Polyubiquitin in crustacean striated muscle: increased expression and conjugation during molt-induced claw muscle atrophy

1995 ◽  
Vol 1264 (3) ◽  
pp. 312-322 ◽  
Author(s):  
Blair S. Shean ◽  
Donald L. Mykles
Keyword(s):  
Muscle Atrophy ◽  
Striated Muscle ◽  
Claw Muscle

scholarly journals Supraphysiological levels of GDF 11 induce striated muscle atrophy

2017 ◽  
Vol 9 (4) ◽  
pp. 531-544 ◽  
Author(s):  
David W Hammers ◽  
Melissa Merscham‐Banda ◽  
Jennifer Ying Hsiao ◽  
Stefan Engst ◽  
James J Hartman ◽  
...  
Keyword(s):  
Muscle Atrophy ◽  
Striated Muscle

A rabbit model for studying degeneration and regeneration properties of young striated muscle at different distraction rates

2012 ◽  
Vol 60 (2) ◽  
pp. 223-232
Author(s):  
Sándor Berki ◽  
Tamás Klára ◽  
György Szőke ◽  
Tibor Németh ◽  
Miklós Dunay ◽  
...  
Keyword(s):  
Muscle Fibre ◽  
Muscle Atrophy ◽  
Scoring System ◽  
Striated Muscle ◽  
Rabbit Model ◽  
Limb Lengthening ◽  
Skeletally Immature ◽  
Histopathological Changes ◽  
Histological Changes ◽  
Semiquantitative Method

The present study evaluated the histological changes in the muscle tissue after limb lengthening in skeletally immature rabbits and assessed the effect of different lengthening rates on the regeneration and degeneration properties of striated muscle. Thirteen different lengthening protocols were applied on a total of 16 male domestic white rabbits divided into four groups. The histopathological changes were analysed by a semiquantitative method according to the scoring system of Lee et al. (1993). After evaluation of the five main degenerative parameters (muscle atrophy, internalisation of muscle nuclei, degeneration of the muscle fibre, perimysial and endomysial fibrosis, haematomas), it is evident that rabbits subjected to limb lengthening at a rate of 3.2 mm/day showed more degenerative changes than those limb-lengthened at 0.8 or 1.6 mm/day. Our study showed that the regenerative mechanisms were not endless. If the daily lengthening rate reached the 3.2 mm/day limit, the regenerating ability of the muscle decreased, and signs of degeneration increased significantly.

scholarly journals Neurohypophyseal hormones and skeletal muscle: a tale of two faces

2020 ◽  
Vol 30 (1) ◽  
pp. 53-57
Author(s):  
Alexandra Benoni ◽  
Alessandra Renzini ◽  
Giorgia Cavioli ◽  
Sergio Adamo
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Cancer Cachexia ◽  
Muscle Wasting ◽  
Striated Muscle ◽  
Cardiac Atrophy ◽  
Neurohypophyseal Hormones

The neurohypophyseal hormones vasopressin and oxytocin were invested, in recent years, with novel functions upon striated muscle, regulating its differentiation, trophism, and homeostasis. Recent studies highlight that these hormones not only target skeletal muscle but represent novel myokines. We discuss the possibility of exploiting the muscle hypertrophying activity of oxytocin to revert muscle atrophy, including cancer cachexia muscle wasting. Furthermore, the role of oxytocin in cardiac homeostasis and the possible role of cardiac atrophy as a concause of death in cachectic patients is discussed.

scholarly journals Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1

2014 ◽  
Vol 307 (6) ◽  
pp. E469-E484 ◽  
Author(s):  
Sue C. Bodine ◽  
Leslie M. Baehr
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Striated Muscle ◽  
Expression Patterns ◽  
Ring Finger ◽  
Physiological Role ◽  
Ubiquitin Ligases ◽  
Skeletal Muscle Atrophy ◽  
E3 Ubiquitin Ligases ◽  
Cellular Functions

