Frankel:ECM Proteins: Difference between revisions
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<br | ''<font align="center" font color=#ffffff font size=8>_________ </font>'''''<font color=#000000 font size=8>ECM Proteins</font>''' | ||
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''<font align="center" font color=#ffffff font size=8>_______ </font>'''''<font color=#000000 font size=3>Fibronectin</font>''' | |||
'''<font color=#000000 font size=3>Fibronectin</font>''' | |||
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Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand. | Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand. | ||
Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains. | Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains. | ||
Revision as of 14:28, 17 November 2012
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_________ ECM Proteins
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_______ Fibronectin
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One of the major components of the extracellular matrix (ECM) is fibronectin, this dimeric glycoprotein is involved in numerous cell processes and has important functions in vertebrate development. Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand. Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains. |
