Fiber-type-specific αB-crystallin distribution and its shifts with T3 and PTU treatments in rat hindlimb muscles

2000 ◽  
Vol 88 (4) ◽  
pp. 1355-1364 ◽  
Author(s):  
Yoriko Atomi ◽  
Kyoko Toro ◽  
Tsuyoshi Masuda ◽  
Hideo Hatta
Keyword(s):  
Fiber Type ◽  
Stress Protein ◽  
Type I ◽  
Gray Level ◽  
Type Ii ◽  
Adult Rat ◽  
Hindlimb Muscles ◽  
Αb Crystallin ◽  
Distribution Shifts ◽  
Edl Muscle

Changes in αB-crystallin content in adult rat soleus and extensor digitorum longus (EDL) were examined after 8 wk of 3,5,3′-triiodothyronine (T3) and propylthiouracil (PTU) treatments. Cellular distributions of αB-crystallin expression related to fiber type, and distribution shifts with these treatments were also examined in detail from the gray level of reactivity to specific anti-αB-crystallin antibody. αB-crystallin content in both soleus and EDL muscles was significantly decreased after T3, and that in EDL was significantly increased over twofold after PTU treatment. In both control soleus and EDL muscles, the gray level of type I fibers was higher than that of type II fibers. αB-crystallin expression among type II subtypes was muscle specific; the order was type I > IIa > IIx > IIb in control EDL muscle and type IIx ≥ IIa in soleus muscle. The relation was basically unchanged in both muscles after T3 treatment and was, in particular, well maintained in EDL muscle. Under hypothyroidism conditions with PTU, the mean αB-crystallin levels of type IIa and IIx fibers were significantly lower than levels under control conditions. Thus the relation between fiber type and the expression manner of stress protein αB-crystallin is muscle specific and also is well regulated under thyroid hormone, especially in fast EDL muscle.

scholarly journals Phosphorylation of αB-crystallin and its cytoskeleton association differs in skeletal myofiber types depending on resistance exercise intensity and volume

2019 ◽  
Vol 126 (6) ◽  
pp. 1607-1618 ◽  
Author(s):  
Daniel Jacko ◽  
Käthe Bersiner ◽  
Jonas Hebchen ◽  
Markus de Marées ◽  
Wilhelm Bloch ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Resistance Exercise ◽  
Mechanical Stress ◽  
Fiber Type ◽  
Type I ◽  
Type Ii ◽  
Αb Crystallin ◽  
Serine 59 ◽  
Type I Fibers ◽  
Type Ii Fibers

αB-crystallin (CRYAB) is an important actor in the immediate cell stabilizing response following mechanical stress in skeletal muscle. Yet, only little is known regarding myofiber type-specific stress responses of CRYAB. We investigated whether the phosphorylation of CRYAB at serine 59 (pCRYABSer59) and its cytoskeleton association are influenced by varying load-intensity and -volume in a fiber type-specific manner. Male subjects were assigned to 1, 5, and 10 sets of different acute resistance exercise protocols: hypertrophy (HYP), maximum strength (MAX), strength endurance (SE), low intensity (LI), and three sets of maximum eccentric resistance exercise (ECC). Skeletal muscle biopsies were taken at baseline and 30 min after exercise. Western blot revealed an increase inpCRYABSer59only following 5 and 10 sets in groups HYP, MAX, SE, and LI as well as following 3 sets in the ECC group. In type I fibers, immunohistochemistry determined increasedpCRYABSer59in all groups. In type II fibers,pCRYABSer59only increased in MAX and ECC groups, with the increase in type II fibers exceeding that of type I fibers in ECC. Association of CRYAB andpCRYABSer59with the cytoskeleton reflected the fiber type-specific phosphorylation pattern. Phosphorylation of CRYAB and its association with the cytoskeleton in type I and II myofibers is highly specific in terms of loading intensity and volume. Most likely, this is based on specific recruitment patterns of the different myofiber entities due to the different resistance exercise loadings. We conclude thatpCRYABSer59indicates contraction-induced mechanical stress exposure of single myofibers in consequence of resistance exercise.NEW & NOTEWORTHY We determined that the phosphorylation of αB-crystallin at serine 59 (pCRYABSer59) after resistance exercise differs between myofiber types in a load- and intensity-dependent manner. The determination ofpCRYABSer59could serve as a marker indirectly indicating contractile involvement and applied mechanical stress on individual fibers. By that, it is possible to retrospectively assess the impact of resistance exercise loading on skeletal muscle fiber entities.

