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  1. Atomic models for the polypeptide backbones of myohemerythrin and hemerythrin
    Hendrickson WA, Ward KB
    Biochem Biophys Res Commun, 1975 Oct 27;66(4):1349-56.
    PMID: 5
    Matched MeSH terms: Muscle Proteins*
  2. Improving animal welfare status and meat quality through assessment of stress biomarkers: A critical review
    Kumar P, Ahmed MA, Abubakar AA, Hayat MN, Kaka U, Ajat M, et al.
    Meat Sci, 2023 Mar;197:109048.
    PMID: 36469986 DOI: 10.1016/j.meatsci.2022.109048
    Stress induces various physiological and biochemical alterations in the animal body, which are used to assess the stress status of animals. Blood profiles, serum hormones, enzymes, and physiological conditions such as body temperature, heart, and breathing rate of animals are the most commonly used stress biomarkers in the livestock sector. Previous exposure, genetics, stress adaptation, intensity, duration, and rearing practices result in wide intra- and inter-animal variations in the expression of various stress biomarkers. The use of meat proteomics by adequately analyzing the expression of various muscle proteins such as heat shock proteins (HSPs), acute phase proteins (APPs), texture, and tenderness biomarkers help predict meat quality and stress in animals before slaughter. Thus, there is a need to identify non-invasive, rapid, and accurate stress biomarkers that can objectively assess stress in animals. The present manuscript critically reviews various aspects of stress biomarkers in animals and their application in mitigating preslaughter stress in meat production.
    Matched MeSH terms: Muscle Proteins/metabolism
  3. Effects of pH on the functional properties of chicken muscle proteins- modified waxy cornstarch blends
    Zhang Q, Noryati I, Cheng LH
    J Food Sci, 2008 Mar;73(2):E82-7.
    PMID: 18298729 DOI: 10.1111/j.1750-3841.2007.00627.x
    Chicken breast muscle powder (CBMP) and modified waxy cornstarch (MWCS) blends were prepared at different pH conditions (pH 4, 5, 6, 7, 8, and 9). The blends were characterized by light microscopy, frequency sweep, flow analysis, and freeze-thaw stability analysis. Light microscopy showed that the blend structure was coarse at pH conditions close to the isoelectric point of protein and became finer with increasing pH. Frequency sweep demonstrated that the blend was more liquid-like with relatively lower storage (G') and loss (G'') moduli as the pH was increased from pH 4 to pH 9. Flow analysis revealed that thixotropy behavior was evident in samples treated at pHs 4 and 5, whereas antithixotropy was shown by those adjusted to pHs 6, 7, 8, and 9. The CBMP-MWCS blends were found to show better freeze-thaw stability at pH 8 that could be attributed to the formation of a highly interactive network structure of CBMP and MWCS.
    Matched MeSH terms: Muscle Proteins/physiology; Muscle Proteins/chemistry*
  4. Structural and gel property changes in chicken myofibrillar protein induced by argon cold plasma-activated water: With a molecular docking perspective
    Li J, Rao W, Sun Y, Zhou C, Xia Q, He J, et al.
    Food Res Int, 2024 Dec;197(Pt 1):115271.
    PMID: 39593348 DOI: 10.1016/j.foodres.2024.115271
    This study investigated the effects of plasma-activated water (PAW) generated with argon at discharge times of 0, 4, 8, 12, and 16 min on the gel properties and structures of chicken myofibrillar protein (MP). Under treatments of 8, 12, and 16 min, both the gel strength and water retention capacity of MP significantly improved, with the gel strength (0.53 N) peaking at 16 min and the lowest cooking loss（30.38 %）. As the treatment time increased from 0 to 16 min, the storage modulus also gradually increased. Results from low-field nuclear magnetic resonance indicated a slowing of water proton mobility, with the proportion of bound water rising from 0.26 % (0 min) to 0.52 % at 16 min. Fourier transform infrared spectroscopy, endogenous fluorescence spectroscopy and scanning electron microscopy confirmed PAW's alteration of MP's secondary and tertiary structures and gel microstructure. Additionally, this study explored the influence of argon PAW's primary active species on MP from a molecular docking perspective·H2O2 could form hydrogen bonds with MP, while O3 and NO2‾could interact via both hydrogen bonds and electrostatic interactions. Thus, PAW can alter protein structure and enhance MP's functional properties, providing insights for applying cold plasma in processing chicken gel products.
