Electrostimulation‐induced increases in fatty acid‐binding protein and myoglobin in rat fast‐twitch muscle and comparison with tissue levels in heart

Kaufmann, M.; Simoneau, J. A.; Veerkamp, J.H.; Pette, Dirk

doi:10.1016/0014-5793(89)80217-0

Cited by 56 publications

(23 citation statements)

References 15 publications

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“…A chronic increase in contractile activity and a shift to oxidative muscle metabolism would require a higher demand in oxygen and fuel supply in the form of fatty acids. Consequently the drastic increase in the oxygen-transporter myoglobin, the intracellular fatty acid binding protein FABP-3 and the extracellular fatty acid transporter albumin strongly indicates that these three central metabolic regulators could function as limiting factors of oxidative metabolism in fast fibres [40,63]. The findings from our DIGE analysis clearly establish the small cytosolic FABP-3 protein as a suitable biomarker of muscle fibre type shifting.…”

Section: Discussionmentioning

confidence: 66%

“…An elevation of aerobic-oxidative capacity, decreased fibre calibre and changes in the density of distinct muscle proteins, switches in isoform expression patterns and alterations in proteinprotein interactions are established biochemical and cell biological hallmarks of transformed skeletal muscles. This includes: (i) metabolic pathways such as the citric acid cycle, fatty acid oxidation and the respiratory chain which causes a drastic increase in enzymes of aerobic substrate oxidation [39,40], (ii) the contractile apparatus that undergoes a stepwise replacement of myosin light and heavy chains from fast isoforms to their slower counterparts [41,42], (iii) the ion-regulatory machinery of the excitation-contractionrelaxation cycle with a shift from fast to slower isoforms with respect to the SERCA-type Ca 21 -ATPases, the voltagesensing dihydropyridine receptor, the ryanodine receptor Ca 21 -release channel and various Ca 21 -binding proteins [43,44], (iv) the neuromuscular junction with distinct changes in the acetylcholinesterase and the nicotinic acetylcholine receptor [45,46] and, (v) a decrease in the supramolecular interaction pattern between Ca…”

Section: Introductionmentioning

confidence: 99%

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Proteomic profiling of chronic low‐frequency stimulated fast muscle

et al. 2007

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Skeletal muscle fibre transitions occur in many biological processes, in response to alterations in neuromuscular activity, in muscular disorders, during age-induced muscle wasting and in myogenesis. It was therefore of interest to perform a comprehensive proteomic profiling of muscle transformation. Chronic low-frequency stimulation of the rabbit tibialis anterior muscle represents an established model system for studying the response of fast fibres to enhanced neuromuscular activity under conditions of maximum activation. We have conducted a DIGE analysis of unstimulated control specimens versus 14-and 60-day conditioned muscles. A differential expression pattern was observed for 41 protein species with 29 increased and 12 decreased muscle proteins. Identified classes of proteins that are changed during the fast-to-slow transition process belong to the contractile machinery, ion homeostasis, excitation-contraction coupling, capillarization, metabolism and stress response. Results from immunoblotting agreed with the conversion of the metabolic, regulatory and contractile molecular apparatus to support muscle fibres with slower twitch characteristics. Besides confirming established muscle elements as reliable transition markers, this proteomics-based study has established the actin-binding protein cofilin-2 and the endothelial marker transgelin as novel biomarkers for evaluating muscle transformation.

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Section: Discussionmentioning

confidence: 66%

Section: Introductionmentioning

confidence: 99%

Proteomic profiling of chronic low‐frequency stimulated fast muscle

et al. 2007

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“…That a metabolic switch takes place in senescent muscles is supported by the finding that the fatty acid-binding protein FABP and the oxygen carrier myoglobin are increased during aging . Both proteins have previously been established as limiting factors of aerobic-oxidative metabolism in slow-twitching fibres (Kaufmann et al, 1989). Thus, both changes in contractile kinetics and metabolic adaptations suggest an age-related switch to a slower muscle type.…”