Absolute amounts and diffusibility of HSP72, HSP25, and αB-crystallin in fast- and slow-twitch skeletal muscle fibers of rat

2012 ◽  
Vol 302 (1) ◽  
pp. C228-C239 ◽  
Author(s):  
Noni T. Larkins ◽  
Robyn M. Murphy ◽  
Graham D. Lamb
Keyword(s):  
Stress Responses ◽  
Type I ◽  
Type Ii ◽  
Plasmic Reticulum ◽  
Αb Crystallin ◽  
Cellular Stress Responses ◽  
Edl Muscle ◽  
Shock Proteins ◽  
Type I Fibers ◽  
Type Ii Fibers

Heat shock proteins (HSPs) are essential for normal cellular stress responses. Absolute amounts of HSP72, HSP25, and αB-crystallin in rat extensor digitorum longus (EDL) and soleus (SOL) muscle were ascertained by quantitative Western blotting to better understand their respective capabilities and limitations. HSP72 content of EDL and SOL muscle was only ∼1.1 and 4.6 μmol/kg wet wt, respectively, and HSP25 content approximately twofold greater (∼3.4 and ∼8.9 μmol/kg, respectively). αB-crystallin content of EDL muscle was ∼4.9 μmol/kg but in SOL muscle was ∼30-fold higher (∼140 μmol/kg). To examine fiber heterogeneity, HSP content was also assessed in individual fiber segments; every EDL type II fiber had less of each HSP than any SOL type I fiber, whereas the two SOL type II fibers examined were indistinguishable from the EDL type II fibers. Sarcolemma removal (fiber skinning) demonstrated that 10–20% of HSP25 and αB-crystallin was sarcolemma-associated in SOL fibers. HSP diffusibility was assessed from the extent and rate of diffusion out of skinned fiber segments. In unstressed SOL fibers, 70–90% of each HSP was readily diffusible, whereas ∼95% remained tightly bound in fibers from SOL muscles heated to 45°C. Membrane disruption with Triton X-100 allowed dispersion of HSP72 and sarco(endo)plasmic reticulum Ca2+-ATPase pumps but did not alter binding of HSP25 or αB-crystallin. The amount of HSP72 in unstressed EDL muscle is much less than the number of its putative binding sites, whereas SOL type I fibers contain large amounts of αB-crystallin, suggesting its importance in normal cellular function without upregulation.

scholarly journals Muscle Changes in Lambs with Surgically Created Scoliosis Produced in Utero

1978 ◽  
Vol 5 (3) ◽  
pp. 283-287 ◽  
Author(s):  
G.M. Kent ◽  
W. Zingg ◽  
D. Armstrong
Keyword(s):  
Musculoskeletal Diseases ◽  
Fiber Type ◽  
Surgical Techniques ◽  
Spinal Curvature ◽  
Surgical Trauma ◽  
Developmental Defect ◽  
Type I ◽  
Type Ii ◽  
Muscle Changes ◽  
Type Ii Fibers

SUMMARY:Spinal curves may be produced in fetal lambs with three surgical techniques. These procedures vary from mere exposure of the costo-vertebral junction of three ribs through a paravertebral incision, to resection of the head and part of the adjacent shaft of three ribs. The fetal age varies from forty-nine to seventy-three days. The degree of curvature present at birth seems to increase in severity with decreasing fetal age at the time of surgery, but the type of surgical procedure does not appear to influence the severity of the curve, suggesting that the mechanical presence of the ribs does not prevent the development of scoliosis in these animals.Histological studies of the m. longissimus dorsi at the apices of the curves reveal two main types of abnormality in the muscle fibers. Both Type I and Type II fibers were significantly reduced in size in the biopsies taken from the side on which the surgery was performed, and there was marked alteration in the proportion of one fiber type to the other in most biopsies taken from both operated sides when compared with biopsies from unoperated twin animals.The fetal age and amount of surgical trauma appeared to play no role in the degree of muscle alteration, suggesting that even minimal surgical trauma to the paraspinal region at any fetal age between 49–73 days is sufficient to produce significant muscle fiber abnormality and spinal curvature.A parallel is drawn between these muscle findings and those in a number of human musculoskeletal diseases, and suggests the possibility of a developmental defect in the pathogenesis of these diseases.

