2005
DOI: 10.1016/j.bbrc.2005.10.134
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Extra domain A and type III connecting segment of fibronectin in assembly and cleavage

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Cited by 17 publications
(15 citation statements)
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“…The present findings therefore support the existence of an allosteric network among the fibrin-binding domain [1][2][3][4][5] [12][13][14]. Such an open conformation may account for the unique ability of EDA-positive FN to be assembled into extensive fibrous networks by CHO cells (42). Interestingly, FN assembly associated with lymphatic valves in mice has been shown to require interaction of ␣9␤1 integrin with the ␣9␤1-recognition sequence in EDA rather than interaction of ␣5␤1 integrin with 10 FNIII (43).…”
Section: Binding Of Hadd Like Binding Of Fud Causes Exposure Of Thesupporting
confidence: 71%
“…The present findings therefore support the existence of an allosteric network among the fibrin-binding domain [1][2][3][4][5] [12][13][14]. Such an open conformation may account for the unique ability of EDA-positive FN to be assembled into extensive fibrous networks by CHO cells (42). Interestingly, FN assembly associated with lymphatic valves in mice has been shown to require interaction of ␣9␤1 integrin with the ␣9␤1-recognition sequence in EDA rather than interaction of ␣5␤1 integrin with 10 FNIII (43).…”
Section: Binding Of Hadd Like Binding Of Fud Causes Exposure Of Thesupporting
confidence: 71%
“…A clinical postmaturity syndrome of a fetus is thought to be a consequence of failing placental function [15] and FN containing alternatively spliced ED-A domain is one of active participants of fibrous network of placental extracellular matrices, [16] thus EDA-FN might be released from matrix to amniotic fluid during placental dysfunction.…”
Section: Statisticsmentioning
confidence: 99%
“…Isoforms of Fn are generated by alternative splicing of the ED-A, ED-B and IIICS region. The inclusion of the IIICS region provides additional proteolytic cleavage sites and modulates the role of the heparin II domain in Wbrillogenesis and cell spreading (Santas et al 2002;Abe et al 2005). Moreover, the IIICS domain is characterized by an alternative de novo O-linked glycosylation.…”
Section: Introductionmentioning
confidence: 99%