Collagen fibril formation. Evidence for a multistep process.

Gelman, Robert A.; Williams, Benfeard; Piez, Karl A.

doi:10.1016/s0021-9258(17)30289-2

Cited by 218 publications

(52 citation statements)

References 14 publications

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“…We did not find normal collagen fibrils in our preparations. This is consistent with observation of a large temperature effect on the rate of fibrillogenesis of normal collagen (Gelman et al, 1979). At the temperature at which we conduct FLS assembly, we have not been able to form normal collagen fibrils within any reasonable time period with our standard procedure.…”

Section: Resultssupporting

confidence: 89%

Fibrous Long Spacing Collagen Ultrastructure Elucidated by Atomic Force Microscopy

Paige

Rainey

Goh

1998

Biophysical Journal

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Fibrous long spacing collagen (FLS) fibrils are collagen fibrils in which the periodicity is clearly greater than the 67-nm periodicity of native collagen. FLS fibrils were formed in vitro by the addition of alpha1-acid glycoprotein to an acidified solution of monomeric collagen and were imaged with atomic force microscopy. The fibrils formed were typically approximately 150 nm in diameter and had a distinct banding pattern with a 250-nm periodicity. At higher resolution, the mature FLS fibrils showed ultrastructure, both on the bands and in the interband region, which appears as protofibrils aligned along the main fibril axis. The alignment of protofibrils produced grooves along the main fibril, which were 2 nm deep and 20 nm in width. Examination of the tips of FLS fibrils suggests that they grow via the merging of protofibrils to the tip, followed by the entanglement and, ultimately, the tight packing of protofibrils. A comparison is made with native collagen in terms of structure and mechanism of assembly.

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Section: Resultssupporting

confidence: 89%

Fibrous Long Spacing Collagen Ultrastructure Elucidated by Atomic Force Microscopy

Paige

Rainey

Goh

1998

Biophysical Journal

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“…Since COL and FN were shown to bind in solution at 37 C, we then applied a turbidimetric analysis to determine how the kinetics of COL assembly were affected by the presence of FN. As a standard assay for COL polymerization in vitro, 42 turbidity measurements enable the identification of key parameters calculated from the absorbance plots: the duration of the lag phase (defined as the time to reach 10% steady-state absorbance), the steady-state absorbance, and the linear growth assembly rate (Figure 2A; Table 1). Prior to experimentation, we evaluated an FNonly solution to ensure that the optical density was not directly affected by the variable amounts of FN at any time in the experiment (Figure 2B).…”

Section: Fn Regulates Col Assemblymentioning

confidence: 99%

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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“…This behavior is characteristic of a cooperative nucleation and growth mechanism. However, uncertainty remains about the exact nature of the nucleus and the degree of cooperativity (17)(18)(19)(20)(21) and about the mechanism of growth (22)(23)(24)(25). There is some evidence that five-stranded microfibrils are already formed during the turbidimetric lag phase, which subsequently grow linearly and laterally during the growth phase (16,18).…”

Section: Introductionmentioning

confidence: 99%

“…As a model system, we use collagen whose telopeptides are removed by pepsin. This is necessary to prevent spontaneous formation of intermolecular covalent cross-links (17,46,(50)(51)(52). We used several complementary methods to characterize the kinetics of cold-induced disassembly of collagen fibrils formed at body temperature (37 C): we used turbimetry to probe the fraction of collagen in fibril form, atomic force microscopy (AFM) to probe the fibril morphology, and confocal microscopy and rheometry to measure the network connectivity.…”

Section: Introductionmentioning

confidence: 99%

Thermal Memory in Self-Assembled Collagen Fibril Networks

Wild

Pomp

Koenderink

2013

Biophysical Journal

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Collagen fibrils form extracellular networks that regulate cell functions and provide mechanical strength to tissues. Collagen fibrillogenesis is an entropy-driven process promoted by warming and reversed by cooling. Here, we investigate the influence of noncovalent interactions mediated by the collagen triple helix on fibril stability. We measure the kinetics of cold-induced disassembly of fibrils formed from purified collagen I using turbimetry, probe the fibril morphology by atomic force microscopy, and measure the network connectivity by confocal microscopy and rheometry. We demonstrate that collagen fibrils disassemble by subunit release from their sides as well as their ends, with complex kinetics involving an initial fast release followed by a slow release. Surprisingly, the fibrils are gradually stabilized over time, leading to thermal memory. This dynamic stabilization may reflect structural plasticity of the collagen fibrils arising from their complex structure. In addition, we propose that the polymeric nature of collagen monomers may lead to slow kinetics of subunit desorption from the fibril surface. Dynamic stabilization of fibrils may be relevant in the initial stages of collagen assembly during embryogenesis, fibrosis, and wound healing. Moreover, our results are relevant for tissue repair and drug delivery applications, where it is crucial to control fibril stability.

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Collagen fibril formation. Evidence for a multistep process.

Cited by 218 publications

References 14 publications

Fibrous Long Spacing Collagen Ultrastructure Elucidated by Atomic Force Microscopy

Fibrous Long Spacing Collagen Ultrastructure Elucidated by Atomic Force Microscopy

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

Thermal Memory in Self-Assembled Collagen Fibril Networks

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