Expression of metalloproteinases and their tissue inhibitors in squamous cell laryngeal carcinoma

Abstract

The hallmark of cancer invasion is the degradation of extracellular matrix components. Matrix metalloproteinases are the major enzymes participating in this event and their activity is regulated extracellularly by their presence as proenzymes and the concomitant presence of the specific tissue inhibitors. The present study describes the immunohistochemical localization of gelatinases, matrix metalloproteinase (MMP)-2 and -9 and tissue inhibitor of metalloproteinase (TIMP)-1 and -2 in human laryngeal carcinoma and their expression with respect to tumor classification and compared with the respective healthy subjects. MMP-2 was immunolocalized in the cytoplasm of the epithelial cells and in the loose connective tissue, whereas MMP-9 was also observed in basement membrane and chondrocytes. Both were also found in tumor cells, but staining was decreased with increasing stage of cancer. TIMP-1 was present exclusively in stroma and totally absent from tumor cells and it was overexpressed in normal cells surrounding the tumor. TIMP-2 was identified in the cytoplasm of epithelial cells, in stroma and sometimes in chondrocytes. In addition, it was present in tumor cells of only stage IV samples. The expression level of both gelatinases and TIMPs increased as the stage of cancer increased, suggesting the possible post-transcriptional removal of their mRNA. These observations, performed in a given head and neck site, suggest that the behavior of head and neck tumors seems to depend on the site and additional studies should be performed to obtain a general understanding of the disease and ascertain the role of the constituents examined.

Immunoexpression of matrix metalloproteinase‐2 and matrix metalloproteinase‐9 in the metastasis of squamous cell carcinoma of the human tongue

“…This is consistent with other studies reporting significantly elevated MMP-2 and MMP-9 in malignant tissues, compared with adjacent normal tissues. [15][16][17] Furthermore, in 20 lymph node-negative tongue cancer specimens, 9 (45%) showed positive staining for MMP-2 and 8 (40%) for MMP-9. Importantly, in 41 lymph node-positive tongue cancers, 71% and 79% of the primary tumours were positively stained for MMP-2 and MMP-9, respectively.…”

Expression of matrix metalloproteinases (MMP-2 and MMP-9) in recurrent respiratory papillomas and laryngeal carcinoma: clinical and morphological parallels

“…gelatinase-A (MMP-2) and gelatinase-B (MMP-9) have the capacity to degrade the triple helix type IV and V collagen of the basement membrane, thus contributing to the invasion and metastases of malignant tumors [23]. Most studies have focused on the prognostic value of MMP expression in laryngeal squamous cell carcinoma growth and spreading to the lymph nodes [24][25][26][27].…”

Serum metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in lung carcinoma patients

“…A number of scientific reports confirms that coordinated increase of MMP-2 and TIMP-2 concentration and expression can accompany adverse prognosis for a patient with neoplastic disease (39)(40)(41). It is thought that the reason of the rise in TIMP-2 concentration is probably intensified expression, inhibited by TIMP-2 metalloproteinase 2, an attempt to maintain the balance between MMP-2/TIMP-2 concentration in neoplastic process (40)(41)(42).…”

“…It is thought that the reason of the rise in TIMP-2 concentration is probably intensified expression, inhibited by TIMP-2 metalloproteinase 2, an attempt to maintain the balance between MMP-2/TIMP-2 concentration in neoplastic process (40)(41)(42).…”