scholarly journals Factors Affecting IL-1-Mediated Collagen Metabolism By Fibroblasts and the Pathogenesis of Periodontal Disease: A Review of the Literature

1997 ◽  
Vol 8 (2) ◽  
pp. 217-236 ◽  
Author(s):  
Anne Havemose-Poulsen ◽  
Palle Holmstrup
Keyword(s):  
Extracellular Matrix ◽  
Connective Tissue ◽  
Periodontal Disease ◽  
Proteolytic Enzymes ◽  
Interleukin 1 ◽  
Collagen Fibrils ◽  
Review Of The Literature ◽  
Tissue Destruction ◽  
Factors Affecting ◽  
Extracellular Matrix Components

Fibroblasts have been studied extensively for their contribution to connective tissue destruction in diseases where the metabolism of extracellular matrix components plays an essential part in their pathogenesis. A considerable dissolution, especially of collagen fibrils, is a well-known characteristic of the periodontal ligament and the gingival connective tissue in microbial-induced periodontal disease. Fibroblasts, responsible for the assembly of the extracellular matrix, are capable of responding directly to oral microbial challenges or indirectly, following activation of the host immune response, and can alter the composition of connective tissue in several ways: synthesis of inflammatory mediators, their receptors and antagonists; fibroblast proliferation; collagen synthesis; phagocytosis of collagen fibrils; and synthesis of proteolytic enzymes, including matrix metalloproteinases and their corresponding inhibitors. The contributions of these cellular fibroblastic properties to the pathogenesis of periodontal disease are reviewed in the context of the cytokine, interleukin-1, as the inflammatory regulator.

Awareness of Periodontal Medicine among Medical Students at a Tertiary Care Center

2019 ◽  
Vol 3 (2) ◽  
pp. 66-69
Author(s):  
Junima Rajkarnikar ◽  
Jemish Acharya ◽  
Karnika Yadav
Keyword(s):  
Medical Students ◽  
Periodontal Disease ◽  
Proteolytic Enzymes ◽  
Care Center ◽  
Tertiary Care ◽  
Tertiary Care Center ◽  
Tissue Destruction ◽  
Periodontal Tissues ◽  
The Impact ◽  
Periodontal Medicine

Introduction: Tissue destruction of supporting periodontal tissues is mediated by an overreactive immune inflammatory response to bacteria in the subgingival environment. Tissue destruction in periodontitis occurs by the stimulatory action of pro inflammatory cytokines and proteolytic enzymes released by neutrophils, macrophages, and the action of bone resorption mediators, all of which are being regulated by B and T cells. Periodontitis act as a focus of infection and bacteria metastases through blood stream to various vital organs like heart, lungs, joints and amniotic fluid. Objective: To assess the awareness of periodontal medicine among medical students at a tertiary care center in Kathmandu. Methods: A total of 115 subjects were taken for the present study. Data was collected using a questionnaire which included questions used to assess the knowledge about periodontal diseases and its possible effects on systemic conditions. Results: Out of the total participants, 58 (50.4%) said that periodontal disease was not related to coronary heart diseases. Only 14 (12.2%) had an idea about the association of pre-term birth and periodontitis. While 86 (74.8%) knew the impact of diabetes on periodontium, only 34 (29.6%) said that there was an association between periodontitis and hospital acquired pneumonia. Conclusion: Knowledge about the association of periodontal disease with various systemic conditions is not satisfactory among the various medical students of this hospital.

scholarly journals Alignment hierarchies: engineering architecture from the nanometre to the micrometre scale

2010 ◽  
Vol 7 (suppl_6) ◽  
Author(s):  
Alvena Kureshi ◽  
Umber Cheema ◽  
Tijna Alekseeva ◽  
Alison Cambrey ◽  
Robert Brown
Keyword(s):  
Extracellular Matrix ◽  
Fluid Flow ◽  
Three Dimensional ◽  
Collagen Scaffold ◽  
Collagen Fibrils ◽  
Dimensional Structure ◽  
Protein Diffusion ◽  
Collagen Gels ◽  
Protein Factor ◽  
Extracellular Matrix Components