Rostrocaudal pattern of fiber-type changes in an overloaded rat ankle extensor

1991 ◽  
Vol 71 (2) ◽  
pp. 558-564 ◽  
Author(s):  
P. F. Gardiner ◽  
B. J. Jasmin ◽  
P. Corriveau
Keyword(s):  
Fiber Type ◽  
Muscle Length ◽  
Similar Degree ◽  
Complex Nature ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Cross Sectional ◽  
Hypertrophic Response ◽  
Type I Fibers

Our aim was to quantify the overload-induced hypertrophy and conversion of fiber types (type II to I) occurring in the medial head of the gastrocnemius muscle (MG). Overload of MG was induced by a bilateral tenotomy/retraction of synergists, followed by 12–18 wk of regular treadmill locomotion (2 h of walking/running per day on 3 of 4 days). We counted all type I fibers and determined type I and II mean fiber areas in eight equidistant sections taken along the length of control and overloaded MG. Increase in muscle weights (31%), as well as in total muscle cross-sectional areas (37%) and fiber areas (type I, 57%; type II, 34%), attested to a significant hypertrophic response in overloaded MG. An increase in type I fiber composition of MG from 7.0 to 11.5% occurred as a result of overload, with the greatest and only statistically significant changes (approximately 70–100%) being found in sections taken from the most rostral 45% of the muscle length. Results of analysis of sections taken from the largest muscle girth showed that it significantly underestimated the extent of fiber conversion that occurred throughout the muscle as a whole. These data obtained on the MG, which possesses a compartmentalization of fiber types, support the notion that all fiber types respond to this model with a similar degree of hypertrophy. Also, they emphasize the complex nature of the adaptive changes that occur in these types of muscles as a result of overload.

scholarly journals Axodendritic versus axosomatic cochlear efferent termination is determined by afferent type in a hierarchical logic of circuit formation

2021 ◽  
Vol 7 (4) ◽  
pp. eabd8637
Author(s):  
Jemma L. Webber ◽  
John C. Clancy ◽  
Yingjie Zhou ◽  
Natalia Yraola ◽  
Kazuaki Homma ◽  
...  
Keyword(s):  
Hair Cells ◽  
Fiber Type ◽  
Afferent Fiber ◽  
Outer Hair Cells ◽  
Type I ◽  
Type Ii ◽  
Efferent Neurons ◽  
Distinct Pair ◽  
Mechanosensory Hair Cells ◽  
Circuit Formation

Hearing involves a stereotyped neural network communicating cochlea and brain. How this sensorineural circuit assembles is largely unknown. The cochlea houses two types of mechanosensory hair cells differing in function (sound transmission versus amplification) and location (inner versus outer compartments). Inner (IHCs) and outer hair cells (OHCs) are each innervated by a distinct pair of afferent and efferent neurons: IHCs are contacted by type I afferents receiving axodendritic efferent contacts; OHCs are contacted by type II afferents and axosomatically terminating efferents. Using an Insm1 mouse mutant with IHCs in the position of OHCs, we discover a hierarchical sequence of instructions in which first IHCs attract, and OHCs repel, type I afferents; second, type II afferents innervate hair cells not contacted by type I afferents; and last, afferent fiber type determines if and how efferents innervate, whether axodendritically on the afferent, axosomatically on the hair cell, or not at all.

Intermittent cold exposure causes a muscle-specific shift in the fiber type composition in rats

1993 ◽  
Vol 75 (1) ◽  
pp. 264-267 ◽  
Author(s):  
T. J. Walters ◽  
S. H. Constable
Keyword(s):  
Soleus Muscle ◽  
Cold Exposure ◽  
Citrate Synthase ◽  
Fiber Type ◽  
Type I ◽  
Fiber Type Composition ◽  
Type Composition ◽  
Edl Muscle ◽  
Type I Fibers