    Matched MeSH terms: Muscle Proteins/metabolism; Muscle Proteins/chemistry
  5. Physicochemical properties and sensory analysis of duck meatballs containing duck meat surimi-like material during frozen storage
    Nurkhoeriyati T, Huda N, Ahmad R
    J Food Sci, 2012 Jan;77(1):S91-8.
    PMID: 22260136 DOI: 10.1111/j.1750-3841.2011.02519.x
    The physicochemical properties and sensory analysis of duck meatballs containing duck meat surimi-like material during frozen storage were evaluated. Properties of meatballs containing duck surimi-like material prepared by acid solubilization (ACDS), alkaline solubilization (ALDS), and conventional processing (CDS) as well as duck mince (as the control, CON) were compared. ACDS had significantly higher (P < 0.05) moisture and protein content and lower fat content compared with CON. The thiobarbituric acid-reactive substances (TBARS) value of all samples increased as the storage time increased up to week 8 (P < 0.05), but thereafter it decreased in most of the samples. ACDS and ALDS had significantly higher TBARS values (P < 0.05), and these values remained higher than those of the other samples throughout the frozen storage period. Addition of surimi-like material to the meatballs had significant effects (P < 0.05) on springiness, gumminess, and chewiness values of all samples. Ingredients and frozen storage affected most sensory attributes in samples significantly (P<0.05). No significant increase in growth of organisms occurred during 12-wk frozen storage The results indicate that acid-alkaline solubilization methods improve both physicochemical and sensory properties of duck meatballs containing duck surimi-like material. Thus, these techniques should be applicable to product development of duck surimi-like material.
    Matched MeSH terms: Muscle Proteins/analysis; Muscle Proteins/isolation & purification; Muscle Proteins/chemistry*
  6. Fulltext Effect of some biopolymers on the rheological behavior of surimi gel
    Sarker ZI, Elgadir MA, Ferdosh S, Akanda JH, Manap MY, Noda T
    Molecules, 2012;17(5):5733-44.
    PMID: 22628045 DOI: 10.3390/molecules17055733
    The objective of this study was to investigate the effect of selected biopolymers on the rheological properties of surimi. In our paper, we highlight the functional properties and rheological aspects of some starch mixtures used in surimi. However, the influence of some other ingredients, such as cryoprotectants, mannans, and hydroxylpropylmethylcellulose (HPMC), on the rheological properties of surimi is also described. The outcome reveals that storage modulus increased with the addition of higher levels of starch. Moreover, the increasing starch level increased the breaking force, deformation, and gel strength of surimi as a result of the absorption of water by starch granules in the mixture to make the surimi more rigid. On the other hand, the addition of cryoprotectants, mannans, and HPMC improved the rheological properties of surimi. The data obtained in this paper could be beneficial particularly to the scientists who deal with food processing field.
    Matched MeSH terms: Muscle Proteins/chemistry*
  7. Quantitation of Protein Cysteine-Phenol Adducts in Minced Beef Containing 4-Methyl Catechol
    Arsad SS, Zainudin MAM, De Gobba C, Jongberg S, Larsen FH, Lametsch R, et al.
    J Agric Food Chem, 2020 Feb 26;68(8):2506-2515.
    PMID: 32013414 DOI: 10.1021/acs.jafc.9b07752
    Thiol groups of cysteine (Cys) residues in proteins react with quinones, oxidation products of polyphenols, to form protein-polyphenol adducts. The aim of the present work was to quantify the amount of adduct formed between Cys residues and 4-methylcatechol (4MC) in minced beef. A Cys-4MC adduct standard was electrochemically synthesized and characterized by liquid chromatography-mass spectrometry (LC-MS) as well as NMR spectroscopy. Cys-4MC adducts were quantified after acidic hydrolysis of myofibrillar protein isolates (MPIs) and LC-MS/MS analysis of meat containing either 500 or 1500 ppm 4MC and stored at 4 °C for 7 days under a nitrogen or oxygen atmosphere. The concentrations of Cys-4MC were found to be 2.2 ± 0.3 nmol/mg MPI and 8.1 ± 0.9 nmol/mg MPI in meat containing 500 and 1500 ppm 4MC, respectively, and stored for 7 days under oxygen. The formation of the Cys-4MC adduct resulted in protein thiol loss, and ca. 62% of the thiol loss was estimated to account for the formation of the Cys-4MC adduct for meat containing 1500 ppm 4MC. Furthermore, protein polymerization increased in samples containing 4MC as evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the polymerization was found to originate from protein-polyphenol interactions as evaluated by a blotting assay with staining by nitroblue tetrazolium.
