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Example sentences for: nidogen
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Fibulin-1 has been reported to interact with such extracellular matrix proteins as fibronectin, laminin, nidogen, aggrecan and versican [ 39 40 41 42 ] . Fibronectin is a glycoprotein found as multimers in insoluble form in the extracellular matrix.
It is well established that EGF-like modules are important structural features found in many extracellular proteins and that these modules enable numerous protein :protein interactions; the binding of EGF-like modules in laminin to nidogen [ 19 ] and the interaction of EGF-like modules within fibrillin monomers [ 20 21 ] . Calcium may be required for some of these protein interactions.
Nidogen is a basement membrane protein composed of three globular domains G1-G3 and two linking sequences; domain G1 is joined to domain G2 through a flexible link and domain G2 is connected to domain G3 by a rod-like element consisting of EGF-like modules [ 47 ] . Nidogen1 is an important structural component of tertiary complexes with other such extracellular components as laminins, collagen IV, perlecan, and fibulins [ 48 ] . Fibulin-1C binds to nidogen1 through domain G2 of nidogen [ 48 ] . The nidogen binding site of fibulin-1C includes the type II EGF-like modules 6-9 and the carboxyl-terminal domain [ 42 ] .
For example, cadherin 13 ( CDH13 ), versican ( CSPG2 ), collagen 8A1 ( COL8A1 ), collagen 12A1 ( COL12A1 ), P4HA2 (encoding a procollagen-modifying enzyme) all showed relatively low expression in the genital skin fibroblasts of normal males, whereas tenascin XB ( TNXB ), nidogen 2 ( NID2 ), laminins ( LAMA3 , LAMA4 ) and tissue inhibitor of metalloproteinase 1 ( TIMP1 ) all showed relatively high expression levels compared to AIS-derived fibroblasts (Figure 2).
Laminin is a glycoprotein composed of three chains, A, B1, and B2 in a cross-shaped molecule; this protein is found in basement membranes where it interacts with other such components as collagen IV, heparan-sulfate proteoglycan, and nidogen [ 45 ] . Laminin contains EGF-like modules in the amino-terminal region of the A, B1, and B2 chains [ 45 ] . Surprisingly, these modules do not appear to be involved in the binding of fibulin-1.
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