Collagen fibril organization in chicken and porcine skeletal muscle perimysium under applied tension and compression

Mohammadkhah, Melika; Murphy, Paula; Simms, Ciaran

doi:10.1016/j.jmbbm.2017.08.007

Cited by 24 publications

(17 citation statements)

References 44 publications

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“…The oxidized peptides obtained from exposed samples could have been generated due to a higher susceptibility of collagen to suffer oxidation reactions, because its abundance in muscle is lower (10%) than sarcoplasmic and myofibrillar proteins (Mohammadkhah, Murphy, & Simms, 2018). This fact is in agreement with the distribution of total peptides obtained after digestion in exposed and control samples (Fig.…”

Section: Identification Of Oxidized Peptides Obtained After Simulated Gi Digestionsupporting

confidence: 85%

“…Additionally, collagen is approximately 10% of skeletal muscle volume and its function is associated with extracellular matrix (ECM), where it is the main protein. In muscle, the ECM organizes the fibers and participates as a retaining mechanism during deformation (Mohammadkhah et al, 2018). In this sense, collagen oxidation promoted by chlorpyrifos residues in in vivo conditions could affect the animal welfare, since carbonylation is associated to the loss of protein functionality (Estévez, 2015;Estévez, 2011).…”

Section: Identification Of Oxidized Peptides Obtained After Simulated Gi Digestionmentioning

confidence: 99%

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In vitro oxidation promoted by chlorpyrifos residues on myosin and chicken breast proteins

Lázaro¹,

Mora

Méndez-Cuadro

et al. 2020

Food Chemistry

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Organophosphate pesticides are frequently used to eliminate or prevent insects in poultry. However, their residues may continue in meat after slaughtering. In this study, proteomics and peptidomics approaches were used to evaluate their oxidative impact on myosin and chicken breast proteins under in vitro conditions. Myosin protein was exposed to diazinon and chlorpyrifos showing an increase in its oxidation by increasing times, especially with chlorpyrifos.Then, chicken breast was contaminated with chlorpyrifos to evaluate carbonylation and the effect of simulated gastrointestinal digestion. Proteins were isolated using size-exclusionchromatography and identified by mass spectrometry in tandem. Myosin, β-enolase, CK-M-type and actin were identified as main proteins susceptible to oxidation. Also, oxidised peptides obtained before and after simulated gastrointestinal digestion were identified.Collagen peptides the most susceptible to oxidation. These results suggest that the presence of chlorpyrifos residues on meat could have a negative effect on its final quality and nutritional value.

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Section: Identification Of Oxidized Peptides Obtained After Simulated Gi Digestionsupporting

confidence: 85%

Section: Identification Of Oxidized Peptides Obtained After Simulated Gi Digestionmentioning

confidence: 99%

In vitro oxidation promoted by chlorpyrifos residues on myosin and chicken breast proteins

Lázaro¹,

Mora

Méndez-Cuadro

et al. 2020

Food Chemistry

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“…Our use of a single modulus term is a simplification of a highly complex combination of ECM collagen amount, type, crosslinking, and crimp. While these each have been studied in regards to tissue stiffness through either experimentation (Smith and Barton, 2014;Chapman et al, 2015;Mohammadkhah et al, 2018;Lieber and Fridén, 2019;Smith et al, 2019) or modeling (Gindre et al, 2013;Bleiler et al, 2019; FIGURE 8 | Parametric study stress-stretch curves for (A) uniaxial stretch and (B) biaxial stretch. Note that for both models (Aligned -solid curves and Disperseddashed curves) they exhibit nearly identical uniaxial behavior for both longitudinal (back curves) and transverse (blue curves), but distinctly different behavior when subject to biaxial stretch, with percentage differences between Aligned and Dispersed shown at λ = 1.3.…”

Section: Constitutive Modeling Of Experimental Datamentioning

confidence: 99%

Investigating Passive Muscle Mechanics With Biaxial Stretch

Wheatley

2020

Front. Physiol.