    Matched MeSH terms: Muscle Proteins/chemistry
  8. Congenital myasthenic syndrome with novel pathogenic variants in the COLQ gene associated with the presence of antibodies to acetylcholine receptors
    Tay CG, Fong CY, Li L, Ganesan V, Teh CM, Gan CS, et al.
    J Clin Neurosci, 2020 Feb;72:468-471.
    PMID: 31831253 DOI: 10.1016/j.jocn.2019.12.007
    Congenital myasthenic syndrome (CMS) is a heterogeneous group of inherited disorder which does not associate with anti-acetylcholine receptor (AChR) antibody. The presence of AChR autoantibody is pathogenic and highly sensitive and specific for autoimmune myasthenia gravis (MG). We describe 2 children from unrelated families who presented with hypotonia, ptosis and fatigability in early infancy with anti-AChR antibodies detected via ELISA on 2 separate occasions in the sera. Both were treated as refractory autoimmune MG due to poor clinical response to acetylcholinesterase inhibitor and immunotherapy. In view of the atypical clinical features, genetic studies of CMS were performed and both were confirmed to have novel pathogenic mutations in the COLQ gene. To the best of our knowledge, the presence of anti-AChR antibody in COLQ-related CMS has never been reported in the literature. The clinical presentation of early onset phenotype, and refractoriness to acetylcholinesterase inhibitor and immunotherapy should prompt CMS as a differential diagnosis.
    Matched MeSH terms: Muscle Proteins/genetics*
  9. Fulltext Muscle protein synthesis and muscle/metabolic responses to resistance exercise training in South Asian and White European men
    Alkhayl FFA, Ismail AD, Celis-Morales C, Wilson J, Radjenovic A, Johnston L, et al.
    Sci Rep, 2022 Feb 15;12(1):2469.
    PMID: 35169204 DOI: 10.1038/s41598-022-06446-7
    The aims of the current study, therefore, were to compare (1) free-living MPS and (2) muscle and metabolic adaptations to resistance exercise in South Asian and white European adults. Eighteen South Asian and 16 White European men were enrolled in the study. Free-living muscle protein synthesis was measured at baseline. Muscle strength, body composition, resting metabolic rate, VO2max and metabolic responses (insulin sensitivity) to a mixed meal were measured at baseline and following 12 weeks of resistance exercise training. Free-living muscle protein synthesis was not different between South Asians (1.48 ± 0.09%/day) and White Europeans (1.59 ± 0.15%/day) (p = 0.522). In response to resistance exercise training there were no differences, between South Asians and White Europeans, muscle mass, lower body strength or insulin sensitivity. However, there were differences between the ethnicities in response to resistance exercise training in body fat, resting carbohydrate and fat metabolism, blood pressure, VO2max and upper body strength with responses less favourable in South Asians. In this exploratory study there were no differences in muscle protein synthesis or anabolic and metabolic responses to resistance exercise, yet there were less favourable responses in several outcomes. These findings require further investigation.
    Matched MeSH terms: Muscle Proteins/metabolism*
  10. Mechanisms of action of 17βH-neriifolin on its anticancer effect in SKOV-3 ovarian cancer cell line
    Mutalip SS, Yunos NM, Abdul-Rahman PS, Jauri MH, Osman A, Adenan MI
    Anticancer Res, 2014 Aug;34(8):4141-51.
