Fibronectin membrane

Protein lateral motion is much slower than that of lipids because proteins are larger than lipids. Also, some membrane proteins can diffuse freely through the membrane, whereas others are bound or anchored to other protein structures in the membrane. The diffusion constant for the membrane protein fibronectin is approximately 0.7 X 10 cmVsec, whereas that for rhodopsin is about 3 X 10 cmVsec. 

Fibronectin receptor is a two-chain glycoprotein of the integrin family that serves as a transmembrane linker by binding to talin on the cytoplasmic side and to fibronectin on the external side of the membrane. The pull exerted by stress fibers on attached structures may be produced by bipolar assemblies of nonmuscle myosin molecules producing a sliding of actin filaments of opposite polarity. 

Figure 48-5. Schematic representation of fibronectin interacting with an integrin fibronectin receptor situated in the exterior of the plasma membrane of a cell of the ECM and of various attachment proteins interacting indirectly or directly with an actin microfilament in the cytosol. For simplicity, the attachment proteins are represented as a complex.

In the intact blood vessel, ligands involved in adhesion to platelets, such as collagen, fibronectin, and von Willebrand factor, are sequestered in the subendothelium, thus preventing access to platelet adhesive receptors. Table 1 summarizes the functions of platelet membrane integrin receptors. 

It has been shown that cell adhesion highly depends on the outermost functional groups on SAMs however, cells do not directly interact with the SAMs. Instead, they interact with proteins adsorbed on SAMs. Cell adherence requires an interaction between integral molecules in the cell membrane and glycoproteins specialized for cell adhesion, like fibronectin (Fn) and vitronectin (Vn), which are adsorbed on the artificial material. Thus, the presence of glycoproteins in serum plays a crucial role in cell adherence to artificial materials. In the first part of this review (Sect. 2), we will briefly survey recent studies of cell adhesion on SAMs with different functional groups and discuss the mechanisms involved. 

Members of this family of molecules may have only one Ig-like domain, as is the case for the myelin protein P0, or, as for most of the family, have many Ig domains. In addition to the subclassification of Ig domains into V-, C- and C2-like domains, Ig family members can be broadly divided into three general classes [8] (a) those that have only Ig-like domains (b) those that have Ig domains and additional domains that resemble regions of the ECM component fibronectin, termed FN-like domains and (c) those that have Ig domains and motifs other than FN-like domains. Moreover, any one Ig family member may have many isoforms, which may differ in the length of the cytoplasmic domain, in their post-translational modifications and whether they are membrane-spanning or glycosylphos-phatidylinositol (GPI)-anchored proteins (see Box 3-1). Also, additional amino acid sequences inserted in the extracellular domain may distinguish isoforms of a particular IgCAM. While it is not known how the majority... 

FIGURE 7-1 The immunoglobulin (Ig) gene family of molecules. Several varieties of Ig domain-containing molecules are contained within the Ig gene superfamily. Most are type I membrane proteins some have only Ig domains or other moieties that may convey function (see text). V, variable Ig domain C, constant Ig domain MAG, myelin-associated glycoprotein NCAM, neural cell adhesion molecule GPI, glycosylphosphatidyl-inositol EC, extracellular domain FN, fibronectin. 

Unlike the acellular basement membranes, the interstitial connective tissue consists of cells distributed in meshwork of collagen fibers, glycoproteins (e.g., fibronectin), proteoglycans, and hyaluronic acid. The main forms of collagen found in interstitial connective tissue are known as type I, II, and III or interstitial collagen. 

Adhesion proteins in this group contain an immunoglobulin domain that is composed of 90-100 amino acids arranged in a sandwich of two sheets of antiparallei strands. Some members of this family also contain fibronectin type III—like domains in addition to the immunoglobulin domain. Immunoglobulin-related adhesion proteins either can exist as transmembrane structures or can be attached to cell membranes via glycosyl phosphatidylinositol links (B4, R5). 

Hematopoiesis, the process of generating mature blood cells, is mainly located in the red bone marrow, predominantly in the sternum, femur and pelvic bones [1]. In the marrow the hematopoietic cells are embedded in stromal tissue. This consists of different cell types (e.g., fibroblasts, endothehal cells, adipocytes, macrophages) that provide soluble and membrane-bound growth factors and produce an extracellular matrix consisting of collagen, laminin, fibronectin, and glycosaminoglycans [2, 3]. The interactions between hematopoietic cells, stromal cells and extracellular matrix are indicated in Fig. 1 [4,5]. 

Cultured BHK cells that had heen maintained in a medium containing tunicamycin still shed various membrane glycoproteins into the medium,539 and this is in keeping with observations mentioned in Section IV,4. However, the proportion of fibronectin found in the medium appeared to he lessened.540-541 Cells kept in the presence of tunicamycin showed profound morphological changes, from epitheloid to elongated, spindle-shaped morphology, and lowered adhesion to the substratum. 

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