425 Effects of pre-mortem stress on protein expression, steak color, and myofibrillar fragmentation index in the longissimus lumborum following harvest

Abstract Undesirable variation in beef tenderness and stability of flavor and color may be associated with the abundance of heat shock proteins (HSP). This study aimed to determine whether pre-mortem stress impacts HSP expression in the skeletal muscle following harvest. Forty Holstein steers were administered an i.v. bolus dose of adrenocorticotropic hormone (ACTH; 0.1 IU/Kg BW) to mimic an acute pre-mortem stress. Longissimus lumborum (LD) biopsy samples were taken prior to the ACTH challenge. Serum cortisol was measured every 0.5 h from -2 to 6 h relative to the ACTH challenge. Skeletal muscle and blood samples from 10 steers were collected at each harvest timepoint at (2, 12, 24 and 48 h post-challenge). Samples were collected from the LD immediately after harvest and after 14 d of aging. Protein expression of HSPβ1, P-HSPβ1, HSPβ5, and DJ-1 was analyzed in muscle samples taken prior to the ACTH challenge, at harvest, and after 14 d of post-mortem wet aging. In addition, steak color and myofibrillar fragmentation index (MFI) was analyzed in 14 d aged samples. Harvest time point following the ACTH challenge affected (P < 0.05) protein expression of HSPβ1 and P-HSPβ1. Protein expression of DJ-1 prior to the ACTH challenge was different (P < 0.05) among steers harvested at different timepoints. In addition, time of harvest had no effect on HSPβ5 expression (P > 0.05). Regarding steak color, time of harvest had an effect (P < 0.01) on a*, b*, hue, chroma, and ratio, but no effect (P > 0.05) on L*. Lastly, time of harvest had an effect (P < 0.05) on MFI. These data indicate that HSP expression, steak color, and MFI in the LD after harvest may be related to time of harvest following a stressful event pre-mortem.

Download Full-text

279 Effects of pre-mortem stress on heat shock protein expression in the longissimus lumborum following harvest

Journal of Animal Science ◽

10.1093/jas/skz258.220 ◽

2019 ◽

Vol 97 (Supplement_3) ◽

pp. 107-107

Author(s):

Reganne K Briggs ◽

Jerrad F Legako ◽

Paul R Broadway ◽

Jeffery A Carroll ◽

Nicole C Sanchez ◽

...

Keyword(s):

Skeletal Muscle ◽

Heat Shock ◽

Protein Expression ◽

White Blood Cells ◽

Meat Products ◽

Serum Cortisol ◽

Acth Challenge ◽

Longissimus Lumborum ◽

Complete Blood Counts ◽

Shock Proteins

Abstract Despite similar production practices, meat products from beef cattle exhibit undesirable variation in tenderness and stability of flavor and color. The objective of this study was to determine whether pre-mortem stress impacts expression of heat shock proteins (HSP) in the skeletal muscle following harvest. In this study, 40 Holstein steers underwent a 6 h adrenocorticotropic hormone (ACTH) challenge designed to emulate pre-mortem stress prior to harvest. Skeletal muscle biopsies from the longissimus lumborum were taken prior to the ACTH challenge. During the challenge, complete blood counts (CBC) were collected every 2 h and serum cortisol every 0.5 h from -2 to 6 h of the ACTH challenge. Following the 6 h ACTH challenge, skeletal muscle and blood samples were collected from 10 animals each harvested at 2, 12, 24 and 48 h post-challenge. Immediately following harvest, samples were collected from the longissimus lumborum and again after 14 d of aging. Protein expression of HSPβ1 was analyzed in skeletal muscle samples taken prior to the ACTH challenge, at harvest, and after 14 d of aging. Expression of HSPβ1 was different (P < 0.05) at harvest between animals that were harvested at different points following induction of stress where steers that were harvested at 12 h had decreased expression when compared to those harvested at 48 h. In addition, time of harvest had an effect (P < 0.01) on cortisol concentrations, hemoglobin, hematocrit, white blood cells, neutrophils, monocytes, and eosinophils. Number of platelets, lymphocytes, and basophils did not differ (P > 0.05) between animals harvested at different time points. These data demonstrate that HSPβ1 protein expression in the longissimus lumborumafter harvest may be related to pre-mortem stress.

Download Full-text

Differences in skeletal muscle proteolysis in Nellore and Angus cattle might be driven by Calpastatin activity and not the abundance of Calpain/Calpastatin

The Journal of Agricultural Science ◽

10.1017/s0021859617000715 ◽

2017 ◽

Vol 155 (10) ◽

pp. 1669-1676 ◽

Cited By ~ 2

Author(s):

T. S. MARTINS ◽

L. M. P. SANGLARD ◽

W. SILVA ◽

M. L. CHIZZOTTI ◽

M. M. LADEIRA ◽

...

