On the other hand, in pathologic processes, there is an overexpression of these proteins,

due to the imbalance between the activity and their inhibitors.7, 31 and 32 Considering the calcifying cystic odontogenic tumor, few studies have been conducted to evaluate the expression of metalloproteinases in these lesions. In the present work, in general, MMPs were expressed in both parenchymal Selleckchem Olaparib and stromal cells but a immunoreactivity for MMPs 1, 7, and 9 was observed, which reinforces the idea of the involvement of stroma cells in the degradation of matrix components. There are several substrates of MMPs 1, 2, 7, 9, and 26. MMP-1 degrades mainly collagens I, II, and III. Gelatinases (MMPs 2 and 9) degrade mainly denatured collagen (gelatin) and collagen type IV, GW3965 nmr and the matrilysins MMP-7 and -26 digest various components of the matrix, which include fibronectin and collagen type IV.31 Score 2 was observed in 100% of cases for MMPs 1, 7, and 9. The positivity displayed by MMP-1 demonstrates the importance of this protease for the degradation of ECM constituents, mainly collagen I, promoting tumor growth and expansion. Similar results in relation to the expression of MMP-1 have been demonstrated in other studies of odontogenic tumors, such as ameloblastoma,22,

24 and 27 odontogenic tumor keratocystic,25 myxoma,33 and adenomatoid odontogenic tumor.27 Amorim et al. (2004)34 analyzed the immunohistochemical Astemizole expression of tenascin, fibronectin, and collagen IV in syndromic (SKOTs) and nonsyndromic (NSKOTs) keratocystic odontogenic tumors and observed that there were differences in the expression of these proteins between the lesions. Tenascin was present along the basal membrane in all cases of SKOT, whereas in 5 cases of NSKOT this protein was negative in certain areas. The distribution of tenascin was focal on the SKOT wall and diffuse in NSKOT. Fibronectin was detected with a discontinuous band in SKOT and discontinuous in NSKOT. Collagen IV was not present in most cases of SKOT. MMPs 2 and 9 are gelatinases, their main difference being that

MMP-2 can degrade collagen type I,35 and 36 both are involved in angiogenesis and in tumor growth.28 Vincent et al. (2005)37 argue that these gelatinases are important in the process of tumor invasion because of the ability to degrade collagen type IV, the main constituent of the basal membrane, which is the first barrier to be breached in the process. Gong et al. (2009)38 evaluated the immunohistochemical expression of MMP-9 in CCOT and concluded that the positivity of this enzyme in the stroma is associated with the ability to promote tumor invasion. Our results demonstrate focal immunostaining for MMP-2, whereas for MMP-9 a score of 2 was observed in 100% of the cases and a diffuse distribution pattern in parenchymal cells, corroborating the studies of Ribeiro et al.