2019
DOI: 10.1016/j.biomaterials.2018.12.010
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Fibril bending stiffness of 3D collagen matrices instructs spreading and clustering of invasive and non-invasive breast cancer cells

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Cited by 66 publications
(66 citation statements)
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“…Among five collagen parameters (alignment, density, width, length, and straightness), increased collagen width is the most powerful parameter for predicting cancer prognosis [175]. The elasticity of the collagen matrix is controlled by fibril bending stiffness rather than by fibril diameter or intrafibrillar crosslinking [176]. Increased collagen fiber alignment, elevated levels of immunoreactive glycosaminoglycans such as heparan sulfate and chondroitin sulfate, and decreased levels of the proteoglycan decorin enhance the stiffness of carcinoma tissues [177].…”
Section: Subtype Of Mmps Associated Collagen Pathological Functions Omentioning
confidence: 99%
“…Among five collagen parameters (alignment, density, width, length, and straightness), increased collagen width is the most powerful parameter for predicting cancer prognosis [175]. The elasticity of the collagen matrix is controlled by fibril bending stiffness rather than by fibril diameter or intrafibrillar crosslinking [176]. Increased collagen fiber alignment, elevated levels of immunoreactive glycosaminoglycans such as heparan sulfate and chondroitin sulfate, and decreased levels of the proteoglycan decorin enhance the stiffness of carcinoma tissues [177].…”
Section: Subtype Of Mmps Associated Collagen Pathological Functions Omentioning
confidence: 99%
“…To reconstitution of collagen matrices, rat-tail type I collagen (Corning, NY, USA) was mixed with 250 mM phosphate buffer at pH 7.5, as previously reported. 37,38 The collagen fibrillation was introduced by incubation at 37°C and 95% humidity. After 5 days of cultivation, cells were lysed with double-distilled water for 1 h at room temperature.…”
Section: Induction and Characterization Of Has2-kd Fibroblastsmentioning
confidence: 99%
“…Rat-tail type I collagen (Corning, USA) was mixed with 250 mM phosphate buffer at pH 7.5 to archive collagen concentration of 2 mg ml −1 , as previously reported. 37,38 Matrices were fibrillated by incubation at 37°C and 95% humidity. HA with a molecular weight of 34 kDa (low molecular weight HA, LMW-HA) and 1170 kDa (HMW-HA) were prepared in 100 mM MES buffer at pH 5.…”
Section: Reconstitution Of Defined Ha-immobilized Collagen Matrices (mentioning
confidence: 99%
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