Matrix association of latent TGF-beta binding protein-2 (LTBP-2) is dependent on fibrillin-1
| Autor: | Jorma Keski-Oja, Piia Vehviläinen, Marko Hyytiäinen |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Physiology
Fibrillin-1 Clinical Biochemistry Gene Expression Biology Matrix (biology) Fibrillins Cell Line Extracellular matrix Mice 03 medical and health sciences Cell Line Tumor Animals Humans Cells Cultured 030304 developmental biology Mice Knockout 0303 health sciences Confluency Binding protein Microfilament Proteins 030302 biochemistry & molecular biology Endothelial Cells Cell Biology Fibroblasts Embryo Mammalian Molecular biology Extracellular Matrix Fibronectins Cell biology Fibronectin Latent TGF-beta binding protein Latent TGF-beta Binding Proteins biology.protein RNA Interference Fibrillin Protein Binding |
| Zdroj: | Journal of Cellular Physiology. 221:586-593 |
| ISSN: | 0021-9541 |
| DOI: | 10.1002/jcp.21888 |
| Popis: | The components of the extracellular matrix (ECM) and their differential expression patterns play important roles in tissue formation. The deposition of latent TGF-beta binding proteins (LTBPs) to the ECM exhibit distinct distribution profiles. We have analyzed here the temporal and spatial ECM association of latent TGF-beta binding protein LTBP-2 in cultured human embryonic lung fibroblasts. We found that LTBP-2 was not assembled to the ECM until by confluency of cultures following the deposition of fibronectin (FN) and fibrillin-1. In 5-day-old cultures LTBP-2 was rapidly secreted from cells and it subsequently associated with the ECM as shown by metabolic labeling and immunoprecipitation. LTBP-2 colocalized transiently with fibronectin and failed to assemble to the ECM of FN deficient mouse fibroblasts. Analysis of different cultured human cell lines revealed partial colocalization of LTBP-2 and fibrillin-1 in the ECM of fibroblasts, MG-63 osteosarcoma cells and human vascular endothelial cells. Silencing of fibrillin-1 expression by lentiviral shRNAs profoundly disrupted the deposition of LTBP-2. Current results suggest that LTBP-2 is not an element of the provisional ECM of fibroblasts but is more likely a component of more mature ECM and indicate that matrix association of LTBP-2 depends on a pre-formed fibrillin-1 network. |
| Databáze: | OpenAIRE |
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