition of multidrug resistance related proteins 1 (MRP-1) promoter activity and impairment of MRP- described in the mammalian cytoplasm, name- 1 function can also act as a potent non-competi- ly: GSTA (alfa;α), GSTM (mu;μ), GSTP (pi;π), tive inhibitor of GST-π. GSTS (sigma;σ), GSTT (theta;θ), GSTZ (zeta;ζ), CONCLUSIONS: GST-π is recognised as an im- GSTO (omega;ω)3-5. GST isoforms present in the portant target in designing new anticancer drugs. cellular mitochondria, nucleus, peroxisomes, cell These drugs are often substrates for GST-π or have membrane are also known4,6. It is proven that the the affinity with its structure, what results in weak- ening its activity and achieving therapeutic goal. microsomal GSTs, also named as membrane-as- sociated proteins, that are involved in eicosanoid Key Words: and glutathione metabolism (MAPEG), consti- Structure of glutathione S-transferase isoforms, Cat- tute integral membrane proteins which are not alytic activity, Reduced glutathione, Reactive Oxy- 7 gen Species (ROS) inactivation, S-glutathionylation of evolutionary related to the other major classes . drugs, Anticancer therapy, Signalling pathways. The GST gene family is encoded by genes grouped into chromosome clusters2. Five genes Corresponding Authors: Milena Ściskalska, Ph.D; e-mail: [email protected] Halina Milnerowicz, Ph.D; e-mail: [email protected] 8537 M. Ściskalska, H. Milnerowicz coding isoenzymes of GST-α (GSTA 1-5) and tive and nitrosative stress, and may be involved GST-μ (GSTM 1-5 ) classes were defined, which in synthesis or modification of leukotrienes and are located in chromosome 6 and 1, respectively8. prostaglandins7,17. Some of them are characterised The GST-θ class is coded by three genes named by the activity of glutathione peroxidase, thiol GSTT1, GSTT2 (gene/pseudogen) and GSTT2B transferase and even isomerase7,18. Furthermore, (gene/pseudogen), which are located on chromo- GST performs chaperones functions4 and have some 228. GST-σ, GST-ζ and GST-π classes are the ability, like ligandins, to bind non-substrates coded by a single gene located on chromosomes compounds, such as heme, bilirubin, steroids, 9, 14 and 11, respectively2-4,6,9,10, while the GST-ω free fatty acids, thyroid hormones19. GST is in- class – by two genes (GSTO1 and GSTO2) locat- volved in regulation of nitric oxide (NO) path- ed on chromosome 105. ways4. In addition, some GST isoforms may The primary function of GST is to catalyse perform non-enzymatic functions by regulating the coupling reaction of reduced glutathione cellular signalling pathways3,7,9. (γ-Glu-Cys-Gly, GSH) with electrophilic carbon, In many studies, it was observed that the sulphur or nitrogen atoms to create many non-po- GST family members, in particular GST-π, are lar and hydrophobic organic compounds, includ- expressed abundantly in tumour cells and can ing carcinogens, chemotherapeutics and envi- promote carcinogenesis20-25. This review sum- ronmental xenobiotics3,6,8,9,11. GST has the ability marises available information on the physiologi- to deprotonise and reduce GSH that lowers the cal role of GSTs, in particular the role of GST-π, pKa value of its thiol group9,12. This process al- in regulation of signalling pathways mechanisms lows to form a highly nucleophilic thiolate anion and cellular homeostasis for understanding and (GS-) under physiological conditions, as well as explaining the basis for GST-π application as a thioether bonds between enzyme and detoxified target for anticancer therapy and implications for molecules4,9,13. Hydrophilic GSH conjugates, gen- clinical practice. erated in this way, can be removed from the cell by membrane-bound transport proteins (pumps) The Structure of GST Isoforms belonging to the C protein subfamily binding ad- The structure of each GST isoform is enosine-5’-triphosphate (ATP), such as multidrug formed by a single protein chain composed of resistance related proteins (MRP/ABCC)14. In the 190-244 amino acids6. In the structure of cy- next stage of this reaction, glutamine and glycine tosolic GSTs, two following domains were dis- residues are separated from GSH. The conjugates tinguished: N-terminal domain I and C-ter- formed with cysteine can be returned to the cell, minal domain II, which are bounded togeth- where they are mostly acetylated to form mer- er by a short α-helix with variable length15. capturic acid derivatives. The mercapturic acids The I domain consists of both α-helixes and formation accompanied by GST, is the first step β-folding structures. It comprises the initial ami- for a physiologically important process allowing no acid positions in the polypeptide chain18,26. to excrete endogenous and exogenous electro- Further positions of polypeptide chain form α-he- philic compounds in bile or urine3,7,14-16. However, lixes, which number varies, depending on GST the above-mentioned process does not always class, and they are characteristic of II domain26. result in the inactivation or reduction of harmful The N-terminal domain I has a fairly constant compounds toxicity. It has been shown that as an structure, while the C-terminal domain II is high- increase in toxicity of short-chain alkyl halides ly variable among GST cytosol isoforms18. may be the result of reaction catalysed by GST. It has been shown that each of mammalian cy- After their enzymatic binding to GSH, these tosolic GST may be in the form of a dimer com- compounds can bind to DNA and induce changes posed of two polypeptide chains constituting two in gene expression15. Additionally, GSH activat- subunits of enzyme18. Additionally, depending ed as a thiolate anion, can bind SO-tioperoxols on the number of genes coding the polypeptide (-SOH) in proteins, which contain cysteine resi- chains of GST, the isoenzymes of the same class- dues with low pKa in their structures13,16. es can exist as homodimers or as heterodimers. Except the ability to catalyse coupling of hy- The appearance of heterodimeric forms of this drophobic or electrophilic compounds to endog- enzyme within GST-α and GST-μ classes was enous glutathione, GST performs many different demonstrated6,18,19,27. biological functions. It was reported that some of The balance between monomers and dimeric GST isoforms may protect cells against oxida- form of the enzyme is influenced by electrostatic 8538 The role of GSTπ isoform in the cells signalling and anticancer therapy interactions of amino acid residues included in the case of GST-α, GST-μ, GST-π, GST-σ, serine various subunits28. In the crystal structure of residue – in GST-θ and GST-ζ and cysteine resi- GST, in its dimeric form, two main areas of in- due in active site of GST-ω15,18. These amino acid teraction of dimer building subunits were shown: residues have the ability to react directly with the hydrophobic and electrostatic region28. In GSH thiol group9,18,33. GSTs, a typical hydrophobic contact, which is It was demonstrated that particular amino acid important for inter-subunit communication, con- residues determining the catalytic activity of stitutes “lock and key” motif29.
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