Browsing by Subject "Matrix metalloproteinase"
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- PublicationOpen AccessCo-localization of integrins and matrix metalloproteinases in the extracellular matrix of chondrocyte cultures(F. Hernández y Juan F. Madrid. Universidad de Murcia: Departamento de Biología Celular e Histología, 2001) Schulze Tanzil, Gundula; de Souza, P.; Merker, H. J.; Shakibaei, M.ß1-int eg rin s we re found in th e ca rtil age matri x, suggesting their implication in the assembly of its architectural sca ffold , but the mechanism fo r this event is not yet clear. Matrix metalloproteinases (MMPs) may be involved in an int egrin -shedding mechanism and matri x 131- integrins may ac t to alter MMP activity. To begin to address this qu esti o n, this stud y was desig ned to determin e wheth er ß1-in teg rin s and MMPs arc colocali zed in th e chondrocy tes or in the ex trace llul ar matrix of cartil age. We investigated high-densit y cultures of limb buds of 12-day -old mo use embryos by double immunoflu o re ce nce, immun oe lectron mi c rosco py and by coimmunoprccipitation assays in order to examine the loca li za ti o n o f ß1-int egrin s and matri x me ta ll oproteinases (MMP-1, MMP-3 and MMP-9) in cartilage. It was found , that all investigated MMPs and 13 1- integrins we re specifically co-loca li zed in high-density cartil age cultures. Immunogold and immunofluorescence labelling of both ß1-integrins and MMPs were observed not only at the surface of chondrocytes but mainl y also in th e pe rice llul ar space a nd distributed be tw ee n coll agen fibrils in th e ex trace llular matrix (ECM) as we ll. Res ults o f immun oprecipitati o n ex pe riments suggest a fun cti onal assoc iati on of MMPs and 13 Lintegrins in chondrocytes as already described fo r other cell types. Further investigations are needed to elu cidate the fun ctional association between Bl-integrins and MMPs in chondrocytes.
- PublicationOpen AccessExpression of matrix metalloproteinase-9 (gelatinase B) in benign, premalignant and malignant laryngeal lesions(Murcia : F. Hernández, 2006) Peschos, D.; Damala, C.; Stefanou, D.; Tsanou, E.; Assimakopoulos, D.; Vougiouklakis, T.; Charalabopoulos, K.; Agnantis, N.J.The matrix metalloproteinases (MMPs) are a family of proteolytic zinc-containing enzymes, which are responsible for the breakdown of the extracellular matrix components in pathological and physiological conditions. They are involved in basement membrane disruption, stroma and blood vessel penetration, metastasis and more recently there is evidence that they participate in tumor growth and angiogenic events. Matrix metalloproteinase 2 and 9 (MMP 2 and 9) belong to the gelatinases, a subgroup of MMPs, and have the capacity to degrade the triple helix type IV collagen of basal lamina of the basement membrane. With the present study, we tried to demonstrate the expression of MMP-9 immunohistochemically, comparatively in benign, premalignant and malignant lesions of the larynx. We studied 154 laryngeal lesions including 55 squamous cell carcinomas, 8 in situ carcinomas, 54 cases of dysplasia (of low and intermediate grade), 13 papillomas and 24 cases of keratosis. Overexpression of MMP 9 was observed in 74.4% and 50% in invasive and in situ squamous cell carcinomas respectively. In dysplastic cases, in papillomas and in keratoses the percentage of overexpression was 62.9%, 61.53% and 54.16% respectively and the expression of MMP-9 was significantly higher in invasive squamous cell carcinomas compared to dysplasias (p=0.000004). Also significantly higher was the expression of MMP-9 in dysplastic cases compared to papillomas (p=0.023). The MMP-9 expression was related neither to survival nor to the other available clinicopathological parameters (tumor size, grade, clinical stage, lymph node status and patient age). In conclusion, our study indicates that the expression of MMP-9 is up-regulated in a stepwise fashion, with two main steps, the first one, when a dysplastic lesion evolves and the next one, when the dysplasia progresses to invasive carcinoma.
