Oxidative status and total proteasomal proteolytic activity on skeletal muscles of hamsters with experimental emphysema

As a member of peroxiredoxin family, peroxiredoxin-3 plays a major role in the control of mitochondrial level of reactive oxygen species. During the breeding of experimental mice, we noticed that the peroxiredoxin-3 knockout mice were listless with aging. In the present study, we compared the swimming exercise performance and oxidative status between peroxiredoxin-3 knockout mice ( n = 15) and wild-type littermates ( n = 15). At the age of 10 months, the physical strength of peroxiredoxin-3 knockout mice was much lower than the wild-type littermates. Increased oxidative damage and decreased mitochondrial DNA copy number of the animal skeletal muscles were observed in peroxiredoxin-3 knockout mice as compared to that in the wild-type littermates. In addition, we found increased apoptotic cells in the brains of peroxiredoxin-3 knockout mice. Our results suggest that the deficiency of peroxiredoxin-3 induces accelerated oxidative stress and mitochondrial impairment, resulting in the decrease of energy supply and cellular activities. Peroxiredoxin-3 might be involved in the inhibition of aging process.

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Effects of low-dose oleuropein diet supplementation on the oxidative status of skeletal muscles and plasma hormonal concentration of growing broiler chickens

British Poultry Science ◽

10.1080/00071668.2019.1662886 ◽

2019 ◽

Vol 60 (6) ◽

pp. 784-789 ◽

Cited By ~ 3

Author(s):

R. Shimao ◽

H. Muroi ◽

K. Furukawa ◽

M. Toyomizu ◽

M. Kikusato

Keyword(s):

Skeletal Muscles ◽

Broiler Chickens ◽

Low Dose ◽

Oxidative Status ◽

Hormonal Concentration ◽

Diet Supplementation

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Expression and Complex Formation of MMP9, MMP2, NGAL, and TIMP1 in Porcine Myocardium but Not in Skeletal Muscles in Male Pigs with Tachycardia-Induced Systolic Heart Failure

BioMed Research International ◽

10.1155/2013/283856 ◽

2013 ◽

Vol 2013 ◽

pp. 1-12 ◽

Cited By ~ 10

Author(s):

Liliana Kiczak ◽

Alicja Tomaszek ◽

Jacek Bania ◽

Urszula Paslawska ◽

Maciej Zacharski ◽

...

Keyword(s):

Heart Failure ◽

Proteolytic Activity ◽

Skeletal Muscles ◽

Systolic Heart Failure ◽

Tissue Inhibitor Of Metalloproteinases ◽

Neutrophil Gelatinase Associated Lipocalin ◽

Remodeling Of Extracellular Matrix ◽

Neutrophil Gelatinase ◽

Formation Of Complexes

Matrix metalloproteinases (MMPs) are involved in the remodeling of extracellular matrix in various tissues. Their functioning could be related to the formation of complexes, containing MMP9, MMP2, tissue inhibitor of metalloproteinases type 1 (TIMP1), and neutrophil gelatinase-associated lipocalin (NGAL). Such complexes have not been investigated in either myocardial or skeletal muscles. We examined 20 male pigs with heart failure (HF), and 5 sham-operated animals. There were no differences in the mRNA expression of MMP9, MMP2, TIMP1, and NGAL between diseased and healthy animals, in either left ventricle (LV) myocardium or skeletal muscles. In LV from both diseased and healthy animals, in nonreducing and nondenaturing conditions, we demonstrated the presence of high molecular weight (HMW) complexes (130, 170, and 220 kDa) containing MMP9, TIMP1, and NGAL (also MMP2 in 220 kDa complex) without proteolytic activity, and a proteolytically active 115 kDa MMP9 form together with 72 and 68 kDa bands (proMMP2 and MMP2). Proteolytically active bands were also spontaneously released from HMW complexes. In skeletal muscles from both diseased and healthy animals, in nonreducing and nondenaturing conditions, we found no HMW complexes, and proteolytic activity was associated with the presence of 72 and 68 kDa bands (proMMP2 and MMP2).

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Distribution of c-protein isoforms in sarcomeres of developing chick skeletal muscle

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010010319x ◽

1988 ◽

Vol 46 ◽

pp. 226-227

Author(s):

D. A. Fischman ◽

J. E. Dennis ◽

T. Obinata ◽

H. Takano-Ohmuro

Keyword(s):

Skeletal Muscles ◽

Thick Filament ◽

Protein Isoforms ◽

Actin Binding ◽

Striated Muscles ◽

C Protein ◽

Sarcomeric Protein ◽

Thick Filaments ◽

Cross Bridges ◽

Bridge Bearing

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.

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The effect of ionophore A23178 on the α-actinin crosslinks in the z-band of frog skeletal muscle: An EM study

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142396 ◽

1986 ◽

Vol 44 ◽

pp. 154-155

Author(s):

F.T. Llados ◽

V. Krlho ◽

G.D. Pappas

Keyword(s):

Muscle Damage ◽

Transmitter Release ◽

Skeletal Muscles ◽

Calcium Uptake ◽

Muscle Membrane ◽

Frog Skeletal Muscle ◽

Ach Release ◽

Sustained Action ◽

Calcium Deposits ◽

Intense Stimulation

It Is known that Ca++ enters the muscle fiber at the junctional area during the action of the neurotransmitter, acetylcholine (ACh). Pappas and Rose demonstrated that following Intense stimulation, calcium deposits are found In the postsynaptic muscle membrane, Indicating the existence of calcium uptake In the postsynaptic area following ACh release. In addition to this calcium uptake, when mammal Ian skeletal muscles are exposed to a sustained action of the neurotransmitter, muscle damage develops. These same effects, l.e., Increased transmitter release, calcium uptake and finally muscle damage, can be obtained by Incubating the muscle with lonophore A23178.

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Sem Observations in Gastric Mucosa Exposed to Progressive Enzymatic Etching

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s1431927600002531 ◽

1980 ◽

Vol 38 ◽

pp. 570-571

Author(s):

C.A.E. Lemmi ◽

D. Booth ◽

G.E. Adomian

Keyword(s):

Gastric Mucosa ◽

Critical Point ◽

Proteolytic Activity ◽

Etching Process ◽

Cellular Types

In order to enrich populations of homogeneous cellular types we dissociated gastric mucosa by enzymatic techniques. In addition, we used SEM to monitor the progressive etching of the mucosa. Two enzymes were tested: collagenase III with minimum proteolytic activity and Pronase with broader proteolytic effects. The gastric mucosa was exposed to the effect of the enzymes using everted stomach preparations. In this way the digestive action occured progressively from the lumen of the stomach toward the base of the glands. This “etching” process could be monitored conveniently by SEM. After incubation for periods varying from 30 to 210 minutes the tissues were stretched on dental wax, fixed in 2 % glutaralheyde, post-fixed in osmium, dehydrated, critical point dryed and coated with gold. A model MSM-5 “Mini-SEM” was used for observation. Gentle uncurling of the preparation before coating with gold produced fractures which revealed the structure of the gastric glandsin more detail.

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Apoptosis and disturbed cellular composition in experimental emphysema

Pneumologie ◽

10.1055/s-0030-1251213 ◽

2010 ◽

Vol 64 (S 03) ◽

Author(s):

L Farkas ◽

D Farkas ◽

J Gauldie ◽

W Shi ◽

M Kolb

Keyword(s):

Cellular Composition ◽

Experimental Emphysema

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