IMMUNOHISTOCHEMISTRY OF THE INTERCELLULAR MATRIX COMPONENTS AND THE EPITHELIOMESENCHYMAL JUNCTION OF THE HUMAN TOOTH GERM

被引:23
作者
GARBARSCH, C
MATTHIESSEN, ME
OLSEN, BE
MOE, D
KIRKEBY, S
机构
[1] UNIV COPENHAGEN,FAC HLTH SCI,SCH DENT,PANUM INST,DEPT ORAL FUNCT,COPENHAGEN,DENMARK
[2] UNIV COPENHAGEN,FAC HLTH SCI,SCH DENT,PANUM INST,DEPT MICROBIOL,COPENHAGEN,DENMARK
来源
HISTOCHEMICAL JOURNAL | 1994年 / 26卷 / 02期
关键词
D O I
10.1007/BF00157959
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The immunohistochemical localization of heparan sulphate, collagen type I, III and IV, laminin, tenascin, plasma- and cellular fibronectin was studied in tooth germs from human fetuses. The lamina basalis ameloblastica or membrana preformativa, which separates the pre-ameloblasts from the pre-dentin and dentin, contained heparan sulphate, collagen type IV, laminin and fibronectin. Enamel reacted with antifibronectin, but the reaction varied depending on the type of fibronectin and the source of antibody. In early pre-dentin, collagen type I, laminin, tenascin and fibronectin were present. In late pre-dentin and dentin collagen type I was found in intertubular dentin and in the zone between enamel and dentin. The close relationship between collagen type I in dentin and fibronectin in immature enamel is interesting, as it may contribute to the stabilization of the amelodentinal interface. In dental pulp, collagen type IV and laminin were found in the endothelial basement membranes. Collagen type I and III, tenascin and fibronectin were localized to the mesenchymal intercellular matrix. The results of this study have supported the assumption that the lamina basalis ameloblastica is a basement membrane, and have lead to the suggestion that ameloblasts are producers of fibronectin or a fibronectin-like substance.
引用
收藏
页码:110 / 118
页数:9
相关论文
共 33 条
[1]   DECALCIFICATION AND STAINING OF ARCHAEOLOGICAL BONES, WITH HISTOCHEMICAL INTERPRETATION OF METACHROMASIA [J].
ANDERSEN, H ;
JORGENSEN, JB .
STAIN TECHNOLOGY, 1960, 35 (02) :91-96
[2]   DISTRIBUTION AND SYNTHESIS OF TYPE-I AND TYPE-III COLLAGENS IN DEVELOPING MOUSE MOLAR TOOTH ROOT [J].
ANDUJAR, MB ;
HARTMANN, DJ ;
EMONARD, H ;
MAGLOIRE, H .
HISTOCHEMISTRY, 1988, 88 (02) :131-140
[3]  
BALAIN G, 1980, J BIOL CHEM, V255, P3234
[4]   DIFFERENTIAL EXPRESSION OF THE FIBRONECTIN ISOFORM CONTAINING THE ED-B ONCOFETAL DOMAIN IN NORMAL HUMAN FIBROBLAST CELL-LINES ORIGINATING FROM DIFFERENT TISSUES [J].
BORSI, L ;
BALZA, E ;
ALLEMANNI, G ;
ZARDI, L .
EXPERIMENTAL CELL RESEARCH, 1992, 199 (01) :98-105
[5]   PROCEDURE FOR THE PURIFICATION OF THE FIBRONECTIN PROTEOLYTIC FRAGMENTS CONTAINING THE ED-B ONCOFETAL DOMAIN [J].
BORSI, L ;
BALZA, E ;
LEPRINI, A ;
PONASSI, M ;
ZARDI, L .
ANALYTICAL BIOCHEMISTRY, 1991, 192 (02) :372-379
[6]  
Bronckers A L, 1989, Connect Tissue Res, V22, P65
[7]   EXPRESSION OF THE ED B FIBRONECTIN ISOFORM IN ADULT HUMAN ARTICULAR-CARTILAGE [J].
BURTONWURSTER, N ;
LUST, G ;
WERT, R .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 165 (02) :782-787
[8]   IDENTIFICATION OF SITES IN COLLAGEN ALPHA-CHAINS THAT BIND SERUM ANTI-GELATIN FACTOR (COLD-INSOLUBLE GLOBULIN) [J].
DESSAU, W ;
ADELMANN, BC ;
TIMPL, R ;
MARTIN, GR .
BIOCHEMICAL JOURNAL, 1978, 169 (01) :55-59
[9]   STRUCTURE AND FUNCTION OF ENAMEL GENE-PRODUCTS [J].
DEUTSCH, D .
ANATOMICAL RECORD, 1989, 224 (02) :189-210
[10]   SERUM AMINOTERMINAL TYPE-III PROCOLLAGEN PEPTIDE - RELATION TO BIOSYNTHESIS OF COLLAGEN TYPE-III IN EXPERIMENTALLY INDUCED GRANULATION-TISSUE IN RATS [J].
HORSLEVPETERSEN, K ;
KIM, KY ;
PEDERSEN, LR ;
BENTSEN, KD ;
ULDBJERG, N ;
OXLUND, H ;
GARBARSCH, C ;
HAHN, EG ;
SCHUPPAN, D ;
LORENZEN, I .
APMIS, 1988, 96 (09) :793-804