Emergence of the mature myosin phenotype in the rat diaphragm muscle

LaFramboise, William A.; Daood, Monica J.; Guthrie, Robert D.; Schiaffino, Stefano; Moretti, Paolo; Brozanski, Beverly; Butler-Browne, Gillian; Whalen, Robert G.; Ontell, Marcia

doi:10.1016/0012-1606(91)90473-g

Cited by 89 publications

(61 citation statements)

References 33 publications

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“…Myosin for electropho resis was prepared by scissor-mincing the muscle tissue in a high salt solution, pH 6.5 at 4°C for 40 min (14). Extracts were centrifuged and supernatants recovered and treated as follows.…”

Section: Methodsmentioning

confidence: 99%

“…Electrophoresis (275 V for 3.5 h then 178 V for 17.5 h) was performed by using a vertical-slab gel unit (SE600, Hoefer Scientific Instruments) with Tris/glycine run ning buffer (29) in a cold room maintained at 4°C. Separating gels were silver stained (14). Monoclonal antibodies were used to identify the specific MHC bands (MHCsi0W , MHCna, MHCiix, MHCub) separated on SDS-polyacrylamide gel elec trophoresis gels and included 1) antibody BF-32 to MHCsi0W and MHCna; 2) antibody SC-71 to MHCua; 3) BF-35 to all but MHCnx; 4) BF-F3 to MHCnb; and 5) RT-D9 to MBClhL and MHCub (14).…”

Section: Methodsmentioning

confidence: 99%

“…Separating gels were silver stained (14). Monoclonal antibodies were used to identify the specific MHC bands (MHCsi0W , MHCna, MHCiix, MHCub) separated on SDS-polyacrylamide gel elec trophoresis gels and included 1) antibody BF-32 to MHCsi0W and MHCna; 2) antibody SC-71 to MHCua; 3) BF-35 to all but MHCnx; 4) BF-F3 to MHCnb; and 5) RT-D9 to MBClhL and MHCub (14). MHC gels were analyzed by using a scanning densitometer (GS 300 Hoefer Scientific) and densitometry software (GS 365, Hoefer Scientific) to quantify the area under individual isoform peaks.…”

Section: Methodsmentioning

confidence: 99%

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Combined myofibrillar and mitochondrial creatine kinase deficiency impairs mouse diaphragm isotonic function

Watchko

Daood

Sieck³

et al. 1997

Journal of Applied Physiology

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atine kinase deficiency impairs mouse diaphragm isotonic function. J. Appl. Physiol. 82(5): 1416-1423,1997.-Creatine kinase (CK) is an enzyme central to cellular high-energy phosphate metabolism in muscle. To characterize the physi ological role of CK in respiratory muscle during dynamic contractions, we compared the fore e-velocity relationships, power, and work output characteristics of the diaphragm (Dia) from mice with combined myofibrillar and sarcomeric mitochondrial CK deficiency (CK [-7-]) with CK-sufficient controls (Ctl). Maximum velocity of shortening was signifi cantly lower in CK[-/-] Dia (14.1 ± 0.9 L Js7 where L0 is optimal fiber length) compared with Ctl Dia (17.5 ± 1.1 LJs) (P < 0.01). Maximum power was obtained at 0.4-0.5 tetanic force in both groups; absolute maximum power (2,293 ± 138 W/m2) and work (201 ± 9 J/m2) were lower in CK[-/ -] Dia compared with Ctl Dia (2,744 ± 146 W/m2 and 284 ± 26 J/m2, respectively) (P < 0.05). The ability of CK [-/-] Dia to sustain shortening during repetitive isotonic activation (75 Hz, 330-ms duration repeated each second at 0.4 tetanic force load) was markedly impaired, with CK[-/-] Dia power and work declining to zero by 37 ± 4 s, compared with 61 ± 5 s in Ctl Dia. We conclude that combined myofibrillar and sarcomeric mitochondrial CK deficiency profoundly impairs Dia power and work output, underscoring the functional importance of CK during dynamic contractions in skeletal muscle. respiratory muscle; fatigue; myosin heavy chain r e s p i r a t o r y MUSCLE FATIGUE is a phenom enon of clini cal im portance contributing to the development of ventilatory failure in neonates and adults. The factors predisposing muscle to fatigue are felt prim arily to resu lt from an im balance betw een energy supply and dem and (25, 35). The accum ulation of energy m etabo lites in all probability also plays an im portant role (1,6,8). A lteration of th e capacity of skeletal muscle to produce or sustain ATP levels is th u s likely to affect muscle fatigue resistance. C reatine kinase (CK), an enzyme central to cellular high-energy phosphate m e tabolism in muscle, m ay be im p o rtan t in this regard. CK catalyzes the following reaction PC r +MgAJDP-+ H + <=> Cr + MgATP2" where PC r is phosphocreatine and Cr is creatine. The high level of CK activity found in skeletal muscle ensures th at, w hen consistent high-energy phosphate production is necessary during repetitive contractile activity, ATP levels will be m aintained at the expense of PCr. This role of CK as an ATP buffer is widely accepted (18, 33).Defining a physiological role for CK in skeletal muscle fatigue, however, has been difficult, with prior studies using substrate analogs (10,16,17,20) of Cr to assess the functional consequences of impaired CK activity. These studies have generated disparate re sults and exclusively examined fatigue under repetitive isometric conditions. The respiratory muscles' capacity to sustain ventilation, however, is determined in large p a rt by its ability to shorten and m aintain for...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Combined myofibrillar and mitochondrial creatine kinase deficiency impairs mouse diaphragm isotonic function

