Immunohistochemical Determination of the Matrix Metalloproteinase-2 and -7 Expression in Transmissible Venereal Tumor in Dogs

Yıl 2018, Cilt: 3 Sayı: 2, 106 - 110, 30.12.2018

Özlem Özmen Ezgi Ogus

https://doi.org/10.24880/maeuvfd.481960

Cited By: 1

Öz

Transmissible venereal
tumor (TVT) is a sexually transmitted, naturally occurring tumor of the canine
family and often occurs in tropical and subtropical countries. The matrix metalloproteinases
(MMPs) are endogenous proteases accountable for the degradation of
extracellular matrix (ECM) components, such as collagen and other proteins including
the basement membrane. MMPs play a vital role in the tumor metastasis and
angiogenesis. Both MMP-2 and -7 strongly associated with the invasion and
metastasis of different cancer types. This study aims to investigate the MMP-2
and -7 expression in naturally occurring TVT in 20 dogs using immunohistochemical
methods. Immunohistochemically, we observed increased MMP-2 and -7 expressions in
tumor cells. In addition, a positive correlation was determined between the tumor
size and immunoexpressions of the markers indicating
that both MMP-2 and -7 participate in the
TVT pathogenesis.

Anahtar Kelimeler

dog, pat

Kaynakça

• References1. Osipov NE, Golubeva VA. Diagnosis and treatment of transmissible sarcoma of dogs. Veterinariia. 1976; 7: 97–8. PMID: 9889382. Singh J, Rama JS, Sood N, Pangawkar G, Gupta PP. Clinico-pathological studies on the effect of different antineoplastic chemotherapy regimens on transmissible venereal tumours in dogs. Vet. Res. Commun. 1996; 20: 71–81. https//doi.org/10.1007/bf003465793. Batamuzi EK, Kassuku AA, Agger JE. Risk factors associated with canine TVT in Tanzania. Prev. Vet. Med. 1992; 13,:13-7. https://doi.org/10.1016/0167-5877(92)90031-A4. Ferreira A J, Jaggy A, Varejao AP, Ferreira ML, Correia JM, Mulas JM, Almeida O, Oliveira P, Prada J. Brain and ocular metastases from a transmissible venereal tumour in a dog. J. Small Anim. Pract. 2000; 41: 165–8. https//doi.org/10.1111/j.1748-5827.2000.tb03187.x5. Varaschin MS, Wouters F, Bernis VM. Tumor venéreo transmissível canino na região de Alfenas, Minas Gerais; formas de apresentação clínico-patológicas. La Clinica Vet. 2001; 6: 32-8.6. Purohit GN. Canine transmissible venerial tumors: A review. I J. Vet. Med. 2009; 6(1). https//doi.org/10.5580/a6a.7. Hoque M. An update on canine transmissible venereal tumor. Intas Polivet. 2002; 3: 227-34.8. Placke ME, Hill DL, Yang TJ. Cranial metastasis of canine transmissible venereal sarcoma. Zent.Vet. Reihe A. 1987; 34: 125–32.9. Schlafer DH, Foster RA. Female genital system. In: Maxie MG, editor. Jubb, Kennedy and Palmer’s Pathology of Domestic Animals. 6th ed. pp 448-449. MO: Elsevier; 2016.10. Lorimier LP, Fan TM. Canine transmissible venereal tumor. In: Withrow SJ., Vail DM, editors. Small Animal Clinical Oncology. 4th ed. pp 799–803. MO: Elsevier; 2007.11. Fink K, Boratynski J. The role of metalloproteinases in modification of extracellular matrix in invasive tumor growth, metastasis and angiogenesis. Postepy Hig. Med. Doswi. 2012; 66: 609-28.12. Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovas. Res. 2006; 69: 562-73. https//doi.org/10.1016/j.cardiores.2005.12.00213. Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Ann. Rev. Cell Develop. Biol. 2001; 17: 463–516. https//doi.org/10.1146/annurev.cellbio.17.1.46314. Folgueras AR, Pendas AM, Sanchez LM, Lopez-Otin C. Matrix metalloproteinases in cancer: from new function to improved inhibition strategies. Inter. J. Develop. Biol. 2004; 48: 411-24. https//doi.org/10.1387/ijdb.041811af15. Karin M, Chang L. AP-1 glucocorticoid receptor crosstalk taken to a higher level. J. Endocrinol. 2001; 169: 447-51. https//doi.org/10.1677/joe.0.169044716. Curran S, Murray GI. Matrix metalloproteinases in tumour invasion and metastasis. J. Pathol. 1999; 189: 300-8. https//doi.org/10.1002/(SICI)1096-9896 17. Hidalgo M, Eckhardt SG. Development of matrix metalloproteinase inhibitors in cancer therapy. J. Nat. Cancer Inst. 2001; 93:178-93. https//doi.org/10.1093/jnci/93.3.17818. O'Reilly MS, Wiederschain D, Stetler-Stevenson WG, Folkman J, Moses MA. Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance. J. Biol. Chem. 1999; 274; 29568-71. https//doi.org/ 10.1074/jbc.274.41.2956819. Roberts LM, Visser JA, Ingraham HA. Involvement of a matrix metalloproteinase in MIS-induced cell death during urogenital development. Development. 2002; 129:1487-96. PMID: 1188035720. Wilson CL, Matrisian LM. Matrilysin: an epithelial matrix metalloproteinase with potentially novel functions. Inter. J. Biochem. Cell Biol. 1996; 28: 123-36. https//doi.org/10.1016/1357-2725(95)00121-221. Zeng Z, Shu W, Cohen AM, Guillem JG. Matrix metalloproteinase-7 expression in colorectal cancer liver metastases: Evidence for involvement of MMP-7 activation in human cancer metastases. Clin. Cancer Res. 2002; 8: 144-8. PMID: 1180155122. Akkoc A, Nak D, Demirer A, Simsek G. Immunocharacterization of matrix metalloproteinase-2 and matrix metalloproteinase-9 in canine transmissible venereal tumors. Biotechic and Histochem. 2017; 92: 100-6. https//doi.org/ 10.1080/10520295.2016.125950023. Luna GL. Manual of Histologic Staining Methods of the Armed Forces Institute of Pathology. 3rd ed. pp. 32-34. New York: McGraw Hill Book Co; 1968.24. Rozanov VD, Hahn-Dantona E, Strickland DK, Strongin AY. The low-density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells. J. Biol. Chem. 2004; 279: 4260-8. https//doi.org/ 10.1074/jbc.M31156920025. Noel A, Jost M, Maquoi E. Matrix metalloproteinases at cancer tumor-host interface. Semin. Cell Develop. Biol. 2008; 19: 52-60. https//doi.org/10.1016/j.semcdb.2007.05.01126. Stetler-Stevenson WG, Yu AE. Proteases in invasion:matrix metalloproteinases. Semin. Cancer Biol. 2001; 11: 143-52. https//doi.org/10.1006/scbi.2000.036527. Imai K, Yokohama Y, Nakanishi I, Ohuchi E, Fujii Y, Nakai N, Okada Y. Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor interaction with other matrix metalloproteinases and enzymic properties. J. Biol. Chem. 1995; 270: 6691–7. https//doi.org/10.1074/jbc.270.12.669128. Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R. The collagenase gene family in humans consists of at least four members. Biochem. J. 1988; 253: 187–92. https//doi.org/ 10.1042/bj2530187