The paper deals with a potential role of fibronectin proteolysis associated with plasma cell membrane receptors in the control of cell behaviour. The molecule of fibronectin contains at least 5 adhesive domains providing its interaction with cell receptors and at least 2 domains interacting with other molecules of an extracellular matrix (ECM). Different cells in various states (steady state, motion, proliferation) interact with all or some of the adhesive domains of fibronectin. Limited fibronectin proteolysis as a linking between the cell and ECM results in a change in the cell status. Limited proteolysis of cell-bound fibronectin may occur with several proteinases: 1) uPA having a receptor in the focal contact of a cell; 2) plasmin resulted from plasminogen under the action of uPA; 3) stromelysin whose synthesis is induced by fibronectin proteolytic fragments; 4) metalloproteinases secreted by some cells and involving in the hapatotactic motion of a cell over fibronectin. Proteolysis of fibronectin and other ECM molecules may be inhibited itself due to proteolysis-induced release of inhibitors via binding to fibronectin (proteasonexin) and via binding to other ECM molecules (PAI-1). The fact that there is a direct and inverse correlation in the proteolytic process associated with a fibronectin cell (and other ECM molecules) indicate that the behavior of a cell can be controlled by the mechanism of proteolytic impairment of the cell-EMC and cell-cell bonds.