Stromelysin-1 (MMP-3) in forming enamel and predentine in rat incisor - coordinated distribution with proteoglycans suggests a functional role

被引:60
作者
Hall, R
Septier, D
Embery, G
Goldberg, M
机构
[1] Univ Paris 05, Fac Chirurg Dent, Grp Matrices Extracellulaires & Biomineralisat, Lab Biol & Physiopathol Craniofaciales EA 2496, F-92120 Montrouge, France
[2] Cardiff Univ, Sch Dent, Cardiff CF4 4XY, S Glam, Wales
来源
HISTOCHEMICAL JOURNAL | 1999年 / 31卷 / 12期
基金
英国惠康基金;
关键词
D O I
10.1023/A:1003945902473
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Stromelysin-1 (matrix metalloproteinase-3) or proteoglycanase was visualized by light and electron microscopy immunolabelling in the forming zone of rat incisors. In predentine, labelling was more dense at the transition zone between the inner proximal third and the two outer thirds. Odontoblast processes were also positively stained, mostly in predentine and to a lesser degree in dentine. The dentine-enamel junction was intensely labelled, whereas dentine and forming enamel were only faintly stained. Gold-antibodies complexes were seen inside secretory ameloblasts and odontoblasts in cytosolic locations. The distribution of stromelysin-1 was compared with the distribution of 2-B-6 epitope, an antibody recognizing chondroitin-4-sulphate/dermatan sulphate and which showed a decreasing gradient from the proximal zone to the distal part of predentine. In contrast, both 5-D-4, an anti-keratan sulphate antibody and an anti-lumican antibody displayed a reversed distribution, with an increase seen from the proximal and central thirds to the distal part of predentine. This coordinated distribution suggests that stromelysin-1 may have a functional role, being implicated in predentine in the degradation of chondroitin-4-sulphate/dermatan sulphate-containing proteoglycans, and consequently allowing keratan sulphate proteoglycan concentration to increase near the border where mineralization is initiated.
引用
收藏
页码:761 / 770
页数:10
相关论文
共 41 条
[1]   Immunolocalization of glycosaminoglycans in ageing, healthy and periodontally diseased human cementum [J].
Ababneh, KT ;
Hall, RC ;
Embery, G .
ARCHIVES OF ORAL BIOLOGY, 1998, 43 (03) :235-246
[2]   The proteasome [J].
Baumeister, W ;
Lupas, A .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1997, 7 (02) :273-278
[3]   PROTEOLYTIC REMODELING OF EXTRACELLULAR-MATRIX [J].
BIRKEDALHANSEN, H .
CURRENT OPINION IN CELL BIOLOGY, 1995, 7 (05) :728-735
[4]   PURIFICATION AND PROPERTIES OF A PROTEASE FROM DEVELOPING PORCINE DENTAL ENAMEL [J].
CARTER, J ;
SMILLIE, AC ;
SHEPHERD, MG .
ARCHIVES OF ORAL BIOLOGY, 1989, 34 (03) :195-202
[5]   VISUALIZATION OF GLYCOSAMINOGLYCANS IN RAT INCISOR EXTRACELLULAR-MATRIX USING A HYALURONIDASE-GOLD COMPLEX [J].
CHARDIN, H ;
LONDONO, I ;
GOLDBERG, M .
HISTOCHEMICAL JOURNAL, 1990, 22 (11) :588-594
[6]   Differential distribution of lumican and fibromodulin in tooth cementum [J].
Cheng, H ;
Caterson, B ;
Neame, PJ ;
Lester, GE ;
Yamauchi, M .
CONNECTIVE TISSUE RESEARCH, 1996, 34 (02) :87-+
[7]  
CHIN JR, 1985, J BIOL CHEM, V260, P2367
[8]  
Crenshaw M. A., 1984, TOOTH ENAMEL, P109
[9]   MATRIX VESICLES PRODUCED BY OSTEOBLAST-LIKE CELLS IN CULTURE BECOME SIGNIFICANTLY ENRICHED IN PROTEOGLYCAN-DEGRADING METALLOPROTEINASES AFTER ADDITION OF BETA-GLYCEROPHOSPHATE AND ASCORBIC-ACID [J].
DEAN, DD ;
SCHWARTZ, Z ;
BONEWALD, L ;
MUNIZ, OE ;
MORALES, S ;
GOMEZ, R ;
BROOKS, BP ;
QIAO, M ;
HOWELL, DS ;
BOYAN, BD .
CALCIFIED TISSUE INTERNATIONAL, 1994, 54 (05) :399-408
[10]   SEPARATION BY POLYACRYLAMIDE-GEL ELECTROPHORESIS OF MULTIPLE PROTEASES IN RAT AND BOVINE ENAMEL [J].
DENBESTEN, PK ;
HEFFERNAN, LM .
ARCHIVES OF ORAL BIOLOGY, 1989, 34 (06) :399-404