- PublicationOpen AccessGradual expression of MMP9 and MT1-MMP at the tumor-stroma interface in head and neck squamous cell carcinoma(Universidad de Murcia, Departamento de Biologia Celular e Histiologia, 2025) Rusu, Stefan; Nuyens, Vincent; Rousseau, Alexandre; Lothaire, Philippe; Nagy, Nathalie; Boudjeltia, Karim Zouaoui; Uzureau, Pierrick; Biología Celular e HistologíaDue to the late-stage diagnosis of head and neck squamous cell carcinoma (HNSCC), treatment remains a significant clinical challenge. The metallo-proteinases MMP-9 and MT1-MMP play a pivotal role in extracellular matrix remodeling, thereby facilitating tumor growth and metastasis. Tumor progression requires the degradation of the basement membrane. The principal components of this structure, namely collagen IV and laminin, are the main targets of both MMP-9 and MT1-MMP. However, they can also exert influence over the expression of these enzymes. Oxidative stress plays an instrumental role in tumor development, functioning as a key inducer of metalloproteinase expression. The present study investigates the distribution of MMP-9 and MT1-MMP within tumor nests and along the basement membrane, comparing these with the distributions of collagen IV, laminin-332, and the antioxidant MnSOD. Biopsies from 12 patients with HNSCC and poor prognostic factors were subjected to immuno-fluorescence analysis. MMP-9 and MT1-MMP were found to be predominantly present in tumor cells, with a significant decrease in expression from the periphery to the center of tumor nests. Co-localization studies with laminin-332 and collagen IV, revealed substantial overlap, in accordance with the role of MMPs in basal membrane degradation. The cellular expression of laminin-332 associated with MMP-9 expression suggests an intricate relationship between metalloproteinases and their targets. While the previously observed pattern of glutathione-producing enzyme was similar to the metalloproteinases pattern, MnSOD expression was homogeneously distributed within tumor nests. Our findings reveal various distribution patterns of oxidative stress regulators, suggesting a complicated interplay in the development of HNSCC
- PublicationOpen AccessImmunohistochemical expression and localization of MMP-9, MMP-13, E-Cadherin and Ki-67 in road pavers' skin chronically exposed to bitumen products.(Universidad de Murcia, Departamento de Biologia Celular e Histiologia, 2019) Loreto, Carla; Lombardo, Claudia; Caltabiano, Rosario; Filetti, Vera; Vitale, Ermanno; Seminara, Danilo; Castorina, Sergio; Fenga, Concettina; Ledda, Caterina; Rapisarda, VenerandoTo investigate the matrix metalloproteinase (MMP)-9, (MMP)-13, E-Cadherin and Ki-67 expressions in road pavers’ skin chronically exposed to bitumen products in order to contribute to a better understanding of the earlier tissue alteration. Skin punch biopsies from 16 daily exposed workers and a control group were studied by immunohistochemistry. Morphometric and densitometric analyses were also conducted. Morphological specimen evaluation of skin of road pavers showed epidermal thinning, flattening and loss of intercellular junction with a decreased expression of E-cadherin confined to the basal skin layer, together with MMP-9 and MMP-13 overexpressions in all epidermis layers, vascular structures and adnexa. No immunohistochemical alteration was reported for Ki-67 vs normal skin. Results from this study show that overexpression of MMP-9 and MMP-13 may represent an early response of the first human barrier to exposure to bitumen products. Regulation of MMPs could be one of the strategies to prevent primary skin disease.
- PublicationOpen AccessMatrix metalloproteinases in bone marrow: roles of gelatinases in physiological hematopoiesis and hematopoietic malignancies(Murcia : F. Hernández, 2006) Yu, X.F.; Han, Z.C.Turnover balance of extracellular matrix (ECM) is a prerequisite for the structural and functional homeostasis of bone marrow (BM) microenvironment. The role of ECM in physiologic hematopoiesis and its pathologic change in hematopoietic malignancies are very important and under extensive investigation. Accumulating evidence suggests that matrix metalloproteinases (MMPs), a family of zinc-dependent proteinases, take an active part in the physiological and pathological hematopoiesis through remodeling the ECM in BM hematopoietic microenvironment. In this review, we will focus on the roles of MMPs in physiological hematopoiesis, hematopoietic stem cells mobilization/transplantation, and hematological malignancies. Furthermore, the preclinical studies on the role of synthetic MMP inhibitors in the treatment of hematological malignancies will be discussed.
- PublicationOpen AccessPromotion of metastasis in nasopharyngeal carcinoma by Epstein-Barr virus latent membrane protein-1(Murcia : F. Hernández, 2002) Yoshizaki, T.Nasopharyngeal carcinoma (NPC) is a malignant tumor associated with Epstein-Barr virus (EBV). Latent membrane protein-1 (LMP-1) is an EBVencoded oncoprotein and is detected in approximately 50-70% of patients with NPC. LMP-1 is thought to play an essential role in tumorigenesis of NPC. In addition to its transforming properties, LMP-1 has been suggested to be associated with promotion of metastasis. Metastasis is a phenomenon composed of multiple sequential cascades. Reduction of tumor cell adhesion, degradation of extracellular matrix, basement membrane, enhancement of cell motility, and promotion of neovascularization are thought to be essential steps. LMP-1 down-regulates expression of E-cadherin, induces matrix metalloproteinase-9 and urokinase typeplasminogen activator through activation of NF-?B and AP-1, and enhances cell motility via ets-1 activation. LMP-1 also induces vascular endothelial growth factor through cyclooxygenase-2 activation and interleukin-8 through NF-?B activation. Clinical studies suggested the association of these factors with metastatic status of patients with NPC. In this review, the role of LMP-1 in the metastasis of NPC is discussed.