Natural tissues are built of metabolites, soluble proteins and solid extracellular matrix components (largely fibrils) together with cells. These are configured in highly organized hierarchies of structure across length scales from nanometre to millimetre, with alignments that are dominated by anisotropies in their fibrillar matrix. If we are to successfully engineer tissues, these hierarchies need to be mimicked with an understanding of the interaction between them. In particular, the movement of different elements of the tissue (e.g. molecules, cells and bulk fluids) is controlled by matrix structures at distinct scales. We present three novel systems to introduce alignment of collagen fibrils, cells and growth factor gradients within a three-dimensional collagen scaffold using fluid flow, embossing and layering of construct. Importantly, these can be seen as different parts of the same hierarchy of three-dimensional structure, as they are all formed into dense collagen gels. Fluid flow aligns collagen fibrils at the nanoscale, embossed topographical features provide alignment cues at the microscale and introducing layered configuration to three-dimensional collagen scaffolds provides microscale- and mesoscale-aligned pathways for protein factor delivery as well as barriers to confine protein diffusion to specific spatial directions. These seemingly separate methods can be employed to increase complexity of simple extracellular matrix scaffolds, providing insight into new approaches to directly fabricate complex physical and chemical cues at different hierarchical scales, similar to those in natural tissues.

Connective Tissue Degradation in Health and Periodontal Disease and the Roles of Matrix Metalloproteinases and Their Natural Inhibitors

1994 ◽  
Vol 8 (2) ◽  
pp. 312-319 ◽  
Author(s):  
J.J. Reynolds ◽  
R.M. Hembry ◽  
M.C. Meikle
Keyword(s):  
Matrix Metalloproteinases ◽  
Connective Tissue ◽  
Periodontal Disease ◽  
Mononuclear Cells ◽  
Transforming Growth Factor ◽  
Periodontal Diseases ◽  
Interleukin 1 ◽  
Tissue Remodeling ◽  
Periodontal Tissues ◽  
Tissue Degradation

Connective tissue remodeling is essential for normal growth and development, and many diseases have long been associated with the breakdown of the collagenous matrix of bone, cartilage, and related tissues. Recent work has established that members of the family of matrix metalloproteinases (MMPs) are key enzymes in matrix degradation. They function at neutral pH and can digest synergistically all the matrix macromolecules. Biochemical and cloning studies indicate that there are three major groups, collagenases, gelatinases, and stromelysins. Naturally occurring inhibitors, TIMPs (Tissue Inhibitors of Metallo Proteinases ), are important controlling factors in the actions of MMPs, and tissue destruction in disease processes often correlates with an imbalance of MMPs over TIMPs. The major inhibitor is TIMP-1 (or TIMP), a 30-kDa glycoprotein that is synthesized by most cells. The expression of MMPs and TIMPs by cells is regulated by many cytokines (particularly interleukin-1, IL-1), growth factors, and hormones, some of which are specific to cell type and others that are ubiquitous (e.g.,transforming growth factor β, TGF-P). One way in which pathogenic organisms might mediate tissue degradation in periodontal diseases is through the ability of cell wall antigens to stimulate cytokine production by circulating mononuclear cells. These would then induce MMP synthesis by resident gingival cells, thereby initiating degradative events. Direct in vivo evidence for the source of collagenase and other MMPs in periodontal tissues is limited. By using specific polyclonal antibodies and indirect immunofluorescence, we could demonstrate the presence of collagenase, stromelysin-1, gelatinase A, and TIMP in human gingival biopsy specimens. Their distributions are extremely variable, in both the connective tissue and the epithelium, but the results indicate that host cell production of MMPs may contribute to tissue remodeling in periodontal disease.

scholarly journals SERUM LEVEL OF MMP-3 IN PATIENTS WITH PSORIATIC ARTRITIS TREATED WITH TNF-α BLOKERS

2019 ◽  
Vol 34 (4) ◽  
pp. 939-941
Author(s):  
Stanislava Popova ◽  
Mariela Geneva-Popova ◽  
Anastas Batalov
Keyword(s):  
Extracellular Matrix ◽  
Serum Level ◽  
Disease Activity ◽  
Proteolytic Enzymes ◽  
Degenerative Joint Disease ◽  
Joint Disease ◽  
Blocker Therapy ◽  
Tnf Α ◽  
Extracellular Matrix Components ◽  
The Mean

