There is binding of collagen IV to β1 integrin during early skin basement membrane assembly

被引:37
作者
Fleischmajer, R
Perlish, JS
Macdonald, ED
Schechter, A
Murdoch, AD
Iozzo, RV
Yamada, Y
机构
[1] CUNY Mt Sinai Sch Med, Dept Dermatol, New York, NY 10029 USA
[2] Thomas Jefferson Univ, Dept Pathol & Cell Biol, Philadelphia, PA 19107 USA
[3] NIDR, Craniofacial Dev Biol & Regenerat Branch, NIH, Bethesda, MD 20892 USA
来源
MORPHOGENESIS: CELLULAR INTERACTIONS | 1998年 / 857卷
关键词
D O I
10.1111/j.1749-6632.1998.tb10118.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This study is concerned with the mechanism of basement membrane assembly in an in vitro 3-dimensional skin-culture system. Dermal fibroblasts alone can synthesize collagen IV, perlecan, and nidogen, but cannot assemble them into a basement membrane. When keratinocytes are added to the culture, however,linear assembly of collagen TV, perlecan, and nidogen is noted at the epidermo-dermal interface. Northern blots and in situ hybridization showed that perlecan and nidogen mRNAs derive exclusively from fibroblasts, while the alpha 2 (TV) collagen chain is expressed by both keratinocytes and fibroblasts, although the major source is in the mesenchyma (80%). Prior to the development of the lamina densa, collagen IV colocalizes with beta 1 integrins, most likely alpha 1 beta 1 and alpha 2 beta 1, which are known receptors for this collagen. Blocking experiments with the AIlB2 mAb (anti-beta 1 integrin subunit) and by peptide inhibition with the CB3(TV) collagen fragment disrupted the assembly of collagen IV. This study suggests that the initiation of basement-membrane formation involves binding of collagen IV molecules to keratinocyte cell-matrix integrins. These complexes act as nucleation sites for further polymerization of collagen IV molecules mostly derived from fibroblasts, by a process of self-assembly.
引用
收藏
页码:212 / 227
页数:16
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