Muscle RING finger 1 (MuRF1) and muscle atrophy F-box (MAFbx)/atrogin-1 were identified more than 10 years ago as two muscle-specific E3 ubiquitin ligases that are increased transcriptionally in skeletal muscle under atrophy-inducing conditions, making them excellent markers of muscle atrophy. In the past 10 years much has been published about MuRF1 and MAFbx with respect to their mRNA expression patterns under atrophy-inducing conditions, their transcriptional regulation, and their putative substrates. However, much remains to be learned about the physiological role of both genes in the regulation of mass and other cellular functions in striated muscle. Although both MuRF1 and MAFbx are enriched in skeletal, cardiac, and smooth muscle, this review will focus on the current understanding of MuRF1 and MAFbx in skeletal muscle, highlighting the critical questions that remain to be answered.

Ultrastructural Localization of Acid Mucosubstance in Skeletal Muscle

1967 ◽  
Vol 25 ◽  
pp. 52-53 ◽  
Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer
Keyword(s):  
Striated Muscle ◽  
Divalent Cations ◽  
Ultrastructural Localization ◽  
Major Elements ◽  
Frozen Sections ◽  
Thorium Dioxide ◽  
Iron Solution ◽  
Coupling System ◽  
Psoas Muscles ◽  
Formalin Fixed

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.

Quantitative Freeze Fracture Studies of Gap Junctions in Somatic Cell Hybrids, Their Parents, and Revertants

1976 ◽  
Vol 34 ◽  
pp. 218-219
Author(s):  
W. J. Larsen ◽  
R. Azarnia ◽  
W. R. Loewenstein
Keyword(s):  
Gap Junctions ◽  
Striated Muscle ◽  
Freeze Fracture ◽  
Cell Movement ◽  
Dye Molecules ◽  
Somatic Cell Hybrids ◽  
Cell Coupling ◽  
Normal Cells ◽  
Mediate Cell ◽  
Almost All

Although the physiological significance of the gap junction remains unspecified, these membrane specializations are now recognized as common to almost all normal cells (excluding adult striated muscle and some nerve cells) and are found in organisms ranging from the coelenterates to man. Since it appears likely that these structures mediate the cell-to-cell movement of ions and small dye molecules in some electrical tissues, we undertook this study with the objective of determining whether gap junctions in inexcitable tissues also mediate cell-to-cell coupling.To test this hypothesis, a coupling, human Lesh-Nyhan (LN) cell was fused with a non-coupling, mouse cl-1D cell, and the hybrids, revertants, and parental cells were analysed for coupling with respect both to ions and fluorescein and for membrane junctions with the freeze fracture technique.

Orientation of actin filaments during motion in motility assay

1995 ◽  
Vol 53 ◽  
pp. 52-53
Author(s):  
J. Borejdo ◽  
S. Burlacu
Keyword(s):  
Actin Filaments ◽  
Thin Filament ◽  
Striated Muscle ◽  
Myosin Head ◽  
Classical Method ◽  
Polarization Of Fluorescence ◽  
Single Protein ◽  
Intracellular Organelles ◽  
Change Orientation ◽  
Active Entity

Polarization of fluorescence is a classical method to assess orientation or mobility of macromolecules. It has been a common practice to measure polarization of fluorescence through a microscope to characterize orientation or mobility of intracellular organelles, for example anisotropic bands in striated muscle. Recently, we have extended this technique to characterize single protein molecules. The scientific question concerned the current problem in muscle motility: whether myosin heads or actin filaments change orientation during contraction. The classical view is that the force-generating step in muscle is caused by change in orientation of myosin head (subfragment-1 or SI) relative to the axis of thin filament. The molecular impeller which causes this change resides at the interface between actin and SI, but it is not clear whether only the myosin head or both SI and actin change orientation during contraction. Most studies assume that observed orientational change in myosin head is a reflection of the fact that myosin is an active entity and actin serves merely as a passive "rail" on which myosin moves.

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