Background: Matrix metalloproteinases (MMPs) are a family of proteolytic enzymes whose primary function is to break down the extracellular matrix. MMPs are important for tissue remodeling and affect cell signaling. MMP-3 (Stromelysin-1, Transin-1) hydrolyzes natural collagen and extracellular matrix components such as proteoglycan, laminin, fibronectin, gelatin and collagen type III, IV and IX and activates the precursor of IL1-beta. Psoriatic arthritis (PsA) is a rapidly developing, debilitating disease, and it is important for patients with it to identify serum biomarkers to predict its development. Patients and Methods: MMP-3 has been studied in 21 patients with PsA, 16 patients with PsA receiving TNF-α blocker therapy, and 22 patients with gonarthrosis and 15 healthy age-matched adults. All patients were treated and monitored at the University Clinic of Rheumatology, UMHAT “Kaspela“ and UMHAT “Steti Georgi”, Medical University, Plovdiv. The study of MMPs was performed using an ELISA methodology. Statistical processing of the data was performed using the SPSS 23 program with confidence (p <0.001). Results: The mean MMP-3 value in patients with PsA was 197.00 ± 35.90 pg / ml, in patients with AS 101.08 ± 15.76 ng / ml. The mean MMP-3 in patients with PsA receiving TNF-α blocker therapy and with low clinical disease activity was 50.48 ± 9.22 ng / ml. The mean MMP-3 in patients with gonarthrosis was 42.91 ± 11.72 ng / ml. The mean MMP-3 values in patients with active PsA were significantly different from those treated with TNF-α-blockers and patients with degenerative joint disease and controls (p <0.05). Conclusion: MMP-3 was significantly increased in patients with PsA compared with patients with osteoarthritis and healthy subjects. Administration of TNF-α blockers gradually leads to a decrease in the serum level of MMP-3 and can serve as a biomarker for disease activity as well as for evaluating the effect of therapy. arthrosis disease

The secretion of enzymes into the pericellular environment

1975 ◽  
Vol 271 (912) ◽  
pp. 315-324 ◽  
Keyword(s):  
Rheumatoid Arthritis ◽  
Extracellular Matrix ◽  
Connective Tissue ◽  
Cathepsin D ◽  
Proteolytic Enzymes ◽  
The Other ◽  
The Third ◽  
Extracellular Release ◽  
Proteoglycan Degradation ◽  
Tissue Cells

Connective tissue cells are capable of both synthesizing and degrading the macromolecular components of the extracellular matrix. The degradation of proteoglycan and collagen has been shown to be associated with the extracellular release of proteolytic enzymes, some of which are of lysosomal origin. The identity in cartilage of two previously unrecognized proteases, capable of proteoglycan breakdown (CPGases), has recently been achieved by the use of a new assay for proteoglycan degradation. These enzymes have been shown to be synthesized and released in response to vitamin A. The third proteoglycan degrading enzyme of connective tissue cells, cathepsin D, has been located in the pericellular environment by trapping with specific antibody and the pattern of release studied in organ culture, experimental arthritis and in human rheumatoid tissues. The secretion of this enzyme and possibly also of the other CPGases is thought to be of importance in the local (pericellular) turnover of matrix macromolecules and, in association with collagenase, to be the cause of the excessive degradation in the pannus erosion of articular cartilage in rheumatoid arthritis.

scholarly journals Extracellular matrix organization in developing muscle: correlation with acetylcholine receptor aggregates.