    PMID: 25075041
    AIM: Abnormalities in apoptotic signalling pathways often occur in cancer cells and limit the successful chemotherapy outcomes in cancers. Therefore, there is an urgent need to discover new anticancer agents with novel mechanisms of action to overcome the resistance effect in chemotherapy.

    MATERIALS AND METHODS: In the present study, the anticancer effects and the mechanisms of action of 17βH-neriifolin (cardiac glycoside) were evaluated by terminal deoxynucleotidyl transferase dUTP nick-end labeling (TUNEL) assay and a proteomic approach in treated and non-treated SKOV-3 ovarian cancer cells.

    RESULTS: 17βH-neriifolin was found to be active with IC50 values of 0.01 ± 0.001 in SKOV-3 ovarian cancer cell line, as evaluated by the sulforhodamine B (SRB) assay. RESULTS from TUNEL assay indicated that 17βH-neriifolin caused apoptosis in SKOV-3 cells in a dose-dependent manner. Based on differential analysis of treated and non-treated SKOV-3 two-dimensional electrophoresis (2-DE) profiles, four proteins, namely vimentin (VIM), pyruvate kinase, muscle (PKM), heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) and transgelin (TAGLN1) were identified to be involved in apoptosis. Other proteins including piggybac transposable element derived 5 (PGBD5), DENN/MADD domain containing 2D (DENND2D) and formin-like 1(FMNL) have also been identified to be associated in SKOV-3 cell death induced by 17βH-neriifolin.

    CONCLUSION: These findings may provide new insights on the potential of 17βH-neriifolin's mechanism of action in killing ovarian cancer cells.

    Matched MeSH terms: Muscle Proteins/physiology
  11. Perilipin 5 is dispensable for normal substrate metabolism and in the adaptation of skeletal muscle to exercise training
    Mohktar RA, Montgomery MK, Murphy RM, Watt MJ
    Am J Physiol Endocrinol Metab, 2016 07 01;311(1):E128-37.
    PMID: 27189934 DOI: 10.1152/ajpendo.00084.2016
    Cytoplasmic lipid droplets provide a reservoir for triglyceride storage and are a central hub for fatty acid trafficking in cells. The protein perilipin 5 (PLIN5) is highly expressed in oxidative tissues such as skeletal muscle and regulates lipid metabolism by coordinating the trafficking and the reversible interactions of effector proteins at the lipid droplet. PLIN5 may also regulate mitochondrial function, although this remains unsubstantiated. Hence, the aims of this study were to examine the role of PLIN5 in the regulation of skeletal muscle substrate metabolism during acute exercise and to determine whether PLIN5 is required for the metabolic adaptations and enhancement in exercise tolerance following endurance exercise training. Using muscle-specific Plin5 knockout mice (Plin5(MKO)), we show that PLIN5 is dispensable for normal substrate metabolism during exercise, as reflected by levels of blood metabolites and rates of glycogen and triglyceride depletion that were indistinguishable from control (lox/lox) mice. Plin5(MKO) mice exhibited a functional impairment in their response to endurance exercise training, as reflected by reduced maximal running capacity (20%) and reduced time to fatigue during prolonged submaximal exercise (15%). The reduction in exercise performance was not accompanied by alterations in carbohydrate and fatty acid metabolism during submaximal exercise. Similarly, mitochondrial capacity (mtDNA, respiratory complex proteins, citrate synthase activity) and mitochondrial function (oxygen consumption rate in muscle fiber bundles) were not different between lox/lox and Plin5(MKO) mice. Thus, PLIN5 is dispensable for normal substrate metabolism during exercise and is not required to promote mitochondrial biogenesis or enhance the cellular adaptations to endurance exercise training.
    Matched MeSH terms: Muscle Proteins/genetics*
  12. Perilipin 5 Deletion Unmasks an Endoplasmic Reticulum Stress-Fibroblast Growth Factor 21 Axis in Skeletal Muscle
    Montgomery MK, Mokhtar R, Bayliss J, Parkington HC, Suturin VM, Bruce CR, et al.
    Diabetes, 2018 04;67(4):594-606.
