Co-Expression and Co-Localization of Cartilage Glycoproteins CHI3L1 and Lubricin in Osteoarthritic Cartilage: Morphological, Immunohistochemical and Gene Expression Profiles.

Osteoarthritis is the most common human arthritis characterized by degeneration of articular cartilage. Several studies reported that levels of human cartilage glycoprotein chitinase 3-like-1 (CHI3L1) are known as a potential marker for the activation of chondrocytes and the progression of Osteoarthritis (OA), whereas lubricin appears to be chondroprotective. The aim of this study was to investigate the co-expression and co-localization of CHI3L1 and lubricin in normal and osteoarthritic rat articular cartilage to correlate their modified expression to a specific grade of OA. Samples of normal and osteoarthritic rat articular cartilage were analyzed by the Kellgren-Lawrence OA severity scores, the Kraus' modified Mankin score and the Histopathology Osteoarthritis Research Society International (OARSI) system for histomorphometric evaluations, and through CHI3L1 and lubricin gene expression, immunohistochemistry and double immuno-staining analysis. The immunoexpression and the mRNA levels of lubricin increased in normal cartilage and decreased in OA cartilage (normal vs. OA, p < 0.01). By contrast, the immunoexpression and the mRNA levels of CHI3L1 increased in OA cartilage and decreased in normal cartilage (normal vs. OA, p < 0.01). Our findings are consistent with reports suggesting that these two glycoproteins are functionally associated with the development of OA and in particular with grade 2/3 of OA, suggesting that in the future they could be helpful to stage the severity and progression of the disease.

Immunohistochemical expression of matrix metalloprotease-2 and matrix metalloprotease-9 in the disks of patients with temporomandibular joint dysfunction.

PURPOSE: Matrix metalloproteases (MMPs) are tissue-remodeling enzymes that function during the remodeling process, such as in immune-inflammatory diseases. Metalloprotease-2 (MMP-2) and metalloprotease-9 (MMP-9) are gelatinases that degrade several types of extracellular matrix collagen. It is hypothesized that in temporomandibular joint (TMJ) dysfunction, MMP-2 and MMP-9 expression levels may be elevated. Therefore, the objective of this study is to determine the association of MMP-2 and MMP-9 expression with temporomandibular joint dysfunction using an immunohistochemical approach to evaluate the joint disk. MATERIAL AND METHODS: A total of 45 human temporomandibular joint samples were collected, with 36 samples in the test group (patients with anterior disk displacement with reduction (n = 29) and without reduction (n = 7)) and nine samples in the control group. The immunostaining of the TMJ disks was statistically compared between the groups (P < 0.05). RESULTS: There was a statistically significant difference for the area of MMP-2 immunostaining between the control group and the displacement disks with reduction group (ADDwR) (P = 0.048) and between the groups with disk displacement and without reduction (ADDwoR) (P = 0.029). The expression of MMP-2 was significantly elevated in the ADDwoR group. CONCLUSION: No statistically significant difference was found between the variable area of MMP-9 expression in the disk with and without disk displacement, as determined by immunohistochemical analysis. However, there was an elevation of MMP-2 expression in the disks of patients with displacement and without reduction (more severe alteration).

Differential expression of heat shock protein 27 in normal oral mucosa, oral epithelial dysplasia and squamous cell carcinoma.

The aim of this study was to evaluate HSP27 expression in fetal, normal and inflamed oral mucosal epithelium and in oral premalignant epithelial lesions and in their ensuing invasive cancers. In developing human oral epithelia, immunoreactions for HSP27 were moderately observed in suprabasal keratinocytes of palate and tongue. Normal oral epithelium had an intense suprabasal positivity. In inflamed oral mucosa, HSP27 staining was stronger in basal and suprabasal keratinocytes than in normal epithelium. Most oral premalignant lesions showed no (5 cases, 29%) or low (8 cases, 46.4%) staining. In OSCC both low and high HSP27 levels of expression were observed. HSP27 immunolabelling was down-regulated in poorly differentiated areas and up-regulated in highly differentiated ones. These findings indicated that HSP27 expression seems to protect cells from apoptosis during inflammation, while the down-regulation in dysplasia could impair the protective mechanism against mutagenesis induced by environmental factors and thus enhancing the transformation of oral epithelial dysplasia into OSCCs.