Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0031099 (
periodontitis
)
12,489
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Deficiency in the number and function of phagocytes is associated with gingival inflammation and
periodontitis
. A hereditary deficiency in membrane glycoproteins involved in granulocyte adherence causes impaired chemotaxis, reduced phagocytosis and periodontal problems. Virus infections of antigen-presenting cells interfere with immune responses and lead to seriously increased susceptibility to infections with bacteria which cause no problems in normal patients. Increased levels of IgG antibodies may limit penetration of antigens in the tissues, but at the cost of local inflammation and tissue injury. Mucosal inflammatory disease with increased local formation of IgG is more frequent in IgA deficient patients. The immunological homeostasis depends on a balance between the respective classes and subclasses of antibodies. Deficiencies in the IgA system may contribute to a
disturbed balance
of the humoral immune response to critical antigens from oral bacteria. A disproportional increase in IgG1 and IgG3 antibodies may persistently activate complement, stimulate the inflammatory activity and cause tissue injury.
...
PMID:Periodontal disease mechanisms in immunocompromised patients. 189 Feb 24
The plasminogen activating system is important for extracellular proteolysis and plays a regulatory role in interactions with other tissue degrading systems. Studies on the plasminogen activating system in gingival crevicular fluid (GCF) as well as gingival tissue are reviewed. t-PA, u-PA, PAI-1 and PAI-2 have all been detected in GCF. Especially t-PA and PAI-2 are found in high concentrations. In tissue studies fibrinolytic activity has been found in the gingival pocket epithelium in humans and in animal studies. t-PA and PAI-2 have been detected there immunohistochemically. Local production of the PAs and PAls has been verified with in situ hybridization. In inflammation, a more intense and widespread immunohistochemical staining of t-PA and PAI-2 is seen. Higher concentrations of t-PA and PAI-2 are found in GCF but the balance between them seems to be constant. A systemically
disturbed balance
of the plasminogen activating system in GCF has been observed during pregnancy, with a possible protective function of PAI-2. In studies of
periodontitis
, the production of PAI-2 seemed to be locally lowered at impaired sites. In a study of children, a higher inflammatory response to bacterial plaque was accompanied by a higher fibrinolytic ativity in GCF samples. Bacterial LPS has been found to change the ratio of t-PA to PAI-2 in cultured gingival fibroblasts. Interactions between PAI-2 and a protease in the gingival epithelium has been verified through the immunohistochemical detection of relaxed PAI-2.
...
PMID:The plasminogen activating system in periodontal health and disease. 1192 25
Several families of enzymes are responsible for the degradation of extracellular matrix (ECM) proteins during the remodeling of tissues. An important family of such enzymes is that of the matrix metalloproteinases (MMPs). To control MMP-mediated ECM breakdown, tissue inhibitors of metalloproteinases (TIMPs) are able to inhibit MMP activity. A
disturbed balance
of MMPs and TIMPs is found in various pathologic conditions, such as cancer, rheumatoid arthritis, and
periodontitis
. The role of MMPs in pathology has been extensively described in the literature. The main focus of this review lies in the biological functions of TIMPs and their occurrence in disease, especially in the head and neck area. Their biological functions and their role in diseases like oral cancers and
periodontitis
, and in the development of cleft palate, will be discussed. Finally, the diagnostic and therapeutical opportunities of TIMPs will be evaluated.
...
PMID:Tissue inhibitors of metalloproteinases (TIMPs): their biological functions and involvement in oral disease. 1712 57