Factors and mechanisms determining the formation of fibrillar collagen structures in adsorbed phases

Gurdak, Elzbieta; Rouxhet, Paul; Dupont‐Gillain, Christine C.

doi:10.1016/j.colsurfb.2006.07.011

Cited by 28 publications

(32 citation statements)

References 40 publications

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“…Col IV cannot form gels as it is not fibrillar protein, but it strongly promotes cell adhesion through binding to α1β1 integrin via sequence localized in a spatial vicinity of Asp461 on α1(IV) chain and Arg461on α2(IV) chain (Tuckwell et al, 1994), or via α2β1 integrins which recognize the GFOGER motif in the αI domain (Knight et al, 1998;Zhang et al, 2003). The role of substratum wettability for Col IV assembly and its subsequent biological recognition is not clear, although some recent studies describe the surface arrangement of fibrillar type I collagen (Dupont-Gillain et al, 2005;Gurdak et al, 2006;Keresztes et al, 2006). Our results show that adsorption of FITC-Col IV is strongly dependent on substratum wettability.…”

Section: Discussionmentioning

confidence: 99%

“…However, gels from natural polymers like collagen, gelatin or fibrin are good substrata for cell attachment (Brown et al, 2006;Daley et al, 2008) and work well also in adsorbed state (Tamada and Ikada, 1994;Ludwig et al, 2006). Conversely, strongly hydrophobic surfaces may support cell adhesion, for example, due to the spontaneous protein network assembly (Gurdak et al, 2006;Rodriguez Hernandez et al, 2007;Gugutkov et al, 2009;Gugutkov et al, 2010). Col IV cannot form gels as it is not fibrillar protein, but it strongly promotes cell adhesion through binding to α1β1 integrin via sequence localized in a spatial vicinity of Asp461 on α1(IV) chain and Arg461on α2(IV) chain (Tuckwell et al, 1994), or via α2β1 integrins which recognize the GFOGER motif in the αI domain (Knight et al, 1998;Zhang et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

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Different assembly of type IV collagen on hydrophilic and hydrophobic substrata alters endothelial cells interaction

Coelho

González-García

Planell

et al. 2010

eCM

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Considering the structural role of type IV collagen (Col IV) in the assembly of the basement membrane (BM) and the perspective of mimicking its organization for vascular tissue engineering purposes, we studied the adsorption pattern of this protein on model hydrophilic (clean glass) and hydrophobic trichloro(octadecyl)silane (ODS) surfaces known to strongly affect the behavior of other matrix proteins. The amount of fluorescently labeled Col IV was quantified showing saturation of the surface for concentration of the adsorbing solution of about 50μg/ml, but with approximately twice more adsorbed protein on ODS. AFM studies revealed a fine -nearly single molecular size -network arrangement of Col IV on hydrophilic glass, which turns into a prominent and growing polygonal network consisting of molecular aggregates on hydrophobic ODS. The protein layer forms within minutes in a concentration-dependent manner. We further found that human umbilical vein endothelial cells (HUVEC) attach less efficiently to the aggregated Col IV (on ODS), as judged by the significantly altered cell spreading, focal adhesions formation and the development of actin cytoskeleton. Conversely, the immunofluorescence studies for integrins revealed that the fine Col IV network formed on hydrophilic substrata is better recognized by the cells via both α1 and α2 heterodimers which support cellular interaction, apart from these on hydrophobic ODS where almost no clustering of integrins was observed.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Different assembly of type IV collagen on hydrophilic and hydrophobic substrata alters endothelial cells interaction

Coelho

González-García

Planell

et al. 2010

eCM

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“…3c. The adsorption of collagen on different substrates was studied by Gurdak et al [20]. They found that the fibrils formed in the adsorbed layers are smaller than the fibrils formed in the solutions and do not show the regular band pattern along the fibril length.…”

Section: Adsorption Of Collagen On Bare Mica and Lb Filmsmentioning

confidence: 98%

Network structure of collagen layers absorbed on LB film

Chen

et al. 2007

Journal of Colloid and Interface Science

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“…In fact, this link is well demonstrated for other ECM proteins, including fibronectin, vitronectin, and fibrinogen (Groth et al, 1994;Hernández et al, 2009;Lee et al, 2006;Toromanov et al, 2010), which are uniformly available in the biological fluids (Daley et al, 2008). We anticipate that although non-soluble in physiological conditions (Gurdak et al, 2006) Col IV may also affect significantly the cellular interaction.…”

Section: Discussionmentioning

confidence: 79%

Arrangement of type IV collagen on NH₂ and COOH functionalized surfaces

Coelho

González-García

Salmerón‐Sánchez

et al. 2011

Biotech & Bioengineering

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Apart from the paradigm that cell-biomaterials interaction depends on the adsorption of soluble adhesive proteins we anticipate that upon distinct conditions also other, less soluble ECM proteins such as collagens, associate with the biomaterials interface with consequences for cellular response that might be of significant bioengineering interest. Using atomic force microscopy (AFM) we seek to follow the nanoscale behavior of adsorbed type IV collagen (Col IV)--a unique multifunctional matrix protein involved in the organization of basement membranes (BMs) including vascular ones. We have previously shown that substratum wettability significantly affects Col IV adsorption pattern, and in turn alters endothelial cells interaction. Here we introduce two new model surfaces based on self-assembled monolayers (SAMs), a positively charged -NH(2) , and negatively charged -COOH surface, to learn more about their particular effect on Col IV behavior. AFM studies revealed distinct pattern of Col IV assembly onto the two SAMs resembling different aspects of network-like structure or aggregates (suggesting altered protein conformation). Moreover, the amount of adsorbed FITC-labeled Col IV was quantified and showed about twice more protein on NH(2) substrata. Human umbilical vein endothelial cells attached less efficiently to Col IV adsorbed on negatively charged COOH surface judged by altered cell spreading, focal adhesions formation, and actin cytoskeleton development. Immunofluorescence studies also revealed better Col IV recognition by both α(1) and α(2) integrins on positively charged NH(2) substrata resulting in higher phosphorylated focal adhesion kinase recruitment in the focal adhesion complexes. On COOH surface, no integrin clustering was observed. Taken altogether these results, point to the possibility that combined NH(2) and Col IV functionalization may support endothelization of cardiovascular implants.

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Factors and mechanisms determining the formation of fibrillar collagen structures in adsorbed phases

Cited by 28 publications

References 40 publications

Different assembly of type IV collagen on hydrophilic and hydrophobic substrata alters endothelial cells interaction

Different assembly of type IV collagen on hydrophilic and hydrophobic substrata alters endothelial cells interaction

Network structure of collagen layers absorbed on LB film

Arrangement of type IV collagen on NH₂ and COOH functionalized surfaces

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Factors and mechanisms determining the formation of fibrillar collagen structures in adsorbed phases

Cited by 28 publications

References 40 publications

Different assembly of type IV collagen on hydrophilic and hydrophobic substrata alters endothelial cells interaction

Different assembly of type IV collagen on hydrophilic and hydrophobic substrata alters endothelial cells interaction

Network structure of collagen layers absorbed on LB film

Arrangement of type IV collagen on NH2 and COOH functionalized surfaces

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Arrangement of type IV collagen on NH₂ and COOH functionalized surfaces