Medical Oncology

, Volume 27, Issue 4, pp 1102–1108 | Cite as

Upregulation of soluble resistance-related calcium-binding protein (sorcin) in gastric cancer

  • Langmei Deng
  • Tao Su
  • Aimin Leng
  • Xiaomei Zhang
  • Meihua xu
  • Lu Yan
  • Huan Gu
  • Guiying ZhangEmail author
Original Paper


The aim of this paper was to identify novel proteins involved in the development of gastric cancer (GC). Isobaric tags for relative and absolute quantification (iTRAQ) analysis was adopted to separate the differentially expressed proteins between normal gastric epithelial cell line GES-1 and GC cell line SGC7901. Western blotting was utilized to validate the increased expression of sorcin in SGC7901; immunohistochemistry was performed to investigate its relationship with clinicopathological features of GC. Twelve differential proteins were identified. Seven proteins were found to be significantly upregulated (≥twofold), while five proteins were markedly downregulated (≤0.5-fold), in SGC7901 cells. Sorcin was detected by this proteomic approach with a 5.4-fold upregulation in SGC7901. Western blotting and immunohistochemistry confirmed the overexpression of sorcin in GC. Immunohistochemistry showed us that sorcin was overexpressed in 55 samples of GC tissue (55/85, 64.71%) and was related closely to the depth of invasion, TNM stage, and lymph node metastasis of GC (P < 0.05). The development of GC is regulated by multiple genes. Sorcin will be a novel molecular biomarker for the diagnosis, treatment, and prognosis of GC.


