Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle

Roman, Brian B.; Wieringa, Bé; Koretsky, Alan P.

doi:10.1074/jbc.272.28.17790

Cited by 28 publications

(19 citation statements)

References 46 publications

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“…Multiple isoforms of CK are thought to constitute an intricate transport and energy buffering system, which connects highenergy phosphate production to sites of energy consumption [22,23]. As such CK is involved intimately in the maintenance of cellular energy homeostasis.…”

Section: Ck Isoform Mappingmentioning

confidence: 99%

Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle

et al. 2007

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The common carp (Cyprinus carpio) has a well-developed capacity to modify muscle properties in response to changes in temperature. Understanding the mechanisms underpinning this phenotypic response at the protein level may provide fundamental insights into the molecular basis of adaptive processes in skeletal muscle. In this study, common carp were subjected to a cooling regimen and soluble extracts of muscle homogenates were separated by 1-D SDS-PAGE and 2-DE. Proteins were identified using MALDI-TOF-MS and de novo peptide sequencing using LC-MS/MS. The 2-D gel was populated with numerous protein spots that were fragments of all three muscle isoforms (M1, M2 and M3) of carp creatine kinase (CK). The accumulation of the CK fragments was enhanced when the carp were cooled to 107C. The protein changes observed in the skeletal muscle of carp subjected to cold acclimation were compared to changes described in a previous transcript analysis study. Genes encoding CK isoforms were downregulated and the genes encoding key proteins of the ubiquitin-proteasome pathway were upregulated. These findings are consistent with a specific cold-induced enhancement of proteolysis of CK.

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Section: Ck Isoform Mappingmentioning

confidence: 99%

Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle

et al. 2007

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“…A portion of total muscle CK becomes localized to the M-line in the early postnatal period (Carlsson et al, 1982), supporting renewal of ATP immediately at the site of energy utilization by myofibrillar ATPase. Striated muscle also expresses sarcomeric mitochondrial CK (sCK), localized to the mitochondria, and there is compelling evidence that CK isoforms can, at least in part, functionally compensate for one another (Roman et al, 1997). CK isoform heterogeneity is, however, tightly coupled to the organization of energy production and utilization pathways and thus may be tailored to the operational mode of a given muscle type (VenturaClapier et al, 1998).…”

mentioning

confidence: 99%

Postnatal suppression of myomesin, muscle creatine kinase and the M-line in rat extraocular muscle

Porter

Merriam

Gong

et al. 2003

Journal of Experimental Biology

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SUMMARYThe M-line and its associated creatine kinase (CK) M-isoform (CK-M) are ubiquitous features of skeletal and cardiac muscle. The M-line maintains myosin myofilaments in register, links the contractile apparatus to the cytoskeleton for external force transfer and localizes CK-based energy storage and transfer to the site of highest ATP demand. We establish here that the muscle group responsible for movements of the eye, extraocular muscle (EOM),is divergent from other striated muscles in lacking both an M-line and its associated CK-M. Although an M-line forms during myogenesis, both in vivo and in vitro, it is actively repressed after birth. Transcripts of the major M-line structural proteins, myomesin 1 and myomesin 2, follow the same pattern of postnatal downregulation, while the embryonic heart-specific EH-myomesin 1 transcript is expressed early and retained in adult eye muscle. By immunocytochemistry, myomesin protein is absent from adult EOM sarcomeres. M-line suppression does not occur in organotypic co-culture with oculomotor motoneurons, suggesting that the mechanism for suppression may lie in muscle group-specific activation or workload patterns experienced only in vivo. The M-line is, however, still lost in dark-reared rats, despite the developmental delay this paradigm produces in the visuomotor system and EOMs. EOM was low in all CK isoform transcripts except for the sarcomeric mitochondrial (Ckmt2) isoform. Total CK enzyme activity of EOM was one-third that of hindlimb muscle. These findings are singularly unique among fast-twitch skeletal muscles. Since EOM exhibits isoform diversity for other sarcomeric proteins, the M-line/CK-M divergence probably represents a key physiological adaptation for the unique energetics and functional demands placed on this muscle group in voluntary and reflexive eye movements.

