Assessment of the textural variation of iced stored Anabas testudineus (Bloch, 1792) muscle tissue with emphasis on their collagen and myofibrillar protein content

Unweighting of rat hindlimb muscles results in skeletal muscle atrophy, decreased protein synthesis, and reduced growth hormone (GH) secretion. Resistance exercise (ladder climbing) and GH treatment partially attenuate skeletal muscle atrophy in hypophysectomized hindlimb-suspended rats. It was hypothesized that a combination of multiple bouts of daily resistance exercise and GH (1 mg.kg-1.day-1) would prevent skeletal muscle atrophy in growing nonhypophysectomized hindlimb-suspended rats. Hindlimb suspension decreased the absolute (mg/pair) and relative (mg/100 g body wt) weights of the soleus, a slow-twitch plantar flexor, by 30 and 21%, respectively, and the absolute and relative weights of the gastrocnemius, a predominantly fast-twitch plantar flexor, by 20 and 11%, respectively (P < 0.05). Exercise did not increase soleus mass but attenuated loss of relative wet weight in the gastrocnemius muscles of hindlimb-suspended rats (P < 0.05). Hindlimb suspension decreased gastrocnemius myofibrillar protein content and synthesis (mg/day) by 26 and 64%, respectively (P < 0.05). The combination of exercise and GH attenuated loss of gastrocnemius myofibrillar protein content and synthesis by 70 and 23%, respectively (P < 0.05). Results of the present investigation indicate that a combination of GH and resistance exercise attenuates atrophy of unweighted fast-twitch skeletal muscles.

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Myofibrillar Protein Abundance and Anabolic Signaling in Myotubes Depleted of E1 Alpha Subunit of Branched-Chain Ketoacid Dehydrogenase Complex

Current Developments in Nutrition ◽

10.1093/cdn/nzaa049_035 ◽

2020 ◽

Vol 4 (Supplement_2) ◽

pp. 642-642

Author(s):

Glory Madu ◽

Olasunkanmi Adegoke

Keyword(s):

Skeletal Muscle ◽

Amino Acids ◽

Protein Content ◽

Muscle Protein ◽

Essential Amino Acids ◽

Myofibrillar Protein ◽

L6 Myotubes ◽

Branched Chain ◽

Ketoacid Dehydrogenase

Abstract Objectives Branched-chain amino acids (BCAAs) are essential amino acids that are crucial for skeletal muscle anabolism. Thus, alterations in their levels are associated with muscle atrophic diseases such as cancer, chronic inflammatory and neurological disorders. Others have linked impairments in BCAA metabolism to the development of insulin resistance and its sequelae. Compared to the effects of theses amino acids, much less is known on how impairment in BCAA catabolism affects skeletal muscle. BCAA catabolism starts with the reversible transamination by the mitochondrial enzyme branched-chain aminotransferase 2 (BCAT2). This is followed by the irreversible carboxylation, catalyzed by branched-chain ketoacid dehydrogenase (BCKD) complex. We have shown that BCAT2 and BCKD are essential for the differentiation of skeletal myoblasts into myotubes. Here, we investigated the effect of depletion of BCAT2 or of E1a subunit of BCKD in differentiated myotubes. Methods On day 4 of differentiation, L6 myotubes were transfected with the following siRNA oligonucleotides: scrambled (control), BCAT2, or E1a subunit of BCKD. Results Forty-eight hours after transfection, compared to control or BCAT2 siRNA group, we observed improved myotube structure in BCKD-depleted cells. BCKD depletion augmented myofibrillar protein levels: myosin heavy chain (MHC, 2-fold) and tropomyosin (4-fold), P < 0.05, n = 3. To further analyze the increase in myofibrillar protein content, we examined signaling through mTORC1 (mechanistic target of rapamycin complex 1), a vital complex necessary for skeletal muscle anabolism. BCKD depletion increased the phosphorylation of mTORC1 upstream activator AKT (52%, P < 0.05, n = 3), and of mTORC1 downstream substrates by 25%-86%, consistent with the increase in myofibrillar proteins. Finally, in myotubes treated with the catabolic cytokine (tumor necrosis factor-a), BCKD depletion tended to increase the abundance of tropomyosin (a myofibrillar protein). Conclusions We showed that depletion of BCKD enhanced myofibrillar protein content and anabolic signaling. If these data are confirmed in vivo, development of dietary and other interventions that target BCKD abundance or functions may promote muscle protein anabolism in individuals with muscle wasting conditions. Funding Sources MHRC, NSERC York U.

