Expression of matrix metalloproteinases in healthy and diseased human gingiva.

Background, Aims: The aim of our study was to investigate the patterns of several metalloproteinases (MMP-1, MMP-2 and MT1-MMP) mRNAs expression using a semi-quantitative reverse transcriptase-polymerase chain reaction (RT-PCR) and to correlate them with clinical parameters and bacteriological diagnosis in healthy versus diseased human gingiva.

Methods: To identify the cell origin of MMP production, in situ hybridization (ISH) was also performed for the MMPs on the same samples. 17 gingival biopsies were collected (13 affected by advanced periodontitis and 4 healthy used as controls) and plaque index, gingival index, pocket depth and bleeding on probing were measured.

Detection of human papillomavirus DNA in bronchopulmonary carcinomas by hybrid capture II: a study of 185 tumors.

Background: Some human papillomaviruses (HPVs) are oncogenic in the cervix and are also associated with benign and malignant proliferations in other organs. Currently, the association of HPV with tumors of the lower respiratory tract is not so clearly defined because the studies are difficult to compare; series of cases reported from different geographic regions have used frozen or formalin fixed samples and a variety of techniques of HPV detection.

Methods: The authors studied the prevalence of HPV in a large series of 185 frozen bronchopulmonary tumor samples with a new solution hybridization technique, Hybrid Capture II assay.

Matrix-metalloproteinases in bronchopulmonary carcinomas.

Matrix metalloproteinases (MMPs) represent a group of enzymes involved in the degradation of most of the components of the extracellular matrix and therefore participate in tumoural invasion. MMPs, especially gelatinases A and B, MT1-MMP, the activator of gelatinase A, and stromelysin-3 were found overexpressed in many cancers including bronchopulmonary carcinomas. In vivo observations revealed that fibroblasts are the principal source of production of MMPs.

Expression of gelatinase A and its activator MT1-MMP in the inflammatory periprosthetic response to polyethylene.

Wear debris of polyethylene prosthetic components is known to induce a host granulomatous reaction which recruits numerous macrophages and multinucleated giant cells. By releasing cellular mediators of a nonspecific inflammatory reaction, activated phagocytic cells are thought to play a key role in osteolysis leading to aseptic loosening of the prosthesis. Matrix metalloproteinases (MMPs) have been implicated in this destructive process by their ability to degrade extracellular matrix components of bone and adjacent connective tissue.

Increased serum stromelysin-1 levels in systemic lupus erythematosus: lack of correlation with disease activity.

Objective: In view of evidence that stromelysin-1 and collagenase-1 are involved in tissue injury in inflammatory joint diseases, we sought to determine whether matrix metalloproteinases (MMP) are implicated in the pathophysiology of systemic lupus erythematosus (SLE).

Methods: Seventy-three patients with SLE and 39 healthy subjects were evaluated. Serum levels of MMP and tissue inhibitor of metalloproteinases were measured.

Cytoplasmic redistribution of E-cadherin-catenin adhesion complex is associated with down-regulated tyrosine phosphorylation of E-cadherin in human bronchopulmonary carcinomas.

The E-cadherin-catenin complex, by mediating intercellular adhesion, regulates the architectural integrity of epithelia. Down-regulation of its expression is thought to contribute to invasion of carcinoma cells. To investigate the involvement of the E-cadherin-catenin adhesion system in the progression of human bronchopulmonary carcinomas, we compared the immunohistochemical distribution of E-cadherin, alpha-catenin, and beta-catenin in four human bronchial cancer cell lines with different invasive abilities and in 44 primary bronchopulmonary tumors.

The elastase-induced expression of secretory leukocyte protease inhibitor is decreased in remodelled airway epithelium.

During airway inflammation, proteinases such as human leukocyte elastase are actively secreted. Secretory leukocyte protease inhibitor is a major serine proteinase inhibitor, secreted by bronchial, bronchiolar and lung epithelial cells. We recently identified secretory leukocyte protease inhibitor in human nasal epithelium, exclusively in remodelled areas of the surface epithelium.

Expression of matrix metalloproteinases and their inhibitors in human bronchopulmonary carcinomas: quantificative and morphological analyses.