We examined the effect of long-term intermittent cold exposure on the fiber type composition of the predominantly type I soleus and the predominantly type IIb extensor digitorum longus (EDL) muscles of rats. Cold exposure was accomplished by submerging the rats in shoulder-deep water, maintained at 20 +/- 0.5 degrees C, for 1 h/day, 5 days/wk, for < or = 19 wk. The efficacy of the treatment was tested by subjecting both groups to 20 degrees C water for 45 min while rectal temperature (Tre) and O2 consumption (VO2) were measured. The cold-exposed group displayed a 22% smaller reduction in Tre (P < 0.05) at the end of the exposure and 23% greater VO2 (P < 0.05) during the same period. Fiber type composition was determined using routine histochemical methods for myosin-adenosinetriphosphatase. In the soleus muscle of the cold-exposed rats, the number of type IIa fibers increased 156% (P < 0.05) and the number of type I fibers decreased 24% (P < 0.05). Cold exposure had no significant influence on the fiber type composition of the EDL muscle. Cold exposure resulted in an increase in citrate synthase activity of 20 and 22% in the soleus and EDL muscles, respectively (P < 0.05). The present study demonstrates that intermittent cold exposure induces a type I-to-type IIa transformation in the soleus muscle while having no influence on the EDL muscle.

Histochemical and physiological characteristics of the rat diaphragm

1985 ◽  
Vol 58 (4) ◽  
pp. 1085-1091 ◽  
Author(s):  
J. M. Metzger ◽  
K. B. Scheidt ◽  
R. H. Fitts
Keyword(s):  
Fiber Type ◽  
Contractile Properties ◽  
Effect Of Temperature ◽  
Type I ◽  
Force Frequency ◽  
Rat Diaphragm ◽  
Shortening Velocity ◽  
Type Distribution ◽  
Adult Rat ◽  
Fiber Type Distribution

The histochemical and contractile characteristics of the adult rat diaphragm were determined. Based on enzyme histochemistry, the rat diaphragm contained 40% type I, 27% type IIa, and 34% type IIb fibers. There were significantly more type I fibers in the ventral costal (VEN) compared with the crural (CRU) region of the muscle and a slightly higher percentage of type I's on the thoracic relative to the abdominal surface. The contractile properties and the effect of temperature (Q10) were similar in the VEN and CRU regions. Increasing temperature produced higher isometric peak tetanic tension, whereas twitch tension, contraction, and one-half relaxation time all decreased. The maximal shortening velocity increased linearly from 22 and 30 degrees C, then plateaued before decreasing between 35 and 37 degrees C. The VEN and CRU force-velocity curves became less concave as temperature increased from 22 to 35 degrees C. Furthermore, the force-frequency relation of both regions was shifted to the right as temperature increased. The isometric and isotonic contractile properties and fiber type distribution are similar in the VEN and CRU regions of the diaphragm. The rat diaphragm is clearly heterogeneous in fiber type distribution and functionally lies intermediate between slow- and fast-twitch limb skeletal muscles.

scholarly journals Denervation and reinnervation of fast and slow muscles. A histochemical study in rats.

1975 ◽  
Vol 23 (11) ◽  
pp. 808-827 ◽  
Author(s):  
M M Jaweed ◽  
G J Herbison ◽  
J F Ditunno
Keyword(s):  
Fiber Diameter ◽  
Histochemical Study ◽  
Fiber Type ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Type I Fibers ◽  
Type Ii Fibers ◽  
Fast Muscles ◽  
Slow And Fast Muscles

A histochemical study, using myosin-adenosine triphosphatase activity at pH 9.4, was conducted in soleus and plantaris muscles of adult rats, after bilateral crushing of the sciatic nerve at the sciatic notch. The changes in fiber diameter and per cent composition of type I and type II fibers plus muscle weights were evaluated along the course of denervation-reinnervation curve at 1, 2, 3, 4 and 6 weeks postnerve crush. The study revealed that in the early denervation phase (up to 2 weeks postcrush) both the slow and fast muscles, soleus and plantaris, resepctively, atrophied similarly in muscle mass. Soleus increased in the number of type II fibers, which may be attributed to "disuse" effect. During the same period, the type I fibers of soleus atrophied as much or slightly more than the type II fibers; whereas the type II fibers of plantaris atrophied significantly more than the type I fibers, reflecting that the process of denervation, in its early stages, may affect the two fiber types differentially in the slow and fast muscles. It was deduced that the type I fibers of plantaris may be essentially different in the slow (soleus) and fast (plantaris) muscles under study. The onset of reinnervation, as determined by the increase in muscle weight and fiber diameter of the major fiber type, occurred in soleus and plantaris at 2 and 3 weeks postcrush, respectively, which confirms the earlier hypotheses that the slow muscles are reinnervated sooner than the fast muscles. It is suggested that the reinnervation of muscle after crush injury may be specific to the muscle type or its predominant fiber type.

scholarly journals Structural features of alveolar wall basement membrane in the adult rat lung.