1984 ◽  
Vol 99 (4) ◽  
pp. 1486-1501 ◽  
Author(s):  
E K Bayne ◽  
M J Anderson ◽  
D M Fambrough
Keyword(s):  
Extracellular Matrix ◽  
Monoclonal Antibodies ◽  
Connective Tissue ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Extracellular Matrix Components ◽  
Matrix Organization ◽  
Matrix Components

Monoclonal antibodies recognizing laminin, heparan sulfate proteoglycan, fibronectin, and two apparently novel connective tissue components have been used to examine the organization of extracellular matrix of skeletal muscle in vivo and in vitro. Four of the five monoclonal antibodies are described for the first time here. Immunocytochemical experiments with frozen-sectioned muscle demonstrated that both the heparan sulfate proteoglycan and laminin exhibited staining patterns identical to that expected for components of the basal lamina. In contrast, the remaining matrix constituents were detected in all regions of muscle connective tissue: the endomysium, perimysium, and epimysium. Embryonic muscle cells developing in culture elaborated an extracellular matrix, each antigen exhibiting a unique distribution. Of particular interest was the organization of extracellular matrix on myotubes: the build-up of matrix components was most apparent in plaques overlying clusters of an integral membrane protein, the acetylcholine receptor (AChR). The heparan sulfate proteoglycan was concentrated at virtually all AChR clusters and showed a remarkable level of congruence with receptor organization; laminin was detected at 70-95% of AChR clusters but often was not completely co-distributed with AChR within the cluster; fibronectin and the two other extracellular matrix antigens occurred at approximately 20, 8, and 2% of the AChR clusters, respectively, and showed little or no congruence with AChR. From observations on the distribution of extracellular matrix components in tissue cultured fibroblasts and myogenic cells, several ideas about the organization of extracellular matrix are suggested. (a) Congruence between AChR clusters and heparan sulfate proteoglycan suggests the existence of some linkage between the two molecules, possibly important for regulation of AChR distribution within the muscle membrane. (b) The qualitatively different patterns of extracellular matrix organization over myotubes and fibroblasts suggest that each of these cell types uses somewhat different means to regulate the assembly of extracellular matrix components within its domain. (c) The limited co-distribution of different components within the extracellular matrix in vitro and the selective immune precipitation of each antigen from conditioned medium suggest that each extracellular matrix component is secreted in a form that is not complexed with other matrix constituents.

Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen

Microbiology ◽  
2004 ◽  
Vol 150 (8) ◽  
pp. 2677-2688 ◽  
Author(s):  
Keith P. Mintz
Keyword(s):  
Extracellular Matrix ◽  
Connective Tissue ◽  
Matrix Protein ◽  
Actinobacillus Actinomycetemcomitans ◽  
Extracellular Matrix Protein ◽  
Collagen Binding ◽  
Extracellular Matrix Components ◽  
Regulatory Cascades ◽  
Cofactor Biosynthesis ◽  
The Individual

Actinobacillus actinomycetemcomitans is an aetiologic agent in the development of periodontal and some systemic diseases in humans. This pathogen localizes to the underlying connective tissue of the oral cavity in individuals with periodontal disease. The adhesion of A. actinomycetemcomitans to extracellular matrix components of the connective tissue prompted this study to identify gene products mediating the interaction of A. actinomycetemcomitans to these molecules. A transposon mutagenesis system was optimized for use in A. actinomycetemcomitans and used to generate an insertional mutant library. A total of 2300 individual insertion transposon mutants were screened for changes in the adhesion to collagen and fibronectin. Mutants were identified which exhibited the following phenotypes: a decrease in collagen binding; a decrease in fibronectin binding; a decrease in binding to both proteins; and an increase in binding to both collagen and fibronectin. The identification of mutants defective in adhesion to the individual proteins indicates that distinct adhesins are expressed by this organism. Molecular analysis of these mutants implicated 11 independent loci in protein adhesion. One gene, emaA, is likely to encode a direct mediator of collagen adhesion, based on predicted protein features homologous to the collagen-binding protein YadA of Yersinia enterocolitica. EmaA was localized to the outer membrane, as expected for an adhesin. Reduction in fibronectin adhesion appeared to be influenced by abrogation of proteins involved in molybdenum-cofactor biosynthesis. Several other loci identified as reducing or increasing adhesion to both collagen and fibronectin are suggested to be involved in regulatory cascades that promote or repress expression of collagen and fibronectin adhesins. Collectively, the results support the hypothesis that A. actinomycetemcomitans host colonization involves afimbrial adhesins for extracellular matrix proteins, and that the expression of adhesion is modulated by global regulatory mechanisms.

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