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Quantitative importance of non-skeletal-muscle Nτ-methylhistidine and creatine in human urine

Biochemical Journal ◽

10.1042/bj2000449 ◽

1981 ◽

Vol 200 (2) ◽

pp. 449-452 ◽

Cited By ~ 31

Author(s):

E G Afting ◽

W Bernhardt ◽

R W C Janzen ◽

H J Röthig

Keyword(s):

Skeletal Muscle ◽

Muscle Tissue ◽

Skeletal Muscle Mass ◽

Myofibrillar Protein ◽

Skeletal Muscle Tissue ◽

Major Contributor ◽

Protein Breakdown ◽

Creatinine Excretion ◽

First Time ◽

Quantitative Importance

The excretion of N tau-methylhistidine and creatinine was determined in a totally paralysed patient wih neither macroscopic nor microscopic detectable skeletal-muscle tissue. In this subject, it was possible for the first time to measure the basal non-skeletal-muscle-dependent excretion of N tau-methylhistidine and creatinine per 24 h and per kg of non-muscular body weight, 1.15 mumol (N tau-methylhistidine) and 35 mumol (creatinine) respectively. For the calculation of myofibrillar protein breakdown and skeletal-muscle mass on the basis of N tau-methylhistidine and creatinine excretion, the values have to be corrected for non-muscular sources. Our data show that skeletal-muscle tissue is the major contributor of N tau-methylhistidine in urine, since it contributes as much as 75% to the urinary excretion.

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Effect of heart failure on skeletal muscle myofibrillar protein content, isoform expression and calcium sensitivity

International Journal of Cardiology ◽

10.1016/j.ijcard.2005.03.024 ◽

2006 ◽

Vol 107 (2) ◽

pp. 211-219 ◽

Cited By ~ 10

Author(s):

Michael J. Toth ◽

Bradley M. Palmer ◽

Martin M. LeWinter

Keyword(s):

Heart Failure ◽

Skeletal Muscle ◽

Protein Content ◽

Calcium Sensitivity ◽

Myofibrillar Protein ◽

Isoform Expression

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High insulin levels do not influence PC-1 gene expression and protein content in human muscle tissue and hepatoma cells

Diabetes/Metabolism Research and Reviews ◽

10.1002/(sici)1520-7560(200001/02)16:1<26::aid-dmrr78>3.0.co;2-n ◽

2000 ◽

Vol 16 (1) ◽

pp. 26-32 ◽

Cited By ~ 14

Author(s):

Lucia Frittitta ◽

Paolo Sbraccia ◽

Benedetta V. Costanzo ◽

Vittorio Tassi ◽

Monica D'Adamo ◽

...

Keyword(s):

Gene Expression ◽

Protein Content ◽

Muscle Tissue ◽

Hepatoma Cells ◽

Human Muscle ◽

Insulin Levels ◽

High Insulin

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Post-operative effects on insulin resistance and specific tension of single human skeletal muscle fibres

Clinical Science ◽

10.1042/cs0970449 ◽

1999 ◽

Vol 97 (4) ◽

pp. 449-455 ◽

Cited By ~ 16

Author(s):

Hans DEGENS ◽

Mattias SOOP ◽

Peter HÖÖK ◽

Olle LJUNGQVIST ◽

Lars LARSSON

Keyword(s):