    PMID: 29378767 DOI: 10.2337/db17-0923
    Lipid droplets (LDs) are critical for the regulation of lipid metabolism, and dysregulated lipid metabolism contributes to the pathogenesis of several diseases, including type 2 diabetes. We generated mice with muscle-specific deletion of the LD-associated protein perilipin 5 (PLIN5, Plin5MKO ) and investigated PLIN5's role in regulating skeletal muscle lipid metabolism, intracellular signaling, and whole-body metabolic homeostasis. High-fat feeding induced changes in muscle lipid metabolism of Plin5MKO mice, which included increased fatty acid oxidation and oxidative stress but, surprisingly, a reduction in inflammation and endoplasmic reticulum (ER) stress. These muscle-specific effects were accompanied by whole-body glucose intolerance, adipose tissue insulin resistance, and reduced circulating insulin and C-peptide levels in Plin5MKO mice. This coincided with reduced secretion of fibroblast growth factor 21 (FGF21) from skeletal muscle and liver, resulting in reduced circulating FGF21. Intriguingly, muscle-secreted factors from Plin5MKO , but not wild-type mice, reduced hepatocyte FGF21 secretion. Exogenous correction of FGF21 levels restored glycemic control and insulin secretion in Plin5MKO mice. These results show that changes in lipid metabolism resulting from PLIN5 deletion reduce ER stress in muscle, decrease FGF21 production by muscle and liver, and impair glycemic control. Further, these studies highlight the importance for muscle-liver cross talk in metabolic regulation.
    Matched MeSH terms: Muscle Proteins/genetics*
  13. Fulltext Challenges and importance of traceability of halal raw materials in processed meat products: a review
    Babji, A.S., Ghassem, M., Hong, P.K., Maizatul, S.M.S.
    ASM Science Journal, 2012;6(2):144-147.
    MyJurnal
    Research and development trends will continue to design innovative composite foods in which muscle proteins are combined with non-conventional animal products, non-meat proteins and functional food additives, many of which have lost their original inherent properties and characteristics. Composite food are products with meat, non-meat proteins, fats, carbohydrates and functional ingredients such as pre-emulsion, probiotics, enzymes, bioactives, peptides, hormones, emulsifiers, gelatin, animal fats/oils, alcohol and visceral tissues. Traceability of halal meat raw materials should start at the point of animal breeding, production to the stage of halal slaughter, processing operations and final point of consumption. Traceability of food additives used in the food industry remains a major hurdle for the Muslim community seeking halal food. The processes and technological advancements made in raw material processing, ingredient extractions, modifications, purification and resynthesized into many food ingredients make the question of traceability and solving of the materials and processes that are halal a monumental task. Food is only halal if the entire food chain from farm to table, is processed, handled and stored in accordance with the syariah and/or halal standards or guidelines, such as in the Jabatan Kemajuan Islam Malaysia (JAKIM): General guidelines, Malaysia Standards MS 1500:2009 and Codex Alimentarius (Food Labeling). Here lies the challenge and importance of traceability to verify the ‘wholesomeness’ of the sources of halal raw materials and final meat-based food products.
    Matched MeSH terms: Muscle Proteins
  14. Studies of the chemical composition of a healing skin wound in rats, and of the concentrations of some constituents of tissues distant from the healing wound
    Candlish J, Chandra N
    Biochem. J., 1967 Mar;102(3):767-73.
    PMID: 16742493
    1. A skin lesion was made in rats by dorsal incision and the insertion of a polythene tube. 2. Over a period of 25 days after wounding, assays were performed for ascorbic acid, DNA, hydroxyproline, methionine, tryptophan, tyrosine and free amino acids in the lesion tissue. 3. The neutral-salt-soluble proteins of the lesion tissue were fractionated on DEAE-Sephadex, with the separation of fibrinogen and gamma-globulin from a serum protein fraction. 4. Over a period of 20 days after wounding, in wounded rats and in controls, assays were conducted for: ascorbic acid in lens and liver, hydroxyproline, soluble protein, methionine and water in muscle and tendon, and free amino acids in muscle. 5. Relative to controls there was a decrease in lens and liver ascorbic acid, a rise in tendon hydroxyproline, a rise in muscle free amino acids, a fall in muscle protein and a rise in tendon and muscle water.
    Matched MeSH terms: Muscle Proteins
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