Intracellular distribution and morphology of mitochondria depend on cytoskeleton structures and are controlled by external factors. One of the main factors responsible for the cytoskeleton organization and the behavior of membrane-bound organelles is the interaction of cellular receptors with the extracellular matrix (ECM). Fibronectin is one of the main ECM components; different parts of the ECM molecules interact with different receptors. It was shown earlier that different fragments of fibronectin caused different rearrangements in the cytoskeleton. We suggested that some of these rearrangements might be involved in the intracellular distribution of mitochondria. To investigate the role of ECM in the mitochondria distribution we have developed a method of covalent binding of fibronectin and its fragments to the activated glass and worked out the conditions of cell culture on this glass in serum-free medium. Cells CV-1 attached and spread on the glass coverslips covered with fibronectin or its 120 kDa-fragment. Unlike the control cells, the cells grown on fibronectin-covered glass contained shortened mitochondria, which mainly localized near the nuclei. When fibronectin solution was added to these cells, mitochondria elongated and some of them redistributed towards the cell periphery. The same effect was produced by fibronectin or its 40 kDa-fragment when added to the cells grown on the coverslips covered with the 120 kDa-fragment of fibronectin. These data indicate that heparin-binding domain of fibronectin may play an important role in the regulation of the mitochondria shape and intracellular distribution. We also show here that the effect of the added fibronectin depends on microtubules.
|Original language||English (US)|
|State||Published - 2005|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology