1982
DOI: 10.1016/s0021-9258(18)33379-9
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Conformational states of fibronectin. Effects of pH, ionic strength, and collagen binding.

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Cited by 208 publications
(55 citation statements)
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“…Though it was widely hypothesized that COL-mediated FN unfolding was responsible for FN fibril growth away from the cell surface, 29,40,41 the adjustment to physiological temperature dominated the unfolding observed in our study and not FN's interaction with COL. This key finding indicates that COL may have been misidentified as the driver of FN allosteric unfolding.…”
Section: Discussioncontrasting
confidence: 48%
See 1 more Smart Citation
“…Though it was widely hypothesized that COL-mediated FN unfolding was responsible for FN fibril growth away from the cell surface, 29,40,41 the adjustment to physiological temperature dominated the unfolding observed in our study and not FN's interaction with COL. This key finding indicates that COL may have been misidentified as the driver of FN allosteric unfolding.…”
Section: Discussioncontrasting
confidence: 48%
“…Intramolecular FRET: Thermal Relaxation Drives FN Unfolding It has been hypothesized that COL binding may induce an allosteric conformational unfolding of FN necessary to enable FN-FN binding, such that FN fibril growth could precede away from the cell surface; 29,40,41 however, this has never been confirmed with intact proteins. To test this hypothesis, we dual labeled FN for FRET and spectrophotometrically measured the I A /I D to determine whether FN experienced conformational unfolding in the presence of increasing molar ratios of COL (Figure 1A, bottom).…”
Section: Resultsmentioning
confidence: 99%
“…It is thought that Fn changes conformation and undergoes a surface activation when it becomes bound to certain other molecules or substrates, such as gelatin, collagen, or plastic (1). Williams et al have demonstrated that plasma Fn exists in a folded globular configuration under physiological conditions and that it can unfold as the pH or ionic strength increases or as it interacts with certain other molecules (35). The same type of unfolding may also occur as Fn interacts with and becomes immobilized on a collagen matrix, and this unfolding could expose new sites which then support S. sanguis adherence.…”
Section: Discussionmentioning
confidence: 99%
“…Decreasing the pH may also affect the binding sites on fibronectin. Several studies have shown that fibronectin undergoes conformational changes in response to pH changes (50). It is possible that these conformational changes also affect the VEGF and ECD-binding sites on fibronectin.…”
Section: Binding Cycle Acidic Ph Neutral Phmentioning
confidence: 99%