Section: Discussionmentioning

confidence: 93%

Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age

Gannon

Doran

Kirwan

et al. 2009

European Journal of Cell Biology

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The age-dependent decline in skeletal muscle mass and function is believed to be due to a multi-factorial pathology and represents a major factor that blocks healthy aging by increasing physical disability, frailty and loss of independence in the elderly. This study has focused on the comparative proteomic analysis of contractile elements and revealed that the most striking age-related changes seem to occur in the protein family representing myosin light chains (MLCs). Comparative screening of total muscle extracts suggests a fast-to-slow transition in the aged MLC population. The mass spectrometric analysis of the myofibril-enriched fraction identified the MLC2 isoform of the slow-type MLC as the contractile protein with the most drastically changed expression during aging. Immunoblotting confirmed an increased abundance of slow MLC2, concomitant with a switch in fast versus slow myosin heavy chains. Staining of two-dimensional gels of crude extracts with the phospho-specific fluorescent dye ProQ-Diamond identified the increased MLC2 spot as a muscle protein with a drastically enhanced phosphorylation level in aged fibres. Comparative immunofluorescence microscopy, using antibodies to fast and slow myosin isoforms, confirmed a fast-to-slow transformation process during muscle aging. Interestingly, the dramatic increase in slow MLC2 expression was restricted to individual senescent fibres. These findings agree with the idea that aged skeletal muscles undergo a shift to more aerobic-oxidative metabolism in a slower-twitching fibre population and suggest the slow MLC2 isoform as a potential biomarker for fibre type shifting in sarcopenia of old age.

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“…Representative examples of stimulation-induced changes in major muscle proteins is the stepwise replacement of myosin heavy chains from the MHCII isoforms to MHCI [14], a shift from the fast SERCA1 isoform of the sarcoplasmic reticulum Ca 2+ -ATPases to the slower SERCA2 isoform [15], the increase in the levels of the a-and ysubunits of the nicotinic acetylcholine receptor [12] and the gradual increase in the activity of enzymes involved in the main metabolic systems of aerobic substrate oxidation, i.e., the citric acid cycle, fatty acid oxidation and the respiratory chain [11,16,17]. The recent blot overlay analysis of the sarcoplasmic reticulum Ca 2+ -binding protein calsequestrin, using a peroxidase conjugate probe, revealed that the fast-toslow transition process triggers a distinct reduction in fast calsequestrin and a concomitant alteration in calsequestrin interactions with the ryanodine receptor Ca 2+ -release channel [13].…”

Section: Introductionmentioning

confidence: 99%

Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

Donoghue

Doran

Dowling

et al. 2005

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Physiological and biochemical responses of skeletal muscle fibres to enhanced neuromuscular activity under conditions of maximum activation can be studied experimentally by chronic low-frequency stimulation of fast muscles. Stimulation-induced changes in the expression pattern of the rabbit fast skeletal muscle proteome were evaluated by two-dimensional gel electrophoresis and compared to the altered isoform expression profile of established transformation markers such as the Ca 2+ -ATPase, calsequestrin and the myosin heavy chain. Sixteen muscle proteins exhibited a marked change in their expression level. This included albumin with a 4-fold increase in abundance. In contrast, glycolytic enzymes, such as enolase and aldolase, showed a decreased expression. Concomitant changes were observed with marker elements of the contractile apparatus. While the fast isoforms of troponin T and myosin light chain 2 were drastically down-regulated, their slow counterparts exhibited increased expression. Interestingly, mitochondrial creatine kinase expression increased while the cytosolic isoform of this key muscle enzyme decreased. The expression of the small heat shock protein HSP-B5/aB-crystallin and the oxygen carrier protein myoglobin were both increased 2-fold following stimulation. The observed changes indicate that the conversion into fatigue-resistant red fibres depends on: (i) the optimum utilization of free fatty acids via albumin transportation, (ii) a rearrangement of the creatine kinase isozyme pattern for enhanced mitochondrial activity, (iii) an increased availability of oxygen for aerobic metabolism via myoglobin transport, (iv) the conversion of the contractile apparatus to isoforms with slower twitch characteristics and (v) the up-regulation of chaperone-like proteins for stabilising myofibrillar components during the fast-to-slow transition process. D

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Electrostimulation‐induced increases in fatty acid‐binding protein and myoglobin in rat fast‐twitch muscle and comparison with tissue levels in heart

Cited by 56 publications

References 15 publications

Proteomic profiling of chronic low‐frequency stimulated fast muscle

Proteomic profiling of chronic low‐frequency stimulated fast muscle

Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age

Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

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