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“…We injected an adenoviral vector carrying the mouse gene for the brain CK isozyme (CK-B) into the tail veins of mice and were able to detect in vivo a PCr peak in the surgically exposed livers by 31 P MRS. Our study demonstrates that CK can be used as a marker for in vivo, potentially noninvasive, monitoring of gene expression in liver. It may also be suitable as a marker gene even in tissues that normally express this enzyme, because the increment in CK activity can be determined by magnetization-transfer experiments, as recently demonstrated by Roman et al (29) in mouse skeletal muscle. In summary, the key advantages of CK as a marker gene are absence of immune reaction, compatibility with magnetic resonance equipment that is readily available in the laboratory and the clinic, absence of radioactivity, and apparent absence of harmful side effects.…”

Section: Mrsmentioning

confidence: 88%

“…Therefore, quantitation of transduction requires measurement of CK activity. This can be accomplished noninvasively by a magnetization-transfer experiment that measures the rate of reaction 1 in the PCr to ATP direction (24,29). This flux should be proportional to V max , which in turn should be proportional to the concentration of CK.…”

Section: Discussionmentioning

confidence: 99%

“…Localized MRS or spectroscopic imaging allows noninvasive mapping of the distribution of metabolites and quantitative measurement of enzymatic activity by magnetization-transfer experiments (24,29). Ideally, an MRS reporter system should provide a unique resonance in the spectrum of the target tissue to eliminate the need for discrimination from background signals emanating from endogenous genes; it should employ a syngeneic marker protein to evade immunological responses; the reporter gene should be small enough to fit in the same expression vector as the therapeutic gene; and its enzymatic activity should not interfere with the function of the target tissue.…”

Section: Mrsmentioning

confidence: 99%

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In vivo detection of gene expression in liver by ³¹ P nuclear magnetic resonance spectroscopy employing creatine kinase as a marker gene

Auricchio

Zhou

Wilson

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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In vivo assessment of gene expression is desirable to obtain information on the extent and duration of transduction of tissue after gene delivery. We have developed an in vivo, potentially noninvasive, method for detecting virally mediated gene transfer to the liver. The method employs an adenoviral vector carrying the gene for the brain isozyme of murine creatine kinase (CK-B), an ATP-buffering enzyme expressed mainly in muscle and brain but absent from liver, kidney, and pancreas. Gene expression was monitored by 31 P magnetic resonance spectroscopy (MRS) using the product of the CK enzymatic reaction, phosphocreatine, as an indicator of transfection. The vector was administered into nude mice by tail vein injection, and exogenous creatine was administered in the drinking water and by i.p. injection of 2% creatine solution before 31 P MRS examination, which was performed on surgically exposed livers. A phosphocreatine resonance was detected in livers of mice injected with the vector and was absent from livers of control animals. CK expression was confirmed in the injected animals by Western blot analysis, enzymatic assays, and immunofluorescence measurements. We conclude that the syngeneic enzyme CK can be used as a marker gene for in vivo monitoring of gene expression after virally mediated gene transfer to the liver.

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Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle

Cited by 28 publications

References 46 publications

Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle

Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle

Postnatal suppression of myomesin, muscle creatine kinase and the M-line in rat extraocular muscle

In vivo detection of gene expression in liver by ³¹ P nuclear magnetic resonance spectroscopy employing creatine kinase as a marker gene

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Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle

Cited by 28 publications

References 46 publications

Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle

Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle

Postnatal suppression of myomesin, muscle creatine kinase and the M-line in rat extraocular muscle

In vivo detection of gene expression in liver by 31 P nuclear magnetic resonance spectroscopy employing creatine kinase as a marker gene

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In vivo detection of gene expression in liver by ³¹ P nuclear magnetic resonance spectroscopy employing creatine kinase as a marker gene