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

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.

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

2020 ◽  
Vol 98 (Supplement_4) ◽  
pp. 198-199
Author(s):  
Reganne K Briggs ◽  
Jerrad F Legako ◽  
Paul R Broadway ◽  
Jeff A Carroll ◽  
Nicole C Burdick-Sanchez ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Expression ◽  
Serum Cortisol ◽  
Stressful Event ◽  
Beef Tenderness ◽  
Acth Challenge ◽  
Fragmentation Index ◽  
Longissimus Lumborum ◽  
Shock Proteins ◽  
Time Of 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.

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

2007 ◽  
Vol 41 (7) ◽  
pp. 453-455 ◽  
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

scholarly journals Exercise, heat shock proteins and insulin resistance

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160529 ◽  
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’.

scholarly journals Se Alleviated Oxidative Stress-Mediated Complex Poisoning Mechanism in Pb-Treated Chicken Kidneys: Inflammation, Heat Shock Response, and Autophagy

2021 ◽  
Author(s):  
Zhiying Miao ◽  
Weikang Yu ◽  
Yueyang Wang ◽  
Xianhong Gu ◽  
Xiaohua Teng
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Protein Expression ◽  
Heat Shock Response ◽  
Potable Water ◽  
Histological Structure ◽  
Standard Diet ◽  
Shock Response ◽  
Mrna And Protein Expression ◽  
Shock Proteins

Abstract Background: Lead (Pb) is a toxic environmental pollutant and can exerts toxicity in kidneys. It is known that selenium (Se) has an antagonistic effect on Pb poisoning. However, biological events during the process were not well understood in chicken kidneys.Methods: One hundred and eighty male Hyline chickens (7-day-old) were randomly divided into the control group (offering standard diet and potable water), the Se group (offering Na2SeO3-added standard diet and potable water), the Pb group (offering standard diet and (CH3OO)2Pb-added potable water), and the Pb+Se group (offering Na2SeO3-added standard diet and (CH3OO)2Pb-added potable water). On 30th, 60th, and 90th days, kidneys were removed to perform the studies of histological structure, oxidative stress indicators, cytokines, heat shock proteins, and autophagy in the chicken kidneys.Results: The experimental results indicated that Pb poisoning changed renal histological structure; decreased catalase, glutathione-s-transferase, and total antioxidative capacity activities; increased hydrogen peroxide content; induced mRNA and protein expression of heat shock proteins; inhibited interleukin (IL)-2 mRNA expression, and induced IL-4 and IL-12β mRNA expression; inhibited mammalian target of rapamycin mRNA and protein expression, and induced autophagy-related gene mRNA and protein expression in the chicken kidneys. Supplement of Se mitigated the above changes caused by Pb.Conclusion: Our research strengthens the evidence that Pb induced oxidative stress, inflammation, heat shock response, and autophagy and Se administration alleviated Pb poisoning through mitigating oxidative stress in the chicken kidneys.

scholarly journals Preservation of skeletal muscle by the heat shock proteins following frostbite injury

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Ruben Mestril ◽  
Colin Schweigert ◽  
Jason Batey ◽  
Tomas Liskutin ◽  
John Baldwin
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

Diathermy treatment increases heat shock protein expression in female, but not male skeletal muscle

2007 ◽  
Vol 102 (3) ◽  
pp. 319-323 ◽  
Author(s):  
Chad Touchberry ◽  
Tung Le ◽  
Scott Richmond ◽  
Mike Prewitt ◽  
David Beck ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Heat Shock Protein Expression

scholarly journals Role of Heat Shock Proteins in Skeletal Muscle

10.5772/47815 ◽  
2012 ◽  
Author(s):  
Thiago Gomes ◽  
Sofia Pizzato ◽  
Mirna Stela ◽  
Paulo Ivo Homem de Bittencourt Jr.
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

Heat shock proteins and exercise: a primer

2008 ◽  
Vol 33 (5) ◽  
pp. 1050-1075 ◽  
Author(s):  
Earl G. Noble ◽  
Kevin J. Milne ◽  
C.W. James Melling
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ion Channel ◽  
The Other ◽  
Cellular Environment ◽  
Shock Proteins ◽  
Fertile Area ◽  
Area Of Study

Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this review is to introduce the reader to the major HSP families, the control of their expression, and some of their biologic functions, specifically with respect to the influence of exercise. Moreover, as the first in a series of reviews from a common symposium, we will briefly introduce the concepts presented by the other authors, which include the effects of different exercise paradigms on skeletal muscle HSPs in the adult and aged systems, HSPs as regulators of inflammation, and the ion channel stabilizing effects of HSPs.

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