Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results.

Williams, Benfeard; Gelman, Robert A.; Poppke, D C; Piez, Karl A.

doi:10.1016/s0021-9258(19)46970-6

Cited by 451 publications

(175 citation statements)

References 25 publications

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“…COL was evident in the main body of the fiber, as well as in the radial arrangement of fibrils on the droplet surface, which had yet to collapse into one fiber. Fibers produced from unlabeled protein solutions were imaged by scanning electron microscopy (SEM) (Figures 4C and 4D), where we observed a decrease in the average diameter from 2.54 G 0.27 mm to 1.54 G 0.06 mm because of the addition of COL. SEM images did not reveal the characteristic banding pattern associated with COL, 44 which suggested that COL may reside below a top layer of FN fibrils. To gain insight into the molecular arrangement of COL within the predominantly FN fibers, we used Fourier transform infrared (FTIR) spectroscopy to help clarify whether COL fibrils were present in the fibers produced from 1:1 FN:COL solution.…”

Section: Fn Induces Col Assemblymentioning

confidence: 94%

Molecular Interactions between Collagen and Fibronectin: A Reciprocal Relationship that Regulates De Novo Fibrillogenesis

Paten

Martin

Wanis

et al. 2019

Chem

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Determining the fundamental mechanisms underlying tissue formation and wound healing allows for bio-inspired approaches that leverage the best practices of biology, as decided upon by millions of years of evolution. To gain insight into how tissue is built, we have studied the interactions between two of the principal proteins found in connective tissues: collagen and fibronectin. We have confirmed a binding affinity in solution, which supports a reciprocal relationship whereby the assembly pathway of one catalyzes the other. The molecular synergy enables complex extracellular matrix formation with a range of mechanical properties.

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Section: Fn Induces Col Assemblymentioning

confidence: 94%

Molecular Interactions between Collagen and Fibronectin: A Reciprocal Relationship that Regulates De Novo Fibrillogenesis

Paten

Martin

Wanis

et al. 2019

Chem

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“…It has been appreciated for more than 40 years that solubilized, tissue-extracted collagen will polymerize spontaneously when physiological pH, temperature, and ionic strength are restored. [5][6][7] Collagen fibrils can also be generated in vitro by subjecting soluble type I procollagen to sequential cleavage of its propeptide termini by procollagen metalloproteinases. This action reduces the solubility of the protein and initiates the entropy-driven self-assembly process.…”

mentioning

confidence: 99%

“…3,10 Moreover, both approaches have been valuable for elucidating conditions for collagen self-assembly and in defining controlling elements for this within the collagen molecule. 7,11 Self-assembly however cannot by itself explain the diverse morphology of collagen fibrils found in tissues, and determinants other than those intrinsic to the collagen molecule are likely required. In this regard, collagen-associating ECM molecules, including decorin, fibromodulin, and lumican, have been found to impact the size and architecture of type I collagen fibrils.…”

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confidence: 99%

Vascular Smooth Muscle Cells Orchestrate the Assembly of Type I Collagen via α2β1 Integrin, RhoA, and Fibronectin Polymerization

Diepstraten

D’Souza

et al. 2003

The American Journal of Pathology

151

143

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Assembly of collagen into fibrils is widely studied as a spontaneous and entropy-driven process. To determine whether vascular smooth muscle cells (SMCs) impact the formation of collagen fibrils, we microscopically tracked the conversion of soluble to insoluble collagen in human SMC cultures, using fluorescent type I collagen at concentrations less than that which supported self-assembly. Collagen microaggregates were found to form on the cell surface, initially as punctate collections and then as an increasingly intricate network of fibrils. These fibrils displayed 67-nm periodicity and were found in membrane-delimited cellular invaginations. Fibril assembly was inhibited by an anti-alpha2beta1 integrin antibody and accelerated by an alpha2beta1 integrin antibody that stimulates a high-affinity binding state. Newly assembled collagen fibrils were also found to co-localize with newly assembled fibronectin fibrils. Moreover, inhibition of fibronectin assembly with an anti-alpha5beta1 integrin antibody completely inhibited collagen assembly. Collagen fibril formation was also linked to the cytoskeleton. Fibrils formed on the stretched tails of SMCs, ran parallel to actin microfilament bundles, and formed poorly on SMCs transduced with retrovirus containing cDNA for dominant-negative RhoA and robustly on SMCs expressing constitutively active RhoA. Lysophosphatidic acid, which activates RhoA and stimulates fibronectin assembly, stimulated collagen fibril formation, establishing for the first time that collagen polymerization can be regulated by soluble agonists of cell function. Thus, collagen fibril formation is under close cellular control and is dynamically integrated with fibronectin assembly, opening new possibilities for modifying collagen deposition.

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“…The influence of buffer composition on fibril formation has been studied by several authors, notably by Williams et al (1978) who recommended diluting cold solutions of collagen I at concentrations up to 1 mg/ml in 5 mM acetic acid with an equal volume of optimum buffer consisting of 60 mM TES (N-[tris (hydroxymethyl)methyl-2-amino]ethanesulphonic acid), 60 mM sodium phosphate, 270 mM NaCl, pH 7.3, and then raising the temperature to up to 30 • C. In these conditions, fibril morphology is optimized, as judged by the presence of compact fibrils with a clear D-periodic banding pattern. The presence of phosphate is important for producing well-banded fibrils.…”

Section: Reconstitution Of Fibrils In Vitromentioning

confidence: 99%

Collagen Diversity, Synthesis and Assembly

Hulmes¹

Collagen

146

169

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The vertebrate collagen superfamily now includes over 50 collagens and collagen-like proteins. Here, their different structures are described, as well as their diverse forms of supramolecular assembly. Also presented here are the various steps in collagen biosynthesis, both intracellular and extracellular, and the functions of the collagen-specific post-translational modifications. Assembly of collagen fibrils, both in vitro and in vivo, is reviewed, including the mechanisms that control this process and the interactions involved. Finally, recent developments in the supramolecular assembly of collagen-like peptides are discussed.

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Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results.

Cited by 451 publications

References 25 publications

Molecular Interactions between Collagen and Fibronectin: A Reciprocal Relationship that Regulates De Novo Fibrillogenesis

Molecular Interactions between Collagen and Fibronectin: A Reciprocal Relationship that Regulates De Novo Fibrillogenesis

Vascular Smooth Muscle Cells Orchestrate the Assembly of Type I Collagen via α2β1 Integrin, RhoA, and Fibronectin Polymerization

Collagen Diversity, Synthesis and Assembly

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