Physicochemical studies on the creatine kinase M-line protein and its interaction with myosin and myosin fragments

Mani, Rajam S.; Kay, Cyril M.

doi:10.1016/0005-2795(76)90134-3

Cited by 35 publications

(10 citation statements)

References 17 publications

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“…Similarly, creatine kinase did not interact with the F-actin-tropomyosin. This enzyme constitutes part of the M-line protein in muscle and interacts with myosin (Wallimann et al, 1978: Mani andKay, 1976) and would not be expected to interact with actin or tropomyosin.…”

Section: Resultsmentioning

confidence: 99%

Interaction of Selected Brain Glycolytic Enzymes with an F‐Actin‐Tropomyosin Complex

Knull

Bronstein

Desjardins

et al. 1980

Journal of Neurochemistry

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Section: Resultsmentioning

confidence: 99%

Interaction of Selected Brain Glycolytic Enzymes with an F‐Actin‐Tropomyosin Complex

Knull

Bronstein

Desjardins

et al. 1980

Journal of Neurochemistry

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“…The mitochondrial CK isoforms, by virtue of their mitochondrial targeting sequences, are bound to the outer surface of the inner membrane, where they are coupled to the adenine nucleotide translocator in the transfer of energy equivalents into the cytoplasm. The muscle isoform, MCK, is bound to the myofibril (Ottaway, 1967;Turner et al, 1973;Mani and Kay, 1976;Walliman et al, 19771, where it serves to regenerate energy for muscle contraction. Our previous data on the localization of BCK in excretory tissues suggested that the isoform-specific function of BCK may be to provide energy for sodium transport in excretory tissues (Friedman and Perryman, 1991;Friedman and Roberts, Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The creatine phosphate produced from oxidative metabolism is then used to regenerate ATP from ADP at specific sites within cells by a different isoform of CK. In striated muscle, for example, the muscle-type (MCK) isoform is bound to the M-line of the myofibril (Turner et al, 1973;Mani and Kay, 1976;Walliman et al, 1977), for the regeneration of ATP from ADP produced during muscle contraction (Krause and Jacobus, 1992).…”

mentioning

confidence: 99%

Compartment of brain‐type cretine kinase and ubiquitous mitochondrial cretine kinase in neurons: Evidence for a cretine phosphate energy shuttle in adult rat brain

Friedman

Roberts

1994

J of Comparative Neurology

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Multiple isoforms of creatine kinase (CK) are expressed in specific cell types as part of an energy delivery or shuttle system. To test the hypothesis that neurons utilize a creatine phosphate energy shuttle, we examined the pattern of CK isoform expression and localization in adult rat brain. Two isoforms of CK are present in brain extracts, "brain-type," or BCK, and the ubiquitous form of the mitochondrial CK (uMtCK), as detected by enzyme activity following nondenaturing electrophoresis and by Western blotting following denaturing electrophoresis. In formalin-fixed and paraffin-embedded sections of rat brain, uMtCK immunostaining is detected in the somata of all Golgi type I neurons in the cerebellum, pontine reticular formation, red nucleus, hippocampus, and cerebral cortex. Immunostaining for uMtCK appears throughout the cell body but not in nuclei. BCK immunostaining is also present in somata of Golgi type I neurons in the cerebellum, red nucleus, and pons and is distributed throughout the cell body and within nuclei. BCK immunostaining also appears in neuronal processes and is concentrated in the molecular layers of the cerebellum and the hippocampus and in cortical pyramidal cell dendrites. These results demonstrate a coordinate pattern of expression and compartmentation of BCK and uMtCK isoforms in neurons, which provides an anatomic basis for the transfer of metabolic energy via a creatine phosphate energy shuttle.

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“…The interactions of creatine kinase and arginine kinase with myosin as well as the preferential localization of the binding sites of these two enzymes (Mani & Kay, 1976 …”

Section: Discussionmentioning

confidence: 99%

Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments

Méjean

Pons

Benyamin

et al. 1989

Biochemical Journal

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The topology of the interfaces between actin monomers in microfilaments and three glycolytic enzymes (glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase) was investigated using several specific antibodies directed against precisely located sequences in actin. A major contact area for glyceraldehyde-3-phosphate dehydrogenase was characterized in a region near residue 103. This interaction altered, by long-range conformational changes, the reactivity of antigenic epitopes in the C-terminal part of actin. The interface between actin and aldolase appeared to involve a sequence around residue 299 in the C-terminal region of actin. The interaction of phosphofructokinase, in contrast, modified the reactivity of all antibodies tested. Finally, the phosphagen kinases arginine kinase and creatine kinase showed no interaction with the microfilament.

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Physicochemical studies on the creatine kinase M-line protein and its interaction with myosin and myosin fragments

Cited by 35 publications

References 17 publications

Interaction of Selected Brain Glycolytic Enzymes with an F‐Actin‐Tropomyosin Complex

Interaction of Selected Brain Glycolytic Enzymes with an F‐Actin‐Tropomyosin Complex

Compartment of brain‐type cretine kinase and ubiquitous mitochondrial cretine kinase in neurons: Evidence for a cretine phosphate energy shuttle in adult rat brain

Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments

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