Keyword(s):

Skeletal Muscle ◽

Protein Expression ◽

Protein Abundance ◽

Longissimus Muscle ◽

Proteolytic System ◽

Angus Cattle ◽

Fragmentation Index ◽

Gene And Protein Expression ◽

Nellore Cattle ◽

Mrna And Protein Expression

SUMMARYThe present study aimed to explore the molecular factors underlying differences in Calpain/Calpastatin proteolytic system in Nellore and Angus cattle. Longissimus muscle samples were collected in Nellore (n = 6; body weight (BW) = 373 ± 37·3 kg) and Angus (n = 6; BW = 383 ± 23·9 kg) cattle at slaughter for analysis of gene and protein expression, and Calpastatin enzyme activity. Additionally, the myofibrillar fragmentation index was used to quantify the extension of proteolysis in longissimus muscle samples. A greater myofibrillar fragmentation was observed in skeletal muscle of Angus compared with Nellore cattle. Conversely, no differences were found between breeds for mRNA expression of Calpain 1 (CAPN1) and Calpastatin (CAST). Similarly, no differences were observed for the abundance of Calpain and Calpastatin proteins between skeletal muscles of Nellore and Angus cattle. Despite the lack of differences in mRNA and protein abundance, a greater activity of Calpastatin was observed in skeletal muscle of Nellore compared with Angus cattle. These data indicate that the greater proteolysis in skeletal muscle of Angus compared with Nellore cattle is mainly driven by a greater Calpastatin activity rather than Calpain or Calpastatin mRNA and protein expression.

Download Full-text

Curcumin induces mitochondrial biogenesis by increasing cAMP levels via PDE4A inhibition in skeletal muscle

British Journal Of Nutrition ◽

10.1017/s0007114521000490 ◽

2021 ◽

pp. 1-34

Author(s):

Hamidie Ronald D Ray ◽

Tsubasa Shibaguchi ◽

Tatsuya Yamada ◽

Rikuhide Koma ◽

Rie Ishizawa ◽

...

Keyword(s):

Skeletal Muscle ◽

Protein Expression ◽

Mitochondrial Biogenesis ◽

Mitochondrial Respiration ◽

Citrate Synthase ◽

Signalling Pathway ◽

Curcumin Treatment ◽

Camp Content ◽

Signalling Molecules ◽

Camp Levels

Abstract Background: Previous research has suggested that curcumin potentially induces mitochondrial biogenesis in skeletal muscle via increasing cAMP levels. However, the regulatory mechanisms for this phenomenon remain unknown. The purpose of the present study was to clarify the mechanism by which curcumin activates cAMP-related signalling pathways that upregulate mitochondrial biogenesis and respiration in skeletal muscle. Methods: The effect of curcumin treatment (i.p., 100 mg/kg-BW/day for 28 days) on mitochondrial biogenesis was determined in rats. The effects of curcumin and exercise (swimming for 2 h/day for 3 days) on the cAMP signalling pathway were determined in the absence and presence of phosphodiesterase (PDE) or protein kinase A (PKA) inhibitors. Mitochondrial respiration, citrate synthase (CS) activity, cAMP content, and protein expression of cAMP/PKA signalling molecules were analysed. Results: Curcumin administration increased COX-IV protein expression, and CS and complex I activity, consistent with the induction of mitochondrial biogenesis by curcumin. Mitochondrial respiration was not altered by curcumin treatment. Curcumin and PDE inhibition tended to increase cAMP levels with or without exercise. In addition, exercise increased the phosphorylation of PDE4A, whereas curcumin treatment strongly inhibited PDE4A phosphorylation regardless of exercise. Furthermore, curcumin promoted AMPK phosphorylation and PGC-1α deacetylation. Inhibition of PKA abolished the phosphorylation of AMPK. Conclusion: The present results suggest that curcumin increases cAMP levels via inhibition of PDE4A phosphorylation, which induces mitochondrial biogenesis through a cAMP/PKA/AMPK signalling pathway. Our data also suggest the possibility that curcumin utilizes a regulatory mechanism for mitochondrial biogenesis that is distinct from the exercise-induced mechanism in skeletal muscle.

Download Full-text

Low-Dose Acrolein, an Endogenous and Exogenous Toxic Molecule, Inhibits Glucose Transport via an Inhibition of Akt-Regulated GLUT4 Signaling in Skeletal Muscle Cells

International Journal of Molecular Sciences ◽

10.3390/ijms22137228 ◽

2021 ◽

Vol 22 (13) ◽

pp. 7228

Author(s):

Ching-Chia Wang ◽

Huang-Jen Chen ◽

Ding-Cheng Chan ◽

Chen-Yuan Chiu ◽

Shing-Hwa Liu ◽

...

