Luting agents differentially modulate inflammation and matrix metalloproteinases in connective tissue

2018 ◽  
Vol 3 (1) ◽  
pp. 8-15
Author(s):  
Alexandra Mussolino de QUEIROZ ◽  
Thais Helena Andreolli do AMARAL ◽  
Francisco Wanderley Garcia PAULA-SILVA ◽  
Léa Assed Bezerra da SILVA ◽  
Paulo NELSON FILHO ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Connective Tissue ◽  
Luting Agents

scholarly journals Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodelling

1999 ◽  
Vol 340 (1) ◽  
pp. 171 ◽  
Author(s):  
Jane L. ASHWORTH ◽  
Gillian MURPHY ◽  
Matthew J. ROCK ◽  
Michael J. SHERRATT ◽  
Stephen D. SHAPIRO ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Connective Tissue ◽  
Tissue Remodelling

Expressions of matrix metalloproteinases and their inhibitor are modified by beta-adrenergic agonist Ractopamine in skeletal fibroblasts and myoblasts

2012 ◽  
Vol 92 (2) ◽  
pp. 159-166 ◽  
Author(s):  
Ming C. Cha ◽  
Peter P. Purslow
Keyword(s):  
Skeletal Muscle ◽  
Matrix Metalloproteinases ◽  
Connective Tissue ◽  
Cell Lines ◽  
C2c12 Cells ◽  
Adrenergic Agonist ◽  
Beta Adrenergic ◽  
Cellular Expression ◽  
Tissue Turnover ◽  
Beta Adrenergic Agonist

Cha, M. C. and Purslow, P. P. 2012. Expressions of matrix metalloproteinases and their inhibitor are modified by beta-adrenergic agonist Ractopamine in skeletal fibroblasts and myoblasts. Can. J. Anim. Sci. 92: 159–166. The beta-adrenergic agonist ractopamine is known to promote growth and improve feed efficiency in animal production, in part by suppressing muscle protein degradation. This investigation aims to determine whether ractopamine modifies the expression of enzymes principally involved in intramuscular connective tissue turnover, the matrix metalloproteinases (MMPs) and their inhibitors, in the principal cell types of skeletal muscle. Mouse skeletal muscle fibroblasts (NOR-10 cells) and myoblasts (C2C12 cells) were cultured with or without 2 or 10 µM ractopamine for 6 or 24 h. Cellular MMP-2 expression was increased (P<0.05) by ractopamine in both cell lines. Cellular MMP-3 expression was also increased in response to ractopamine in myoblasts (P<0.03). The amount of a tissue inhibitor of MMPs (TIMP-1) in cell lysates of both cell lines was increased (P<0.05) by the 6-h ractopamine treatment. The extracellular expression of MMP-2 and TIMP-1 was increased (P<0.05) in myoblasts, but not in fibroblasts. The elevated TIMP-1 expression in medium is in the order of three times higher (P<0.02) than the increased activity of MMP-2 expressed by myoblasts at 6 h. In summary, ractopamine treatment results in a higher cellular expression of MMP-2 and MMP-3 as compared with the expression of their inhibitor TIMP-1. However, the increased extracellular MMP-2 activity is counterbalanced by the increased presence of TIMP-1. The findings show that ractopamine has the potential to alter connective tissue turnover in treated animals.

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.

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