Characterization of the Methylthioadenosine Phosphorylase Polymorphism rs7023954 - Incidence and Effects on Enzymatic Function in Malignant Melanoma

PLoS One. 2016 Aug 1;11(8):e0160348. doi: 10.1371/journal.pone.0160348. eCollection 2016.

Abstract

Deficiency of methylthioadenosine phosphorylase (MTAP) supports melanoma development and progression through accumulation of its substrate 5'-methylthioadenosine (MTA), which leads amongst others to a constitutive inhibition of protein arginine methyltransferases (PRMTs) and activation of the transcription factor AP-1 via the receptor ADORA2B. Genetic association studies have also suggested that genetic polymorphism in MTAP may modulate the risk of melanoma. Here, we investigated the only globally common non-synonymous single nucleotide polymorphism (SNP) reported to date for MTAP. The SNP rs7023954 is located in exon 3 (c.166G>A), and leads to the conservative substitution of one branched-chain amino acid residue (valine) for another (isoleucine) at position 56 (p.Val56Ile). Whereas genotype frequencies in normal and primary melanoma tissues or cell lines were in Hardy-Weinberg equilibrium based on cDNA amplicon sequencing, a marked (P = 0.00019) deviation was observed in metastatic melanoma tissues and cell lines due to a deficit of heterozygotes. Enzyme assays conducted on the co-dominantly expressed alleles revealed no difference in the conversion rate of MTA to adenine and 5-methylthioribose-1-phosphate, indicating that this known enzymatic activity does not modulate the tumor suppressive function of MTAP.

MeSH terms

  • Alleles
  • Enzyme Activation / genetics
  • Exons
  • Gene Frequency
  • Genetic Association Studies
  • Genotype
  • Humans
  • Incidence
  • Kinetics
  • Melanoma / enzymology*
  • Melanoma / epidemiology
  • Melanoma / genetics*
  • Melanoma / pathology
  • Polymorphism, Single Nucleotide
  • Purine-Nucleoside Phosphorylase / genetics*
  • Purine-Nucleoside Phosphorylase / metabolism
  • RNA / chemistry
  • RNA / isolation & purification
  • RNA / metabolism
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Sequence Analysis, RNA
  • Spectrometry, Mass, Electrospray Ionization
  • Tumor Cells, Cultured

Substances

  • Recombinant Proteins
  • RNA
  • Purine-Nucleoside Phosphorylase
  • 5'-methylthioadenosine phosphorylase

Grants and funding

This work was supported by grants from the Medical Faculty of the University of Regensburg (ReForM) and the German Research Foundation (DFG BO1573, KFO 262), further by BioSysNet and the German Cancer Aid. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.