Dr. Voraratt Champattanachai


voraratt
Name: Dr. Voraratt Champattanachai
Office address: B705A, 7th Floor, Biomedical Science Building
54 Kamphaeng Phet 6 Talat Bang Khen, Lak Si, Bangkok 10210, Thailand
Tel: +66 25530 8555 (ext. 8347 )
E-mail: vorarattResearch Scientist II
Research Interests              My research has been focused on abnormal proteins associated to diseases, mainly in cancer. Cancer is a curable disease if diagnosis is made at the early stage of cancer progression and effective treatments are received in time. Available tumor markers currently used for cancer screening, however, are still not good enough due to lacking for specificity and they might be detected in some healthy people. In addition, although current treatments can inhibit or kill cancer cells at the certain point, they may have side effects against normal cells in the body. Currently, I am working mainly on two cancer research projects.

My first project is to search novel cancer biomarker. This research aims to seek abnormal proteins as well as proteins with post-translational modifications (PTMs) in cancer. Abnormality of PTMs including phosphorylation, glycosylation, and O-GlcNAcylation is one of most important characteristics of cancer hallmarks and they play vital roles in tumor aggressiveness and drug resistances. Finding these abnormal proteins can be applied not only as tumor biomarkers but also as potential targets for cancer treatment. Currently, I am using an advance technology of proteomics-base mass spectrometry, in collaboration with our colleagues, to identify and quantify these abnormal proteins in breast and colorectal cancer, in particular cancer tissues, cell lines, and liquid specimens i.e. plasma and exosomes obtained from patients with cancer.

Another cancer project is to investigate the immune-checkpoint proteins for cancer therapeutics. Some cancer cells have partner proteins that bind to the checkpoint of native immune cells such as macrophages and cytotoxic T cells, inhibiting their functions. Immunotherapy drugs block this binding. We just explored the potential use of inhibitors of CD47/SIRPa and PD-L1/PL-1. Our preliminary results indicate that some breast cancer sub-types showed a good response for these inhibitory effects. In the future, I am planning to test of cancer cells and blood obtained from patients with breast cancer which may apply as an option in personalized medicine for those patients.

Beside cancer, I am interested in inborn errors of metabolism (IEMs). IEMs are rare diseases found in children; however, more than 500 types currently identify around the world. They normally result from defects in a single gene coding for an enzyme in living metabolism. In collaboration with pediatricians and our colleagues, the objective of this research is to reveal unusual inborn errors of metabolism not previously characterized in Thailand and to study the molecular mechanisms by which they lead to their defects as well as to elucidate the correlation between genotype and phenotype of diseases.

Many laboratory techniques are used for these research projects including proteomic 2-D IEF/PAGE, immunoblotting, immunoprecipitation, mass spectrometry, molecular techniques, RNA interference (RNAi), bacterial and mammalian cell culture techniques, HPLC, DNA sequencing, recombinant protein expression, and fluorescent spectrophotometer and microscope.

Education
B.Sc. (Biology), Kasetsart University, Thailand
M.S. (Biochemistry), Mahidol University, Thailand
Ph.D. (Cell Biology), The University of Alabama at Birmingham, U.S.A.