Insulin Resistance ◽

Protein Content ◽

Muscle Weakness ◽

Maximum Velocity ◽

Myofibrillar Protein ◽

Muscle Fibres ◽

Single Muscle ◽

Specific Tension ◽

Generating Capacity ◽

Single Fibres

Surgery and accidental trauma are associated with a transient period of insulin resistance, substrate catabolism and muscle weakness. In the present study, we evaluated the changes in the force-generating capacity of chemically skinned single muscle fibres following abdominal surgery. Biopsies of the m. vastus lateralis were obtained in three patients 1 day before and 3 or 6 days after surgery. Part of the biopsy was frozen for histochemical analysis of the fibre cross-sectional area (FCSA) and myofibrillar protein content, and another part was used for single-fibre contractile measurements. All patients developed insulin resistance following surgery. The maximum velocity of unloaded shortening of single muscle fibres did not change following surgery. The FCSA did not decrease after surgery, as determined either from histochemical sections or from single fibres measured at a fixed sarcomere length of 2.76±0.09 μm (mean±S.D.). Further, the force-generating capacity of the single fibres, measured as maximal Ca2+-activated force (P0) or as P0 normalized to FCSA (specific tension), remained unchanged, as did the myofibrillar protein content of the muscle. In conclusion, the muscle weakness associated with post-operative insulin resistance is not related to a decreased specific tension or a loss of myofibrillar proteins. Other potential cellular mechanisms underlying post-operative weakness are discussed.

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Effect of dietary protein level and salinity on growth, survival, enzymatic activities and amino-acid composition of the white shrimp Litopenaeus vannamei (Boone, 1931) juveniles

Crustaceana ◽

10.1163/15685403-00003390 ◽

2015 ◽

Vol 88 (1) ◽

pp. 82-95 ◽

Cited By ~ 8

Author(s):

Liying Sui ◽

Guannan Ma ◽

Yuangao Deng

Keyword(s):

Amino Acid ◽

Protein Content ◽

Muscle Tissue ◽

Litopenaeus Vannamei ◽

Dietary Protein ◽

Protein Level ◽

White Shrimp ◽

Lower Growth ◽

Protein Levels ◽

Dietary Protein Level

Litopenaeus vannamei (Boone, 1931) postlarvae with average initial body weight of 0.089 g were reared in 75-litre PVC tanks for 40 days at salinities of 30 and 60 g l−1. The shrimps were fed compound feed containing protein levels of 35, 40, 45 and 50%, respectively. Salinity had a remarkable effect on growth and survival of L. vannamei juveniles. Higher survival rate and lower growth were observed at 60 g l−1 salinity. Dietary protein level affected the survival and growth of juveniles at both salinities, increased with dietary protein levels in the range of 35 to 45%, but decreased slightly with 50% dietary protein. Broken line analysis showed that the estimated optimal dietary protein levels at salinities of 30 and 60 g l−1 were 45.93 and 46.74%, respectively. Higher salinity resulted in an increased moisture content, ash and crude protein content in the shrimp muscle tissue. The amino acid contents in the shrimp muscle tissue were generally higher at 60 g l−1 salinity and increased dietary protein level led to higher protein content, except with 50% dietary protein. At salinity 60 g l−1, the soluble protein content and activities of glutamic oxalacetic transferase (GOT) and glutamic pyruvic transaminase (GPT) in shrimp muscle tissue were higher, while catalase (CAT) activities were lower. Farming of L. vannamei at a marginal culture salinity (60 g l−1) is feasible though the shrimps were likely exposed to stressful conditions. Reduced growth rate at higher salinity may be attributed to the higher total ammonium (TAN) concentration in the culture medium and extra energy consumption for osmoregulation at hypersaline conditions.

