Autor: |
Fleischmajer R; Department of Dermatology, Mount Sinai School of Medicine, New York, New York 10029, USA. RF@doc.mssm.ed.w, Perlish JS, MacDonald ED 2nd, Schechter A, Murdoch AD, Iozzo RV, Yamada Y |
Jazyk: |
angličtina |
Zdroj: |
Annals of the New York Academy of Sciences [Ann N Y Acad Sci] 1998 Oct 23; Vol. 857, pp. 212-27. |
DOI: |
10.1111/j.1749-6632.1998.tb10118.x |
Abstrakt: |
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 IV, 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 (IV) 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 AIIB2 mAb (anti-beta 1 integrin subunit) and by peptide inhibition with the CB3(IV) 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. |
Databáze: |
MEDLINE |
Externí odkaz: |
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