Publications

  1. Effects of gentamicin inducing read through premature stop Codons: A study of alpha-L-iduronidase nonsense variants in COS-7 Cells. Ngiwsara L, Sawangareetrakula P, Wattanasirichaigoonb D, TimAroonb T, Dejkhamronc P, Champattanachaia V, Ketudat-Cairns J, Svasti J. Biochem. Biophys. Res. Commun. 2022;636:147-154.
  2. Verathamjamras C, Sriwitool TE, Netsirisawan P, Chaiyawat P, Chokchaichamnankit D, Prasongsook N, et al. Aberrant RL2 O-GlcNAc antibody reactivity against serum-IgA1 of patients with colorectal cancer. Glycoconjugate journal. 2021;38(1):55-65.
  3. Sawangareetrakul P, Ngiwsara L, Champattanachai V, Chokchaichamnankit D, Saharat K, Ketudat Cairns JR, et al. Aberrant proteins expressed in skin fibroblasts of Parkinson’s disease patients carrying heterozygous variants of glucocerebrosidase and parkin genes. Biomedical reports. 2021;14(4):36.
  4. Ngiwsara L, Vatanavicharn N, Sawangareetrakul P, Liammongkolkul S, Ratanarak P, Boonyawat B, et al. Molecular characterization of Thai patients with phenylalanine hydroxylase deficiency and in vitro functional study of two novel PAH variants. Molecular biology reports. 2021;48(3):2063-70.
  5. Chantaraamporn J, Kongmanee, A, Verathamjamras, C, Chutipongtanate, S Prasongsook, N, Svasti, J, Champattanachai V. Colorectal Cancer Blood-Based Biomarker Discovery: Label-Free Quantitative Proteomics of Glycoproteins Based on Lectin selection. Online Conference of 10th Asia-Oceania Human Proteome Organization Congress, June 30 – July 2, 2021 BEXCO, Busan, Korea. 2021.
  6. Netsirisawan P, Chokchaichamnankit D, Saharat K, Srisomsap C, Svasti J, Champattanachai V. Quantitative proteomic analysis of the association between decreasing OGlcNAcylation and metastasis in MCF7 breast cancer cells. International journal of oncology. 2020;56(6):1387-404.
  7. Lumkul L, Pothipan, P, Svasti,J, Champattanachai, V. Inhibition of CD47 in breast cancer mammospheres enhances phagocytosis through macrophage engulfment. Abstracts and Proceedings: The 15th International Symposium of the Protein Society of Thailand, Convention Center, Chulabhorn Research Institute, Bangkok, Thailand, November 4-6, 2020, PP192-199, ISBN: 978-616-92908-4-1. 2020.
  8. Chantaraamporn J, Champattanachai V, Khongmanee A, Verathamjamras C, Prasongsook N, Mingkwan K, et al. Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer. Proteomes. 2020;8(3).
  9. Bhandari J, Pothipan, P, Ngiwsara, L, Svasti, J, Champattanachai, V. Investigation of PD-1 and PD-L1 interaction in breast cancer cells. The 15th International Symposium of the Protein Society of Thailand, Convention Center, Chulabhorn Research Institute, Bangkok, Thailand, November 4-6, 2020, page 229-236, ISBN: 978-616-92908-4-1 2020.
  10. Weeraphan C, Phongdara A, Chaiyawat P, Diskul-Na-Ayudthaya P, Chokchaichamnankit D, Verathamjamras C, et al. Phosphoproteome Profiling of Isogenic Cancer Cell-Derived Exosome Reveals HSP90 as a Potential Marker for Human Cholangiocarcinoma. Proteomics. 2019;19(12):e1800159.
  11. Ngiwsara L, Wattanasirichaigoon D, Tim-Aroon T, Rojnueangnit K, Noojaroen S, Khongkraparn A, et al. Clinical course, mutations and its functional characteristics of infantile-onset Pompe disease in Thailand. BMC medical genetics. 2019;20(1):156.
  12. Thi Do T, Phoomak C, Champattanachai V, Silsirivanit A, Chaiyarit P. New evidence of connections between increased O-GlcNAcylation and inflammasome in the oral mucosa of patients with oral lichen planus. Clinical and experimental immunology. 2018;192(1):129-37.
  13. Ngiwsara L, Ketudat-Cairns JR, Sawangareetrakul P, Charoenwattanasatien R, Champattanachai V, Kuptanon C, et al. p.X654R IDUA variant among Thai individuals with intermediate mucopolysaccharidosis type I and its residual activity as demonstrated in COS-7 cells. Annals of human genetics. 2018;82(3):150-7.
  14. Netsirisawan P, Chaiyawat P, Chokchaichamnankit D, Lirdprapamongkol K, Srisomsap C, Svasti J, et al. Decreasing O-GlcNAcylation affects the malignant transformation of MCF-7 cells via Hsp27 expression and its O-GlcNAc modification. Oncology reports. 2018;40(4):2193-205.
  15. Verathamjamras C, Weeraphan C, Chokchaichamnankit D, Watcharatanyatip K, Subhasitanont P, Diskul-Na-Ayudthaya P, et al. Secretomic profiling of cells from hollow fiber bioreactor reveals PSMA3 as a potential cholangiocarcinoma biomarker. International journal of oncology. 2017;51(1):269-80.
  16. Ngiwsara L, Rojnueangnit K, Wattanasirichaigoon D, Tim-Aroon T, Sawangareetrakul P, Champattanachai V, et al. Molecular analysis of the novel IDS allele in a Thai family with mucopolysaccharidosis type II: The c.928C>T (p.Gln310*) transcript is sensitive to nonsense-mediated mRNA decay. Experimental and therapeutic medicine. 2017;13(6):2989-96.
  17. Ketudat Cairns JR, Champattanachai V, Srisomsap C, Paricharttanakul NM, Verathamjamras C, Lirdprapamongkol K, et al. Conference report: the 5th Asia Pacific Protein Association Conference joint meeting with the 12th International Symposium of the Protein Society of Thailand. Biophysical reviews. 2017.