The expression of various matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in 88 primary bronchopulmonary cancers and in 13 neighbouring pulmonary parenchyma samples was quantified by Northern-blot analysis, and morphologically examined by in situ hybridization and immunohistochemistry in order to evaluate the involvement of MMPs in the pathophysiology of these carcinomas and to look for potential markers of aggressivity of lung tumours. Northern-blot analysis showed that the predominantly expressed MMPs in bronchopulmonary cancers were gelatinase A (66%), its activator MT1-MMP (membrane-type-1 matrix metalloproteinase) (56%) and stromelysin-3 (61%). MMP expression frequencies and mRNA levels increased progressively with malignant phenotype, lack of differentiation and TNM stage of the tumours, whereas TIMP expression decreased very early during tumour progression.

Expression of stromelysin-3 in the human placenta and placental bed.

Human placentation is mediated by fetal trophoblastic cells which penetrate into the decidualized uterine endometrium. Trophoblast invasion requires the precisely regulated secretion of specific proteinases able to degrade the endometrial basement membranes and extracellular matrix. To document further the involvement of these proteinases during human placentation, we evaluated in vivo the expression of stromelysin-3, a member of the metalloproteinase family, during the first and third trimesters of pregnancy, by means of immunohistochemistry, in situ hybridization and Northern blot analysis.

Membrane-type matrix metalloproteinase-1 expression at the site of human placentation.

Human trophoblast implantation is a highly regulated process of invasion that requires action of proteolytic enzymes to degrade extracellular matrix components of the endometrium. Among these enzymes, matrix metalloproteinases (MMPs) seem to be particularly important in this degradative process. We previously showed that gelatinase A is extensively expressed in vivo in the human placenta.

Expression of interleukin-4 in scleroderma skin specimens and scleroderma fibroblast cultures. Potential role in fibrosis.

Background: Scleroderma (systemic sclerosis) is a fibrotic disease characterized by an uncontrolled tissular accumulation of collagen. Several cytokines have been implicated in the fibroblast activation leading to fibrosis. For instance, we have previously demonstrated that interleukin-4 (IL-4) is a potent activator of collagen synthesis in fibroblast cultures.

MT-MMP expression and localisation in human lung and breast cancers.

Thirteen primary pulmonary squamous cell carcinomas, 4 specimens of normal lung from around tumours, 4 benign proliferations of the mammary gland and 16 breast carcinomas were analysed by in situ hybridisation. Northern blot and immunohistochemistry for the expression of a recently described metalloproteinase (MMP), the MT-MMP (membrane-type matrix metalloproteinase). This MT-MMP can activate gelatinase A, involved in the degradation of basement membranes.

Expression of gelatinases A and B and their tissue inhibitors by cells of early and term human placenta and gestational endometrium.

Background: Human placentation is mediated by fetal trophoblastic cells that invade the maternal uterine endometrium. Trophoblast invasion requires a precisely regulated secretion of specific proteolytic enzymes able to degrade the endometrial basement membrane and extracellular matrix.

Experimental Design: Several studies have documented the key roles of matrix metalloproteinases and their tissue inhibitors in the invasion of various matrices by cultured trophoblasts.

Expression of stromelysin 3 and tissue inhibitors of matrix metallo-proteinases, TIMP-1 and TIMP-2, in rheumatoid arthritis.

Rheumatoid hyperplastic synovial lining cells and sublining fibroblasts are known to produce, in vivo and in vitro, matrix metallo-proteinases which degrade extracellular matrix components of joints. We have studied by immunohistochemistry and in situ hybridization the presence of matrix metallo-proteinase stromelysin 3 and its potential inhibitors TIMP-1 and TIMP-2 in 5 cases of normal synovia, 5 cases of chronic synovitis and 12 cases of rheumatoid arthritis. Few hyperplastic synoviocytes and some sparse fibroblasts have been found to produce stromelysin 3 in all rheumatoid arthritis and 2 chronic synovitis.

Gelatinase A expression and localization in human breast cancers. An in situ hybridization study and immunohistochemical detection using confocal microscopy.

The gelatinase A (72 kDa type IV collagenase) is a matrix metallo-proteinase which degrades basement membrane collagens. Various studies emphasize its role in stromal invasion of cancers, but there is some controversy about its origin. Gelatinase A was localized by immunohistochemistry using confocal microscopy in 15 human mammary carcinomas.

Becoming chart smart the academic way.

Instead of relying on another "quick fix" approach to medical record problems, write Eileen Chiama, M.S., Robert Morisse, M.