Keyword(s):

Skeletal Muscle ◽

Glucose Metabolism ◽

Glucose Tolerance ◽

Protein Expression ◽

Glucose Uptake ◽

Glucose Transport ◽

Diabetic Patients ◽

Type 2 Diabetic Patients ◽

Type 2 Diabetic

Urinary acrolein adduct levels have been reported to be increased in both habitual smokers and type-2 diabetic patients. The impairment of glucose transport in skeletal muscles is a major factor responsible for glucose uptake reduction in type-2 diabetic patients. The effect of acrolein on glucose metabolism in skeletal muscle remains unclear. Here, we investigated whether acrolein affects muscular glucose metabolism in vitro and glucose tolerance in vivo. Exposure of mice to acrolein (2.5 and 5 mg/kg/day) for 4 weeks substantially increased fasting blood glucose and impaired glucose tolerance. The glucose transporter-4 (GLUT4) protein expression was significantly decreased in soleus muscles of acrolein-treated mice. The glucose uptake was significantly decreased in differentiated C2C12 myotubes treated with a non-cytotoxic dose of acrolein (1 μM) for 24 and 72 h. Acrolein (0.5–2 μM) also significantly decreased the GLUT4 expression in myotubes. Acrolein suppressed the phosphorylation of glucose metabolic signals IRS1, Akt, mTOR, p70S6K, and GSK3α/β. Over-expression of constitutive activation of Akt reversed the inhibitory effects of acrolein on GLUT4 protein expression and glucose uptake in myotubes. These results suggest that acrolein at doses relevant to human exposure dysregulates glucose metabolism in skeletal muscle cells and impairs glucose tolerance in mice.

Download Full-text

Microwave hyperthermia treatment increases heat shock proteins in human skeletal muscle * COMMENTARY

British Journal of Sports Medicine ◽

10.1136/bjsm.2006.032938 ◽

2007 ◽

Vol 41 (7) ◽

pp. 453-455 ◽

Cited By ~ 15

Author(s):

Y. Ogura ◽

H. Naito ◽

T. Tsurukawa ◽

N. Ichinoseki-Sekine ◽

N. Saga ◽

...

Keyword(s):

Skeletal Muscle ◽

Heat Shock ◽

Heat Shock Proteins ◽

Human Skeletal Muscle ◽

Hyperthermia Treatment ◽

Shock Proteins ◽

Microwave Hyperthermia

Download Full-text

Exercise, heat shock proteins and insulin resistance

Philosophical Transactions of the Royal Society B Biological Sciences ◽

10.1098/rstb.2016.0529 ◽

2017 ◽

Vol 373 (1738) ◽

pp. 20160529 ◽

Cited By ~ 19

Author(s):

Ashley E. Archer ◽

Alex T. Von Schulze ◽

Paige C. Geiger

Keyword(s):

Insulin Resistance ◽

Skeletal Muscle ◽

Heat Shock ◽

Heat Shock Proteins ◽

Metabolic Effects ◽

Diabetic Patients ◽

Alcoholic Fatty Liver ◽

Insulin Resistant ◽

Exercise Induced ◽

Shock Proteins

Best known as chaperones, heat shock proteins (HSPs) also have roles in cell signalling and regulation of metabolism. Rodent studies demonstrate that heat treatment, transgenic overexpression and pharmacological induction of HSP72 prevent high-fat diet-induced glucose intolerance and skeletal muscle insulin resistance. Overexpression of skeletal muscle HSP72 in mice has been shown to increase endurance running capacity nearly twofold and increase mitochondrial content by 50%. A positive correlation between HSP72 mRNA expression and mitochondrial enzyme activity has been observed in human skeletal muscle, and HSP72 expression is markedly decreased in skeletal muscle of insulin resistant and type 2 diabetic patients. In addition, decreased levels of HSP72 correlate with insulin resistance and non-alcoholic fatty liver disease progression in livers from obese patients. These data suggest the targeted induction of HSPs could be a therapeutic approach for preventing metabolic disease by maintaining the body's natural stress response. Exercise elicits a number of metabolic adaptations and is a powerful tool in the prevention and treatment of insulin resistance. Exercise training is also a stimulus for increased HSP expression. Although the underlying mechanism(s) for exercise-induced HSP expression are currently unknown, the HSP response may be critical for the beneficial metabolic effects of exercise. Exercise-induced extracellular HSP release may also contribute to metabolic homeostasis by actively restoring HSP72 content in insulin resistant tissues containing low endogenous levels of HSPs. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

Download Full-text