Autor: |
Gaubin Y; Faculté de Médecine Toulouse-Purpan, Laboratoire de Biologie Cellulaire, Toulouse, France., Pianezzi B, Soleilhavoup JP, Croute F |
Jazyk: |
angličtina |
Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1995 Oct 19; Vol. 1245 (2), pp. 173-80. |
DOI: |
10.1016/0304-4165(95)00088-s |
Abstrakt: |
In vitro human dermal fibroblasts were submitted to normal gravity (1 g) or to chronic hypergravity (20 g) over a period of 8 days. Changes in organization of extracellular matrix molecules were seen by indirect immunofluorescence. In the fibronectin layer, bundles of fibrils were gathered together leading to a disorganisation of the normal parallel pattern of fibers seen in control cultures. Type I collagen fibrils appeared with wooly outlines in controls whereas thick fibers were closely packed in 20-g cultures. A moderate increase of type III collagen fibril density was observed. No elastic fibers were seen in control or in 20-g cultures. In the culture medium, the release of soluble elastin (ELISA) and type I and III collagens (RIA) was undisturbed. Assays of enzymes involved in the remodeling of extracellular matrix showed an increase of cellular elastase activity (10%) and a decrease of the spontaneously active collagenase. Nevertheless, the total collagenase activity, (activated by trypsin), was increased by up to 30%. These data show a significant rise of the latent collagenase activity and suggest that release of the tissue inhibitor of metalloproteinase (TIMP1) was enhanced by hypergravity. |
Databáze: |
MEDLINE |
Externí odkaz: |
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