  18. Chaiyawat P, Klangjorhor J, Settakorn J, Champattanachai V, Phanphaisarn A, Teeyakasem P, et al. Activation Status of Receptor Tyrosine Kinases as an Early Predictive Marker of Response to Chemotherapy in Osteosarcoma. Translational oncology. 2017;10(5):846-53.
  19. Chaiyawat P, Weeraphan C, Netsirisawan P, Chokchaichamnankit D, Srisomsap C, Svasti J, et al. Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells. Cancer genomics & proteomics. 2016;13(5):387-98.
  20. Sawangareetrakul P, Ketudat Cairns JR, Vatanavicharn N, Liammongkolkul S, Wasant P, Svasti J, et al. Analysis of Novel Mutations and Methylmalonyl-CoA Mutase Levels in Thai Patients with Isolated Methylmalonic Acidemia. Biochemical genetics. 2015;53(11-12):310-8.
  21. Netsirisawan P, Chokchaichamnankit D, Srisomsap C, Svasti J, Champattanachai V. Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion. Cancer genomics & proteomics. 2015;12(4):201-9.
  22. Chaiyawat P, Chokchaichamnankit D, Lirdprapamongkol K, Srisomsap C, Svasti J, Champattanachai V. Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells. Oncology reports. 2015;34(4):1933-42.
  23. Chaiyawat P, Netsirisawan P, Svasti J, Champattanachai V. Aberrant O-GlcNAcylated Proteins: New Perspectives in Breast and Colorectal Cancer. Frontiers in endocrinology. 2014;5:193.
  24. Phueaouan T, Chaiyawat P, Netsirisawan P, Chokchaichamnankit D, Punyarit P, Srisomsap C, et al. Aberrant O-GlcNAc-modified proteins expressed in primary colorectal cancer. Oncology reports. 2013;30(6):2929-36.
  25. Champattanachai V, Netsirisawan P, Chaiyawat P, Phueaouan T, Charoenwattanasatien R, Chokchaichamnankit D, et al. Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer. Proteomics. 2013.
  26. Vatanavicharn N, Champattanachai V, Liammongkolkul S, Sawangareetrakul P, Keeratichamroen S, Ketudat Cairns JR, et al. Clinical and molecular findings in Thai patients with isolated methylmalonic acidemia. Molecular genetics and metabolism. 2012;106(4):424-9.
  27. Charoenwattanasatien R, Cairns JR, Keeratichamroen S, Sawangareetrakul P, Tanpaiboon P, Wattanasirichaigoon D, et al. Decreasing Activity and Altered Protein Processing of Human Iduronate-2-sulfatase Mutations Demonstrated by Expression in COS7 Cells. Biochemical genetics. 2012;50(11-12):990-7.
  28. Champattanachai V NP, Chaiyawat P, Phueaouan T, Charoenwattanasatien R, Chokchaichamnankit D, Punyarit P, Srisomsap C, Svasti J. Alteration of O-GlcNAc proteins Expressed in Breast Malignant Tumors and in vitro: Proteomic Identification and Analysis. Abstract Book: The 11th National Cancer Conference, Rama Garden Hotel, Thailand 2012;March 14-16:133.
  29. Phueaouan T SC, Punyarit P, Svasti J, Champattanachai V. Proteomic studies of O-GlcNAcylation in colon cancer. Abstracts and proceedings, The 5th Annual Symposium of Protein Society of Thailand, Chulabhorn Research Institute, Bangkok, Thailand. 2010;Aug 23-25, 2010:152-7.
  30. Zou L, Yang S, Champattanachai V, Hu S, Chaudry IH, Marchase RB, et al. Glucosamine improves cardiac function following trauma-hemorrhage by increased protein O-GlcNAcylation and attenuation of NF-{kappa}B signaling. American journal of physiology Heart and circulatory physiology. 2009;296(2):H515-23.
  31. Champattanachai V, Marchase RB, Chatham JC. Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein O-GlcNAc and increased mitochondrial Bcl-2. American journal of physiology Cell physiology. 2008;294(6):C1509-20.
  32. Keeratichamroen S, Cairns JR, Sawangareetrakul P, Liammongkolkul S, Champattanachai V, Srisomsap C, et al. Novel mutations found in two genes of thai patients with isolated methylmalonic acidemia. Biochemical genetics. 2007;45(5-6):421-30.
  33. Champattanachai V, Marchase RB, Chatham JC. Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc. American journal of physiology Cell physiology. 2007;292(1):C178-87.
  34. Nagy T, Champattanachai V, Marchase RB, Chatham JC. Glucosamine inhibits angiotensin II-induced cytoplasmic Ca2+ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine. American journal of physiology Cell physiology. 2006;290(1):C57-65.
  35. Ketudat Cairns JR, Keeratichamroen S, Sukcharoen S, Champattanachai V, Ngiwsara L, Lirdprapamongkol K, et al. The molecular basis of mucopolysaccharidosis type I in two Thai patients. The Southeast Asian journal of tropical medicine and public health. 2005;36(5):1308-12.
  36. Champattanachai V, Ketudat Cairns JR, Shotelersuk V, Keeratichamroen S, Sawangareetrakul P, Srisomsap C, et al. Novel mutations in a Thai patient with methylmalonic acidemia. Molecular genetics and metabolism. 2003;79(4):300-2.
  37. Ketudat Cairns JR, Champattanachai V, Srisomsap C, Wittman-Liebold B, Thiede B, Svasti J. Sequence and expression of Thai Rosewood beta-glucosidase/beta-fucosidase, a family 1 glycosyl hydrolase glycoprotein. Journal of biochemistry. 2000;128(6):999-1008.
  38. Srisomsap C, Svasti J, Surarit R, Champattanachai V, Sawangareetrakul P, Boonpuan K, et al. Isolation and characterization of an enzyme with beta-glucosidase and beta-fucosidase activities from Dalbergia cochinchinensis Pierre. Journal of biochemistry. 1996;119(3):585-90.