Gastric cancer Sorcin iTRAQ Mass spectrometry Biomarker 


  1. 1.
    Ohgaki H, Matsukura N. Stomach cancer. In: Stewart BW, Kleihues P, editors. World cancer report. Lyon: IARC Press; 2003. p. 197–207.Google Scholar
  2. 2.
    Roth AD. Curative treatment of gastric cancer: towards a multidisciplinary approach? Crit Rev Oncol Hematol. 2003;46:59–100.PubMedCrossRefGoogle Scholar
  3. 3.
    Ellis DJ, Speirs C, Kingston RD, Brookes VS, Leonard J, Dykes PW. Carcinoembryonic antigen levels in advanced gastric carcinoma. Cancer (Phila.). 1978;42:623–5.CrossRefGoogle Scholar
  4. 4.
    Sikoroska H, Shuster J, Gold P. Clinical application of carcinoembryonic antigen. Cancer Detect Prev. 1988;12:321–55.Google Scholar
  5. 5.
    Ritts R, Del Villano B, Go VL, Herberman RB, Klug TL, Zurawski VR Jr. Initial clinical evaluation of an immunoradiometric assay for CA19-9 using the NCI serum bank. Int J Cancer. 1984;33:339–45.PubMedCrossRefGoogle Scholar
  6. 6.
    Hisamichi S. Screening for gastric cancer. World J Surg. 1989;13:31–7.PubMedCrossRefGoogle Scholar
  7. 7.
    Zhang J, Sui J, Ching CB, Chen WN. Protein profile in neuroblastoma cells incubated with S- and R-enantiomers of ibuprofen by iTRAQ-coupled 2-D LC–MS/MS analysis: possible action of induced proteins on Alzheimer’s disease. Proteomics. 2008;8:1595–607.PubMedCrossRefGoogle Scholar
  8. 8.
    Lu H, Yang Y, Allister EM, Wijesekara N, Wheeler MB. The identification of potential factors associated with the development of type 2 diabetes: a quantitative proteomics approach. Mol Cell Proteomics. 2008;7:1434–51.PubMedCrossRefGoogle Scholar
  9. 9.
    Yokota T, et al. Identification of histological markers for malignant glioma by genome-wide expression analysis dynein a-PIX and sorcin. Acta Neuropathol. 2006;111:29–38.PubMedCrossRefGoogle Scholar
  10. 10.
    Glen A, et al. iTRAQ-facilitated proteomic analysis of human prostate cancer cells identifies proteins associated with progression. J Proteome Res. 2008;7(3):897–907.PubMedCrossRefGoogle Scholar
  11. 11.
    Keshamouni VG, et al. Differential protein expression profiling by iTRAQ- 2DLC-MS/MS of lung cancer cells undergoing epithelial-mesenchymal transition reveals a migratory/invasive phenotype. J Proteome Res. 2006;5:1143–54.PubMedCrossRefGoogle Scholar
  12. 12.
    Armah HB, Parwani AV. Epithelioid sarcoma. Arch Pathol Lab Med. 2009;133(5):814–9.PubMedGoogle Scholar
  13. 13.
    Zheng LD, et al. Gastric carcinoma with osteoclast-like giant cells: a case report and review of the literature. J Zhejiang Univ Sci B. 2009;10(3):237–41.PubMedCrossRefGoogle Scholar
  14. 14.
    Izdebska M, Grzanka A, Ostrowski M. The cytoskeleton reorganization and differentiation of HL-60 and K-562 human leukemia cell lines. Postepy Hig Med Dosw (Online). 2006;60:64–70.Google Scholar
  15. 15.
    Zhang X, Xu W. Aminopeptidase N (APN/CD13) as a target for anti-cancer agent design. Curr Med Chem. 2008;15(27):2850–65.PubMedCrossRefGoogle Scholar
  16. 16.
    Badea L, Herlea V, Dima SO, Dumitrascu T, Popescu I. Combined gene expression analysis of whole-tissue and microdissected pancreatic ductal adenocarcinoma identifies genes specifically overexpressed in tumor epithelia. Hepatogastroenterology. 2008;55(88):2016–27.PubMedGoogle Scholar
  17. 17.
    Yan H, et al. IDH1 and IDH2 mutations in gliomas. N Engl J Med. 2009;360(8):765–73.PubMedCrossRefGoogle Scholar
  18. 18.
    Perut F, et al. Immunogenic properties of renal cell carcinoma and the pathogenesis of osteolytic bone metastases. Int J Oncol. 2009;34(5):1387–93.PubMedGoogle Scholar
  19. 19.
    Kondo T, et al. ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. J Cell Biol. 1997;139(3):749–58.PubMedCrossRefGoogle Scholar
  20. 20.
    Kannan K, et al. Lysosome-associated membrane proteins h-LAMP1 (CD107a) and h-LAMP2 (CD107b) are activation-dependent cell surface glycoproteins in human peripheral blood mononuclear cells which mediate cell adhesion to vascular endothelium. Cell Immunol. 1996;171(1):10–9.PubMedCrossRefGoogle Scholar
  21. 21.
    Mizuuchi E, Semba S, Kodama Y, Yokozaki H. Down-modulation of keratin 8 phosphorylation levels by PRL-3 contributes to colorectal carcinoma progression. Int J Cancer. 2009;124(8):1802–10.PubMedCrossRefGoogle Scholar
  22. 22.
    Kim TM, et al. Determination of genes related to gastrointestinal tract origin cancer cells using a cDNA microarray. Clin Cancer Res. 2005;11(1):79–86.PubMedGoogle Scholar
  23. 23.
    Kralovánszky J, Szentirmay Z, Besznyák I, Eckhardt S. Placental type alkaline phosphatase in possibly premalignant alterations of human gastric mucosa. Oncology. 1984;41(3):189–94.PubMedCrossRefGoogle Scholar
  24. 24.
    Marian MB, et al. Association of sorcin with the cardiac ryanodine receptor. J Biol Chem. 1995;270(44):26411–8.CrossRefGoogle Scholar
  25. 25.
    Nagpal JK, Das BR. Identification of differentially expressed genes in tobacco chewing-mediated oral cancer by differential display-polymerase chain reaction. Eur J Clin Invest. 2007;37(8):658–64.PubMedCrossRefGoogle Scholar
  26. 26.
    Meyers MB, Biedler JL. Increased synthesis of a low molecular weight protein in vincristine-resistant cells. Biochem Biophys Res Commun. 1981;99:228–35.PubMedCrossRefGoogle Scholar
  27. 27.
    Meyers MB. Sorcin: a calcium-binding protein overproduced in many multidrug-resistant cells. In: Smith VL, Dedman JR, editors. Stimulus response coupling: the role of intracellular calcium-binding proteins, Boca Raton: CRC Press Inc; 1990. p. 159–171.Google Scholar
  28. 28.
    Yang Y-X, Chen Z–C, Zhang G-Y, Yi H, Xiao Z-Q. A subcelluar proteomic investigation into vincristine-resistant gastric cancer cell line. J Cell Biochem. 2008;104:1010–21.PubMedCrossRefGoogle Scholar
  29. 29.
    He QC, Zhang GY, Cao WJ. Correlation of sorcin overexpression to multidrug resistance of human gastric cancer cell line SGC7901. Ai Zheng. 2008;27(4):337–42.PubMedGoogle Scholar

Copyright information

© Humana Press Inc. 2009

Authors and Affiliations

  • Langmei Deng
    • 1
  • Tao Su
    • 2
  • Aimin Leng
    • 1
  • Xiaomei Zhang
    • 1
  • Meihua xu
    • 1
  • Lu Yan
    • 1
  • Huan Gu
    • 1
  • Guiying Zhang
    • 1
    Email author
  1. 1.Department of Gastroenterology, Xiangya HospitalCentral South UniversityChangshaPeople’s Republic of China
  2. 2.The Medical Research Center of Xiangya HospitalCentral South UniversityChangshaPeople’s Republic of China

Personalised recommendations