Relative orientation of collagen molecules within a fibril: a homology model for<i>homo sapiens</i>type I collagen

Collier, Thomas A.; Nash, Anthony; Birch, Helen L.; Leeuw, Nora H. de

doi:10.1080/07391102.2018.1433553

Cited by 8 publications

(9 citation statements)

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“…This chronic inflammation response may induce parenchymal tissue destruction and recomposition of extracellular matrix (ECM). In the lung, type I collagen could form a tight fibrillar network throughout the large conducting airways, bronchi, and bronchioles, providing the mechanical strength and stability required for their proper functions 6,7. Furthermore, among a variety of proteins participating in the progression of small airway remodeling in COPD, type I collagen was the predominant constituent of the altered ECM composition 8…”

Section: Introductionmentioning

confidence: 99%

“…Then, after shedding the C-terminus trimeric nucleus which is known as procollagen type I C-terminal peptide (PICP), the trimer is deposited in tissues as the insoluble fibrillary collagen. Additionally, mature type I collagen with type-specific collagen cross-links can liberate from tissues and regain solubility via enzymatic degradation into small fragments, and the C-terminal telopeptide is known as C-terminal telopeptide of type I collagen (ICTP) 6,9. Therefore, the expression and release of PICP and ICTP could reflect the ongoing turnover of deposition and degradation of type I collagen in tissues.…”

Section: Introductionmentioning

confidence: 99%

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Altered serum levels of type I collagen turnover indicators accompanied by IL-6 and IL-8 release in stable COPD

Zeng¹,

Hu²,

Zuo³

et al. 2019

COPD

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BackgroundCOPD, characterized by chronic inflammation and airway remodeling, has significant pathological alterations in composition and deposition of the extracellular matrix. The expression of procollagen 1 C-terminal peptide (PICP) and collagen type 1 C-terminal telopeptide (ICTP), two major by-products in the synthesis and degradation of collagen, was shown to be positively correlated with inflammatory mediator levels in previous studies.PurposeIn this study, we investigated whether the serum concentrations of PICP and ICTP were associated with the inflammation level for patients with stable COPD.Patients and methodsWe collected serum samples from 25 control subjects and 20 patients with stable COPD from December 2011 to October 2012 in Shanghai Zhongshan Hospital and Shanghai Dahua Hospital. We determined concentrations of PICP, ICTP, C-reactive protein (CRP), IL-6, IL-8, and tumor necrosis factor (TNF)-α by using enzyme-linked immunosorbent assay methods.ResultsDemographic characteristics were comparable between the two groups. In patients with stable COPD, serum levels of CRP, IL-6, IL-8, and TNF-α were all elevated compared to control subjects, but only changes of IL-6 achieved statistical significance. Serum concentration of PICP was significantly elevated in patients with COPD, and level of ICTP was slightly decreased. Moreover, serum concentrations of PICP were positively correlated with the levels of both IL-6 and IL-8.ConclusionThe increased levels of serum PICP in COPD might indicate the condition of airway remodeling, and IL-6 and/or IL-8 might play an important role in stimulating collagen synthesis.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Altered serum levels of type I collagen turnover indicators accompanied by IL-6 and IL-8 release in stable COPD

Zeng¹,

Hu²,

Zuo³

et al. 2019

COPD

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“…The long-term relaxation behaviour was predicted by three factors: (1) more densely packed collagen, as reflected by hydroxyproline, resulted in greater magnitude or recruitment (E 2 ) and shorter duration of fast relaxation (τ 2 ), (2) proteoglycans increased the duration of the long-term relaxation (η 2 , τ 2 ) and (3) a high crimp angle increased the magnitude or recruitment of long-term relaxation (E 2 ). We speculate the long-term relaxation to originate mainly from the collagen fibrils [21,22,27], perhaps from molecular rearrangement inside the fibril, or fibrillar network reorganization. Dense packing has more fibrils per area, and thus more fibrils are involved, leading to higher magnitude or recruitment of relaxation.…”

Section: Structure-function Relationshipsmentioning

confidence: 96%

“…When ligaments and tendons are stretched, the relaxation occurs at the levels of collagen fibril [21][22][23], fibre [23,24], fascicle [23][24][25] and tissue [26]. The fibril level relaxation possibly originates from molecular interactions and fluid flow inside the fibrils [27] and fibrils may slide relative to each other inside fibres [23] causing fibre relaxation. Fascicle relaxation was shown to occur primarily through between-fibre sliding [23,24].…”

