The role of matrix metalloproteinases in the oral environment

被引:300
作者
Hannas, Angelica R.
Pereira, Jose C.
Granjeiro, Jose M.
Tjaderhane, Leo
机构
[1] Univ Sao Paulo, Bauru Sch Dent, Dept Operat Dent, BR-05508 Sao Paulo, Brazil
[2] Univ Sao Paulo, Bauru Sch Dent, Dept Biol Sci Biochem, BR-05508 Sao Paulo, Brazil
[3] Univ Helsinki, Inst Dent, Helsinki, Finland
[4] Univ Helsinki, Cent Hosp, Dept Oral & Maxillofacial Dis, Helsinki, Finland
基金
芬兰科学院;
关键词
dentin-pulp complex; endopeptidases; enzymes; MMP; periodontium; GINGIVAL CREVICULAR FLUID; GELATINASE-A MMP-2; COLLAGEN IN-SITU; ADULT PERIODONTITIS; HUMAN ODONTOBLASTS; DENTIN MATRIX; NEUTROPHIL COLLAGENASE; TISSUE INHIBITORS; BONE-RESORPTION; BACTERIAL-COLONIZATION;
D O I
10.1080/00016350600963640
中图分类号
R78 [口腔科学];
学科分类号
1003 ;
摘要
This review focuses specifically on matrix metalloproteinases (MMPs) and their role in physiological and pathological extracellular matrix (ECM) remodeling and degradation processes in the oral environment. A group of enzymes capable of degrading almost all ECM proteins, MMPs contribute to both normal and pathological tissue remodeling. The expression of different MMPs may be upregulated in pathological conditions such as inflammation and tumor invasion. The balance between activated MMPs and tissue inhibitors of metalloproteinases (TIMPs) controls the extent of ECM remodeling. Prior to mineralization, MMPs may participate in the organization of enamel and dentin organic matrix, or they may regulate mineralization by controlling the proteoglycan turnover. There is evidence indicating that MMPs could be involved in the etiology of enamel fluorosis and amelogenesis imperfecta. They seem to play a part in dentinal caries progression, since they have a crucial role in dentin collagen breakdown in caries lesions. MMPs have been identified in pulpal and periapical inflammation and are strongly correlated with periodontal diseases, since they are the major players in collagen breakdown during periodontal tissue destruction. The use of MMP inhibitors could help the prevention and treatment of many MMP-related oral diseases.
引用
收藏
页码:1 / 13
页数:13
相关论文
共 112 条
[1]   Decreased mineral content in MMP-20 null mouse enamel is prominent during the maturation stage [J].
Bartlett, JD ;
Beniash, E ;
Lee, DH ;
Smith, CE .
JOURNAL OF DENTAL RESEARCH, 2004, 83 (12) :909-913
[2]   ROLE OF MATRIX METALLOPROTEINASES IN HUMAN PERIODONTAL-DISEASES [J].
BIRKEDALHANSEN, H .
JOURNAL OF PERIODONTOLOGY, 1993, 64 (05) :474-484
[3]  
Black GV., 1916, DENT COSMOS, V58, P129
[4]   ADAMs: focus on the protease domain [J].
Black, RA ;
White, JM .
CURRENT OPINION IN CELL BIOLOGY, 1998, 10 (05) :654-659
[5]  
BLAVIER L, 1995, J CELL SCI, V108, P3649
[6]   Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF alpha and notch [J].
Blobel, CP .
CELL, 1997, 90 (04) :589-592
[7]   THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY [J].
BODE, W ;
REINEMER, P ;
HUBER, R ;
KLEINE, T ;
SCHNIERER, S ;
TSCHESCHE, H .
EMBO JOURNAL, 1994, 13 (06) :1263-1269
[8]   Gelatinase a (MMP-2) in developing tooth tissues and amelogenin hydrolysis [J].
Caron, C ;
Xue, J ;
Sun, X ;
Simmer, JP ;
Bartlett, JD .
JOURNAL OF DENTAL RESEARCH, 2001, 80 (07) :1660-1664
[9]   Mechanical stability of resin-dentin bond components [J].
Carrilho, MRD ;
Tay, FR ;
Pashley, DH ;
Tjäderhane, L ;
Carvalho, RM .
DENTAL MATERIALS, 2005, 21 (03) :232-241
[10]   Enamelysin (matrix metalloproteinase 20)-deficient mice display an amelogenesis imperfecta phenotype [J].
Caterina, JJ ;
Skobe, Z ;
Shi, J ;
Ding, YL ;
Simmer, JP ;
Birkedal-Hansen, H ;
Bartlett, JD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (51) :49598-49604