Founded in 1993
  Year: 2000 | Volume: 8 | Issue: 3 | Pages: 95-98
  Original Article
  IMUNOHISTOCHEMICAL LOCALIZATION OF MATRIX METALLOPROTEINASE-2 (MMP-2) IN MEDULLARY THYROID CARCINOMA
Dubravka CVEJIC, Svetlana SAVIN, Ivan PAUNOVIC, Svetislav TATIC, Marija HAVELKA
  DOI:
  Abstract:
  Background: Matrix metalloproteinases (MMPs) are a family of proteolytic enzymes that degrade protein components of the extracellular matrix. These enzymes are believed to play an important role in tumor progression, invasion and metastasis.
Materials and Methods: We examined the expression of one member of the MMP family, matrix metalloproteinase-2 (MMP-2, collagenase A) in twenty-two paraffin-embedded specimens of medullary thyroid carcinoma (MTC) using an immunohistochemical method and a monoclonal antibody against MMP-2. In addition, we compared MMP-2 expression with clinicopathological data at the time of surgery.
Results: Immunohistochemical staining showed moderate to strong positivity in 19/22 cases and weak positivity in 3/22 cases. MMP-2 was immunohistochemically localized mainly in tumor cells, but was also present in surrounding stromal tissue. MMP-2 expression, however, was not associated with histopathological appearance of the tumor tissue, tumor size or the presence of lymph node metastases.
Conclusion: Considerble production of MMP-2 is associated with the malignant phenotype of parafollicular thyroid cells, suggesting a potential role of this proteolytic enzyme in tumorigenesis in vivo. However, since MMP-2 expression was not related to clinicopathological data, immunohistochemical staining of MMP-2 does not seem to be helpful in predicting the prognosis of medullary thyroid carcinoma.
  Key words: Matrix metalloproteinase-2; Medullary thyroid carcinoma; Prognosis; Immunohistochemistry
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Founder and owner: Oncology Institute of Vojvodina, Serbia
Publisher: Oncology Institute of Vojvodina
Co-publisher: Faculty of Medicine, University of Novi Sad
Online since 1997 (Abstracts only); 2000 (Abstracts and Full text)
ISSN: 0354-7310 eISSN: 1450-9520