Tissue distribution of perlecan domains III and V during embryonic and fetal human development

被引:0
作者
Roediger, Matthias [1 ]
Kruegel, Jenny [1 ]
Miosge, Nicolai [1 ]
Gersdorff, Nikolaus [1 ]
机构
[1] Univ Gottingen, Tissue Regenerat Work Grp, Dept Prosthodont, D-37075 Gottingen, Germany
关键词
Perlecan; Basement membrane; Human embryogenesis; Immunohistochemistry; HEPARAN-SULFATE PROTEOGLYCAN; SCHWARTZ-JAMPEL-SYNDROME; BASEMENT-MEMBRANES; CELL-ADHESION; EXPRESSION; LAMININ; BINDS; FIBULIN-2; NIDOGEN; LOCALIZATION;
D O I
暂无
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A major component of basement membranes (BMs) is perlecan, a five-domain heparan sulphate proteoglycan. During murine embryogenesis, nearly all BMs of mesenchymal origin express perlecan, and it is believed to participate in the supramolecular assembly of BMs. However, the distribution of perlecan in human embryonic and fetal tissues is widely unknown, except for cartilage anlagen of developing extremities and the fetal spine. Clinical syndromes, caused by perlecan-associated mutations or gene-defects, suggest its multifunctional involvement during human development. Here we reveal the immunohistochemistry of perlecan domains III and V during human development from gestational weeks (gw) 6 to 12 in basement membrane zones (BMZs) of the developing brain, nervous system, blood vessels, skin, lung, heart, kidney, liver, intestine and skeletal system. Interestingly, a difference in the distribution of the two perlecan domains was found in the endoneurium of ganglia. Domain III is strongly present from gw 6 onwards, while domain V shows attenuated expression at this stage and has been detected abundantly only from gw 8 onwards, possibly indicating vascularization of the endoneurium during this early stage. We found perlecan to be present particularly at those stages of human development where epithelial-mesenchymal interactions occur.
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页码:859 / 868
页数:10
相关论文
共 53 条
[1]   Structural and functional mutations of the perlecan gene cause Schwartz-Jampel syndrome, with myotonic myopathy and chondrodysplasia [J].
Arikawa-Hirasawa, E ;
Le, AH ;
Nishino, I ;
Nonaka, I ;
Ho, NC ;
Francomano, CA ;
Govindraj, P ;
Hassell, JR ;
Devaney, JM ;
Spranger, J ;
Stevenson, RE ;
Iannaccone, S ;
Dalakas, MC ;
Yamada, Y .
AMERICAN JOURNAL OF HUMAN GENETICS, 2002, 70 (05) :1368-1375
[2]   Perlecan is essential for cartilage and cephalic development [J].
Arikawa-Hirasawa, E ;
Watanabe, H ;
Takami, H ;
Hassell, JR ;
Yamada, Y .
NATURE GENETICS, 1999, 23 (03) :354-358
[3]   Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene [J].
Arikawa-Hirasawa, E ;
Wilcox, WR ;
Le, AH ;
Silverman, N ;
Govindraj, P ;
Hassell, JR ;
Yamada, Y .
NATURE GENETICS, 2001, 27 (04) :431-434
[4]   The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor [J].
Bengtsson, E ;
Mörgelin, M ;
Sasaki, T ;
Timpl, R ;
Heinegård, D ;
Aspberg, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (17) :15061-15068
[5]   Novel interactions of perlecan: Unraveling perlecan's role in angiogenesis [J].
Bix, Gregory ;
Iozzo, Renato V. .
MICROSCOPY RESEARCH AND TECHNIQUE, 2008, 71 (05) :339-348
[6]   MYOCARDIAL PROTECTION [J].
BRETSCHNEIDER, HJ .
THORACIC AND CARDIOVASCULAR SURGEON, 1980, 28 (05) :295-302
[7]   The C-terminal domain V of perlecan promotes beta 1 integrin-mediated cell adhesion, binds heparin, nidogen and fibulin-2 and can be modified by glycosaminoglycans [J].
Brown, JC ;
Sasaki, T ;
Gohring, W ;
Yamada, Y ;
Timpl, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 250 (01) :39-46
[8]   FETAL AND POSTNATAL-DEVELOPMENT OF THE LUNG [J].
BURRI, PH .
ANNUAL REVIEW OF PHYSIOLOGY, 1984, 46 :617-628
[9]  
CARLIN B, 1981, J BIOL CHEM, V256, P5209
[10]   Hyperplastic conotruncal endocardial cushions and transposition of great arteries in perlecan-null mice [J].
Costell, M ;
Carmona, R ;
Gustafsson, E ;
González-Iriarte, M ;
Fässler, R ;
Muñoz-Chápuli, R .
CIRCULATION RESEARCH, 2002, 91 (02) :158-164