1981 ◽  
Vol 91 (2) ◽  
pp. 427-437 ◽  
Author(s):  
C A Vaccaro ◽  
J S Brody
Keyword(s):  
Basement Membrane ◽  
Ruthenium Red ◽  
Basement Membranes ◽  
Alveolar Wall ◽  
Type I ◽  
Type Ii ◽  
Rat Lung ◽  
Anionic Sites ◽  
Lamina Densa ◽  
Adult Rat

The ultrastructural characteristics of alveolar (ABM) and capillary (CBM) basement membranes in the adult rat lung have been defined using tannic acid fixation, ruthenium red staining, or incubation in guanidine HCl. ABM is dense and amorphous, has 3- to 5-nm filaments in the lamina rara externa (facing the alveolus) that run between the lamina densa and the basal cell surface of the epithelium, has an orderly array of ruthenium red-positive anionic sites that appear predominantly (79%) on the lamina rara externa, and has discontinuities beneath alveolar type II cells but not type I cells that allow penetration of type II cytoplasmic processes into the interstitium of the alveolar wall. The CBM is fibrillar and less compact than ABM, has no lamina rara filaments, and has one fifth the number of ruthenium red-positive anionic sites of ABM that appear predominantly (64%) overlying the lamina densa. Incubation of lung tissue with Flavobacterium heparinum enzyme or with chondroitinase has shown that ABM anionic sites represent heparan sulfate proteoglycans, whereas CBM anionic sites contain this and other sulfated proteoglycans. The CBM fuses in a local fashion with ABM, compartmentalizing the alveolar wall into a thick and thin side and establishing a thin, single, basement-membrane gas-exchange surface between alveolar air, and capillary blood. The potential implications of ABM and CBM ultrastructure for permeability, cell differentiation, and repair and morphogenesis of the lung are discussed.

scholarly journals Satellite cell content is specifically reduced in type II skeletal muscle fibers in the elderly

2007 ◽  
Vol 292 (1) ◽  
pp. E151-E157 ◽  
Author(s):  
Lex B. Verdijk ◽  
René Koopman ◽  
Gert Schaart ◽  
Kenneth Meijer ◽  
Hans H. C. M. Savelberg ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Fiber Type ◽  
The Elderly ◽  
Type I ◽  
Type Ii ◽  
Fiber Area ◽  
Muscle Fiber Atrophy ◽  
Fiber Atrophy ◽  
Type Ii Fibers

Satellite cells (SC) are essential for skeletal muscle growth and repair. Because sarcopenia is associated with type II muscle fiber atrophy, we hypothesized that SC content is specifically reduced in the type II fibers in the elderly. A total of eight elderly (E; 76 ± 1 yr) and eight young (Y; 20 ± 1 yr) healthy males were selected. Muscle biopsies were collected from the vastus lateralis in both legs. ATPase staining and a pax7-antibody were used to determine fiber type-specific SC content (i.e., pax7-positive SC) on serial muscle cross sections. In contrast to the type I fibers, the proportion and mean cross-sectional area of the type II fibers were substantially reduced in E vs. Y. The number of SC per type I fiber was similar in E and Y. However, the number of SC per type II fiber was substantially lower in E vs. Y (0.044 ± 0.003 vs. 0.080 ± 0.007; P < 0.01). In addition, in the type II fibers, the number of SC relative to the total number of nuclei and the number of SC per fiber area were also significantly lower in E. This study is the first to show type II fiber atrophy in the elderly to be associated with a fiber type-specific decline in SC content. The latter is evident when SC content is expressed per fiber or per fiber area. The decline in SC content might be an important factor in the etiology of type II muscle fiber atrophy, which accompanies the loss of skeletal muscle with aging.

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