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Comparison of Proximate Composition of Raw and Cooked Intramuscle Tissue ofThunnus tonggol from Terengganu, Malaysia

Pertanika Journal of Science and Technology ◽

10.47836/pjst.29.1.33 ◽

2021 ◽

Vol 29 (1) ◽

Author(s):

Norhazirah Abd Aziz ◽

Ahmad Shamsudin Ahmad ◽

Adiana Ghazali ◽

Nurul Izzah Ahmad ◽

Ahmad Ali ◽

...

Keyword(s):

Protein Content ◽

Muscle Tissue ◽

Lipid Content ◽

Proximate Composition ◽

White Muscle ◽

The Other ◽

Dark Muscle ◽

Other Hand ◽

Cooking Process ◽

The Mean

A study was carried out to determine the effects of the steaming process on the proximate composition of the dark and white muscle tissue of Thunnus tonggol sampled from Terengganu waters. The mean percentage of moisture, ash, lipid, and protein of the raw dark muscle was 59.1%, 3.8%, 12.1% and 33.9%, while in the raw white muscle were 66.7%, 2.9%, 2.7% and 33.9%, respectively. Both types of muscle showed a significantly different value in the lipid content. There was significant increase recorded in the protein content in both types of muscle after the steaming process (79.1% and 93.0% in dark and white muscles, respectively). Likewise, the percentage of ash showed some increment with 4.8% in the dark muscle and 7.9% in the white muscle. However, the cooking process decreased the percentage of moisture and lipid in both dark and white muscles. The percentage of moisture in dark muscle was reduced to 7.7%, and 9.7% in white muscle. On the other hand, percentage of lipid content in both types of muscles after the steaming process was 0.43% in dark muscle and 0.03% in white muscle. This study reveals that the cooking process had considerable effects on the proximate composition of both dark and white muscles.

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Canned Products Based on Animal Hearts as Collagen and Ferrum Sources

Food Industry ◽

10.29141/2500-1922-2020-5-3-5 ◽

2020 ◽

Vol 5 (3) ◽

pp. 44-51

Author(s):

Olga Mitryashkina ◽

Lydia Shulgina ◽

Yuriy Shulgin

Keyword(s):

Amino Acids ◽

Protein Content ◽

Muscle Tissue ◽

Human Body ◽

Raw Materials ◽

Farm Animals ◽

Elastic Tissue ◽

Canned Food ◽

Organoleptic Characteristics ◽

Vegetable Raw Materials

To activate the elastic tissues regeneration, a man needs to receive at least 5 g of such amino acids as proline and oxyproline, which are involved in the process of the body’s own collagen production, with food every day. The source of collagen can be products made from the hearts of farm animals. High temperature influence destroys collagen, and there is an accumulation of low-molecular peptides that are available to the human body. The article presents the results on the development of new types of canned food based on the farm animal hearts and plant raw materials. The animal hearts are high-protein raw materials in terms of protein content. The fat content does not exceed 3.7 ± 0.5 %, which results in a lower energy value compared to muscle tissue. Proteins in animal hearts are balanced in terms of amino acid composition; the content of collagen in them is 4.8–4.5 %, which is significantly higher than its amount in muscle tissue proteins. The researchers developed technology and recipes of canned food based on animal hearts and vegetable raw materials. The mass fraction of hearts in canned food recipes is 60.0–65.0 %. The additional components were beans and vegetables. Developed canned food made on the basis of animal hearts and vegetable raw materials had high organoleptic characteristics: protein content was 10.7–12.6 %; fat – 7.6–9.1 %. 100 g of canned food contains 0.85 ± ± 0.5 g of collagen-forming amino acids, which allows the human body to provide 16.5 ± ± 0.5 % of the daily need for them. Canned food is an additional source of iron (the content of which is 2.9 ± 0.3 g/100 g). A man recommends canned foods based on animal hearts and vegetable raw materials as specialized products for dietary and preventive nutrition of people of older age groups and persons with reduced processes of elastic tissue regeneration.

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