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  2. Fibronectin - Wikipedia

    en.wikipedia.org/wiki/Fibronectin

    Fibronectin is a high- molecular weight (~500-~600 kDa) [5] glycoprotein of the extracellular matrix that binds to membrane -spanning receptor proteins called integrins. [6] Fibronectin also binds to other extracellular matrix proteins such as collagen, fibrin, and heparan sulfate proteoglycans (e.g. syndecans).

  3. Fetal fibronectin - Wikipedia

    en.wikipedia.org/wiki/Fetal_fibronectin

    Fetal fibronectin. Fetal fibronectin (fFN) is a fibronectin protein produced by fetal cells. It is found at the interface of the chorion and the decidua (between the fetal sac and the uterine lining). Fetal fibronectin is found normally in vaginal fluid in early pregnancy prior to 22 weeks due to normal growth and development of tissues at the ...

  4. Fibronectin type I domain - Wikipedia

    en.wikipedia.org/wiki/Fibronectin_type_I_domain

    Fibronectin is a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Type I domain (FN1) is approximately 40 residues in length. Four conserved cysteines are involved in disulfide bonds. The 3D structure of the FN1 domain has been determined.

  5. Fibronectin type II domain - Wikipedia

    en.wikipedia.org/wiki/Fibronectin_type_II_domain

    Fibronectin type II domain is a collagen-binding protein domain. Fibronectin is a multi-domain glycoprotein , found in a soluble form in plasma, and in an insoluble form in loose connective tissue and basement membranes , that binds cell surfaces and various compounds including collagen , fibrin , heparin , DNA , and actin .

  6. Fibronectin type III domain - Wikipedia

    en.wikipedia.org/wiki/Fibronectin_type_III_domain

    The fibronectin protein in which this domain was first identified contains 16 copies of this domain. The domain is about 100 amino acids long and possesses a beta sandwich structure. Of the three fibronectin-type domains, type III is the only one without disulfide bonding present. Fibronectin domains are found in a wide variety of extracellular ...

  7. Hemidesmosome - Wikipedia

    en.wikipedia.org/wiki/Hemidesmosome

    Integrin α6β4 is composed to two α and β subunit dimers. The larger β4 subunit has domains that bind to fibronectin III and calcium. The α6 subunit binds to extracellular BP180, CD151 and laminin-322. When integrin α6β4 binds to Plectin 1a and BPAG1, it associates with the keratin intermediate filaments in the cytoskeleton. [2]

  8. Alpha-5 beta-1 - Wikipedia

    en.wikipedia.org/wiki/Alpha-5_beta-1

    α5β1, also known as the fibronectin receptor, [1] is an integrin that binds to matrix macromolecules and proteinases and thereby stimulates angiogenesis. [2] It is composed of α 5 (ITGA5 /CD49e) and β 1 (ITGB1 /CD29) subunits. It is the primary receptor for fibronectin. The interaction of VLA-5 with fibronectin plays an important role in ...

  9. Dermal fibroblast - Wikipedia

    en.wikipedia.org/wiki/Dermal_fibroblast

    Dermal fibroblast. Dermal fibroblasts are cells within the dermis layer of skin which are responsible for generating connective tissue and allowing the skin to recover from injury. [1] Using organelles (particularly the rough endoplasmic reticulum), dermal fibroblasts generate and maintain the connective tissue which unites separate cell layers ...