Section: Introductionmentioning

confidence: 99%

Structure, composition and fibril-reinforced poroviscoelastic properties of bovine knee ligaments and patellar tendon

Ristaniemi

Regmi

Mondal

et al. 2021

J. R. Soc. Interface.

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Tissue-level stress-relaxation of ligaments and tendons in the toe region is characterized by fast and long-term relaxations and an increase in relaxation magnitude with strain. Characterizing the compositional and structural origins of these phenomena helps in the understanding of mechanisms of ligament and tendon function and adaptation in health and disease. A three-step tensile stress-relaxation test was conducted on dumbbell-shaped pieces of bovine knee ligaments and patellar tendon (PT) ( n = 10 knees). Their mechanical behaviour was characterized by a fibril-reinforced poroviscoelastic material model, able to describe characteristic times and magnitudes of fast and long-term relaxations. The crimp angle and length of tissues were measured with polarized light microscopy, while biochemical contents were determined by colorimetric biochemical methods. The long-term relaxation time was longer in the anterior cruciate ligament (ACL) and PT compared with collateral ligaments ( p < 0.05). High hydroxyproline content predicted greater magnitude and shorter time of both fast and long-term relaxation. High uronic acid content predicted longer time of long-term relaxation, whereas high crimp angle predicted higher magnitude of long-term relaxation. ACL and PT are better long-term stabilizers than collateral ligaments. The long-term relaxation behaviour is affected or implied by proteoglycans and crimp angle, possibly relating to slow structural reorganization of the tissue.

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“…We have demonstrated previously [26,27] that our MD approach reproduces experimentally observed structural and mechanical properties of hydroxylated rat type I collagen. Additionally, MD simulations have also been employed to gain molecular insights into monomer stability [31], selfassembly of fibrils [31,32], inter-monomer cross-linking in fibrils [33], fibril elasticity [27], surface accessibility of protein binding sites [34], and relative orientations of monomers in fibrils [35].…”

Section: ~ 67 Nm Fibrilmentioning

confidence: 99%

Contrasting Local and Macroscopic Effects of Collagen Hydroxylation

Varma

Orgel

Schieber

2021

IJMS

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Collagen is heavily hydroxylated. Experiments show that proline hydroxylation is important to triple helix (monomer) stability, fibril assembly, and interaction of fibrils with other molecules. Nevertheless, experiments also show that even without hydroxylation, type I collagen does assemble into its native D-banded fibrillar structure. This raises two questions. Firstly, even though hydroxylation removal marginally affects macroscopic structure, how does such an extensive chemical change, which is expected to substantially reduce hydrogen bonding capacity, affect local structure? Secondly, how does such a chemical perturbation, which is expected to substantially decrease electrostatic attraction between monomers, affect collagen’s mechanical properties? To address these issues, we conduct a benchmarked molecular dynamics study of rat type I fibrils in the presence and absence of hydroxylation. Our simulations reproduce the experimental observation that hydroxylation removal has a minimal effect on collagen’s D-band length. We also find that the gap-overlap ratio, monomer width and monomer length are minimally affected. Surprisingly, we find that de-hydroxylation also has a minor effect on the fibril’s Young’s modulus, and elastic stress build up is also accompanied by tightening of triple-helix windings. In terms of local structure, de-hydroxylation does result in a substantial drop (23%) in inter-monomer hydrogen bonding. However, at the same time, the local structures and inter-monomer hydrogen bonding networks of non-hydroxylated amino acids are also affected. It seems that it is this intrinsic plasticity in inter-monomer interactions that preclude fibrils from undergoing any large changes in macroscopic properties. Nevertheless, changes in local structure can be expected to directly impact collagen’s interaction with extra-cellular matrix proteins. In general, this study highlights a key challenge in tissue engineering and medicine related to mapping collagen chemistry to macroscopic properties but suggests a path forward to address it using molecular dynamics simulations.

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Relative orientation of collagen molecules within a fibril: a homology model forhomo sapienstype I collagen

Cited by 8 publications

References 50 publications

Altered serum levels of type I collagen turnover indicators accompanied by IL-6 and IL-8 release in stable COPD

Altered serum levels of type I collagen turnover indicators accompanied by IL-6 and IL-8 release in stable COPD

Structure, composition and fibril-reinforced poroviscoelastic properties of bovine knee ligaments and patellar tendon

Contrasting Local and Macroscopic Effects of Collagen Hydroxylation

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