Watchko

Daood

Sieck³

et al. 1997

Journal of Applied Physiology

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“…Third, a differential augmentation of expression occurs during the early postnatal maturation of the fast fiber population, giving rise to a IIBϾIIXϾIIA differential expression pattern. It is interesting to note that each of these three developmental steps is spatiotemporally associated with one of three developmental regulatory events at the fast MHC gene cluster (Weydert et al, 1987;Russell et al, 1988;Condon et al, 1990a;LaFramboise et al, 1991;Weiss et al, 1999). These are, in corresponding order: First, tissue-specific activation of the fast MHC gene cluster during myoblast differentiation, with resultant expression of the MHCemb gene; Second, activation of the MHCperi gene during formation of secondary fibers; Third, differential activation of the adult fast MHC isoforms IIB, IIX, and IIA during early postnatal maturation of the fast fiber population.…”

Section: Relationship To Fast Mhc Gene Regulationmentioning

confidence: 99%

TnIfast IRE enhancer: Multistep developmental regulation during skeletal muscle fiber type differentiation

Hallauer

Hastings

2002

Developmental Dynamics

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To identify developmental steps leading to adult skeletal muscle fiber-type-specific gene expression, we carried out transgenic mouse studies of the IRE enhancer of the quail TnIfast gene. Histochemical analysis of IRE/herpesvirus tk promoter/␤-galactosidase reporter transgene expression in adult muscle directly demonstrated IRE-driven fast vs. slow fiber-type specificity, and IIB>IIX>IIA differential expression among the fast fiber types: patterns similar to those of native-promoter TnIfast constructs. These tissue-and cell-type specificities are autonomous to the IRE and do not depend on interactions with a muscle gene promoter. Developmental studies showed that the adult pattern of IRE-driven transgene expression emerges in three steps: (1) activation during the formation of primary embryonic (presumptive slow) muscle fibers; (2) activation, to markedly higher levels, during formation of secondary (presumptive fast) fibers, and (3) differential augmentation of expression during early postnatal maturation of the IIB, IIX, IIA fast fiber types. These results provide insight into the roles of gene activation and gene repression mechanisms in fiber-type specificity and can account for apparently disparate results obtained in previous studies of TnI isoform expression in development. Each of the three IRE-driven developmental steps is spatiotemporally associated with a different major regulatory event at the fast myosin heavy chain gene cluster, suggesting that diverse muscle gene families respond to common, or tightly integrated, regulatory signals during multiple steps of muscle fiber differentiation.

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“…We then investigated whether LWA300 correlates with a myofiber type. A muscle is composed of different myofibers that can be distinguished by the expression of myosin heavy chain (MyHC) isotypes 34. We assessed whether LWA300 intensity is associated with myofiber type in sequential cryosections that were stained for LWA300 or with a mix of conjugated antibodies to MyHC type‐2b, type‐2a, and type‐1.…”

Section: Resultsmentioning

confidence: 99%

Proteasomal activity‐based probes mark protein homeostasis in muscles

Raz¹,

Raz²,

Soriano

et al. 2017

J cachexia sarcopenia muscle

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BackgroundProtein homeostasis, primarily regulated by the ubiquitin–proteasome system is crucial for proper function of cells. In tissues of post‐mitotic cells, the impaired ubiquitin–proteasome system is found in a wide range of neuromuscular disorders. Activity‐based probes (ABPs) measure proteasomal proteolytic subunits and can be used to report protein homeostasis. Despite the crucial role of the proteasome in neuromuscular pathologies, ABPs were not employed in muscle cells and tissues, and measurement of proteasomal activity was carried out in vitro using low‐throughput procedures.MethodsWe screened six ABPs for specific application in muscle cell culture using high throughput call‐based imaging procedures. We then determined an in situ proteasomal activity in myofibers of muscle cryosections.ResultsWe demonstrate that LWA300, a pan‐reactive proteasomal probe, is most suitable to report proteasomal activity in muscle cells using cell‐based bio‐imaging. We found that proteasomal activity is two‐fold and three‐fold enhanced in fused muscle cell culture compared with non‐fused cells. Moreover, we found that proteasomal activity can discriminate between muscles. Across muscles, a relative higher proteasomal activity was found in hybrid myofibers whereas fast‐twitch myofibers displayed lower activity.ConclusionsOur study demonstrates that proteasomal activity differ between muscles and between myofiber types. We suggest that ABPs can be used to report disease progression and treatment efficacy.

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Emergence of the mature myosin phenotype in the rat diaphragm muscle

Cited by 89 publications

References 33 publications

Combined myofibrillar and mitochondrial creatine kinase deficiency impairs mouse diaphragm isotonic function

Combined myofibrillar and mitochondrial creatine kinase deficiency impairs mouse diaphragm isotonic function

TnIfast IRE enhancer: Multistep developmental regulation during skeletal muscle fiber type differentiation

Proteasomal activity‐based probes mark protein homeostasis in muscles

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