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Seminars in Cancer Biology, 2002
Fibronectin (Fn) was the first 'structural' glycoprotein intensively studied as an ubiquitous matrix component of early phylogenetic appearance. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases.
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Fibronectin (Fn) was the first 'structural' glycoprotein intensively studied as an ubiquitous matrix component of early phylogenetic appearance. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases.
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2003
Fibronectin (FN) matrix fibrils assembled in cell culture have been observed to stretch in response to cell movements, and when broken relax to 1/3 to 1/4 of their rest length. Two molecular mechanisms have been proposed, for the elasticity. One proposes that FN molecules in relaxed fibers are bent and looped into a compact conformation, and stretching
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Fibronectin (FN) matrix fibrils assembled in cell culture have been observed to stretch in response to cell movements, and when broken relax to 1/3 to 1/4 of their rest length. Two molecular mechanisms have been proposed, for the elasticity. One proposes that FN molecules in relaxed fibers are bent and looped into a compact conformation, and stretching
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Plasma fibronectin contributes to fibronectin in tissues.
Acta chirurgica Scandinavica, 1985Fibronectin is produced by several cell types, with hepatocytes currently recognized as the main source of plasma fibronectin. Mesenchymal cells produce fibronectin in vitro and probably do so even in vivo. But it is not clear if these cells represent the sole source of tissue fibronectin.
T, Gauperaa, R, Seljelid
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