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Introduction: The passive stiffness of skeletal muscle can drastically affect muscle function in vivo, such as the case for fibrotic tissue or patients with cerebral palsy. The two constituents of skeletal muscle that dominate passive stiffness are the intracellular protein titin and the collagenous extracellular matrix (ECM). However, efforts to correlate stiffness and measurements of specific muscle constituents have been mixed, and thus the complete mechanisms for changes to muscle stiffness remain unknown. We hypothesize that biaxial stretch can provide an improved approach to evaluating passive muscle stiffness. Methods: We performed planar biaxial materials testing of passively stretched skeletal muscle and identified three previously published datasets of uniaxial materials testing. We developed and employed a constitutive model of passive skeletal muscle that includes aligned muscle fibers and dispersed ECM collagen fibers with a bimodal von Mises distribution. Parametric modeling studies and fits to experimental data (both biaxial and previously published) were completed. Results: Biaxial data exhibited differences in time dependent behavior based on orientation (p < 0.0001), suggesting different mechanisms supporting load in the direction of muscle fibers (longitudinal) and in the perpendicular (transverse) directions. Model parametric studies and fits to experimental data exhibited the robustness of the model (<20% error) and how differences in tissue stiffness may not be observed in uniaxial longitudinal stretch, but are apparent in biaxial stretch. Conclusion: This work presents novel materials testing data of passively stretched skeletal muscle and use of constitutive modeling and finite element analysis to explore the interaction between stiffness, constituent variability, and applied deformation in passive skeletal muscle. The results highlight the importance of biaxial stretch in evaluating muscle stiffness and in further considering the role of ECM collagen in modulating passive muscle stiffness.

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“…The active response of skeletal muscle is responsible for the contractile behavior, usually refers to the response of the muscular fiber [11,12]. Meanwhile, the passive mechanical properties of skeletal muscle clearly depend on the size, orientation, and organizational arrangement of collagen fibers, particularly in the perimysium [38]. These pathologic changes of collagen hyperplasia induce muscle contracture and finally increased passive stiffness [39,40].…”

Section: Collagen and The Mechanical Properties Of Pvmmentioning

confidence: 99%

Exploring the Pathological Role of Collagen in Paravertebral Muscle in the Progression of Idiopathic Scoliosis

Peng

Jin

Meng

et al. 2020

BioMed Research International

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Background. Paravertebral muscle (PVM) is considered as a contributing factor of idiopathic scoliosis (IS); collagen is crucial for maintaining the mechanical properties of PVM, but only a few researches have described this field. In this study, we observed the muscle stiffness of PVM and the curvature of the spine by adjusting the content of collagen in PVM of rats and explored the role of collagen in the progression of IS. Methods. 32 female Sprague Dawley rats were randomly divided into four groups: neutralizing antibody (NA) group (group 1), normal control group (group 2), IS group (group 3), and IS with NA group (group 4). TGF-β1 NA was injected into PVM in group 1 and group 4, while Normal saline in group 2 and group 3. The Cobb angle and muscle stiffness were measured before and after injection; the rats were sacrificed at one week after injection, and performed histological, Western Blot, and qRT-PCR examinations. Results. X-rays showed that scoliosis occurred in group 1 and relieved in group 4. The stiffness of PVM was decreased significantly on the convex side in group 1, while on the concave side in group 4. The expression of TGF-β1 and COL1 on the concave side in IS rats (group 3) was significantly increased than that in normal rats (group 2), the concentration of COL1 and COL3 in group 3 was significantly higher than that in group 2, and the addition of TGF-β1 NA significantly downregulated COL1 and COL3 in group 1 and group 4. The concentration of COL1 in convex PVM was negatively related to Cobb angle in group 1 and group 2, and in concave PVM was positively related to Cobb angle in group 3 and group 4. However, no significant correlation was found between COL3 and Cobb angle in group 3 and group 4. Conclusions. Asymmetric biomechanical characteristics of PVM was an important etiological factor of IS, which was directly correlated with collagen, it could be adjusted by local intramuscular injecting of TGF-β1 NA, and finally had an effect on the shape of the spine.

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Collagen fibril organization in chicken and porcine skeletal muscle perimysium under applied tension and compression

Cited by 24 publications

References 44 publications

In vitro oxidation promoted by chlorpyrifos residues on myosin and chicken breast proteins

In vitro oxidation promoted by chlorpyrifos residues on myosin and chicken breast proteins

Investigating Passive Muscle Mechanics With Biaxial Stretch

Exploring the Pathological Role of Collagen in Paravertebral Muscle in the Progression of Idiopathic Scoliosis

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