The X-chromosome and the enzymes controlling muscle glycogen: Phosphorylase kinase

Lyon, John B.

doi:10.1007/bf00484028

Cited by 55 publications

(17 citation statements)

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“…RNA blot hybridization analysis demonstrates a predominant RNA species of -4500 nucleotides and a less abundant RNA of 8700 nucleotides. (19,21,22), and rats (23). Defects of the muscular and of the hepatic form of the enzyme and X chromosomal as well as autosomal transmission are observed.…”

Section: Introductionmentioning

confidence: 99%

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cDNA cloning and complete primary structure of skeletal muscle phosphorylase kinase (alpha subunit).

Zander

Meyer

Hoffmann-Posorske

et al. 1988

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

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We have isolated and sequenced a cDNA encoding the a subunit of phosphorylase kinase from rabbit fast-twitch skeletal muscle. The cDNA molecule consists of 388 nucleotides of 5'-nontranslated sequence, the complete coding sequence of 3711 nucleotides, and 342 nucleotides of 3'-nontranslated sequence followed by a poly(dA) tract. It encodes a polypeptide of 1237 amino acids and a deduced molecular mass of 138,422 Da. Nearly half of the deduced amino acid sequence is confirmed by peptide sequencing. Seven positions of endogenously phosphorylated serine residues and autophosphorylation sites, identified by peptide sequencing, could be assigned. They cluster in a segment of only 60 amino acids. RNA blot hybridization analysis demonstrates a predominant RNA species of -4500 nucleotides and a less abundant RNA of 8700 nucleotides. (19,21,22), and rats (23). Defects of the muscular and of the hepatic form of the enzyme and X chromosomal as well as autosomal transmission are observed. The isolation of DNA sequences encoding the subunits of phosphorylase kinase would make it possible to characterize the molecular nature of these deficiencies and may improve clinical diagnosis and genetic counseling.To these ends, we have determined large parts of the peptide sequence of the a subunit of phosphorylase kinase from rabbit fast-twitch skeletal muscle. We have used these sequences to design oligonucleotide probes and to isolate and identify cDNA molecules encoding this subunit. Here, we present the nucleotide sequence of a nearly complete mRNA copy, and the complete primary structure of the a subunitA Phosphorylase kinase (ATP:phosphorylase-b phosphotransferase, EC 2.7.1.38) was the first regulatory protein kinase to be discovered (1) and the starting point for revealing, during the last three decades, reversible protein phosphorylation as an important control mechanism in eukaryotic cells. It is a large oligomeric enzyme (1.3 MDa) with the subunit structure (afOyS)4. In linking glycogen breakdown to both nervous and endocrine stimulation, the enzyme is regulated in a complex way by phosphorylation of various serine residues and by calcium (2-4). The subunit 8 is identical to calmodulin and confers Ca2+ sensitivity to the enzyme (5). The subunit y carries catalytic activity (6) and is similar to other known protein kinases (7). The primary structures of these subunits have been determined, and cDNAs encoding the subunit y have been cloned (8-10). The two large subunits, a and X3, comprise 80%o of the total protein. They carry all phosphorylation sites; furthermore, they have been implicated in catalytic function (4, 11) as well as binding of nucleotides (11, 12), calmodulin (13), and troponin (14). Only small partial amino acid sequences have been published from a and ,8. To provide a structural basis for the wealth of enzymological data that has been accumulated and to correlate the various functional properties to structural features, it is necessary to determine the primary structures of these subunits.There are c...

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Section: Introductionmentioning

confidence: 99%

“…20), mice (19,21,22), and rats (23). Defects of the muscular and of the hepatic form of the enzyme and X chromosomal as well as autosomal transmission are observed.…”

mentioning

confidence: 99%

cDNA cloning and complete primary structure of skeletal muscle phosphorylase kinase (alpha subunit).

Zander

Meyer

Hoffmann-Posorske

et al. 1988

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

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“…29, 113-115 (1973)]. New-born mice of this strain were also reported (Lyon, 1970) to reveal a small amount of skeletal muscle enzyme activity.…”

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confidence: 94%

Phosphorylase Kinase Isoenzymes in Deficient ICR/IAn Mice

Daegelen-Proux¹,

Alexandre²,

Dreyfus³

1978

European Journal of Biochemistry

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ICR/IAn mice present a deficiency in phosphorylase kinase activity; the extent of this deficiency is less in some tissues (Lyon, S. B. Biochem. Genet. 4, 169–185 (1970)] than in skeletal muscle, where enzyme activity is 0.3% of normal [Cohen, P. T. W. & Cohen, P. FEBS Lett. 29, 113–115 (1973)]. New‐born mice of this strain were also reported (Lyon, 1970) to reveal a small amount of skeletal muscle enzyme activity. The properties of these residual phosphorylase kinases were compared to those of control C57BL mice, with reference to control muscle and liver enzymes which were shown to be of different molecular species [Daegelen‐Proux et al. Biochim. Biophys. Acta, 452, 398–405 (1976)]. The properties investigated were the immunological reactivity against an antiserum raised against muscle phosphorylase kinase, the thermal stability and the Ca2+ dependency. The results suggest that the muscle enzyme from the new‐born ICR/IAn mice and the heart enzyme from adult deficient mice are different to the muscle enzyme from adult normal mice, but they have properties in common with normal adult liver enzyme. These results lead to the conclusion that there exists in the muscle of I strain a ‘foetal form’ of phosphorylase kinase, the activity of which decreases progressively after birth. Our work also confirmed the observations made by Cohen et al. [Eur. J. Biochem. 66, 347–356 (1976)] which showed that there is no evidence for the existence of a cross‐reacting material in the muscle of adult deficient mice.

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“…Lyon reported that phosphorylase kinase is completely absent from skeletal muscle of deficient mice. Brain, heart and kidney are affected to a lesser extent than skeletal muscle, showing approximately 9, 20 and 66% respectively of the activity found in normal control tissue [4]. Deficient mice show a normal activity of phosphorylase kinase in intestine [4] and liver [6] .…”

Section: Introductionmentioning

confidence: 99%

“…to a defect in a gene coding for the localization of the enzyme, as is known for glucuronidase [9] . In this respect it is of interest that heterozygous female mice do not differ significantly from normal with respect to the activity of phosphorylase kinase in a 5,000 g supernatant [4,5] . Table 5 shows that the kinase activity of homogenates assayed at pH 6.8 or 8.2 does not differ significantly from normal values nor does the percentage of the enzyme remaining in the supernatant after centrifugation at 13,000 g for 10 min.…”

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confidence: 99%

Phosphorylase kinase deficiency in mice

Huijing

1970

FEBS Letters

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The X-chromosome and the enzymes controlling muscle glycogen: Phosphorylase kinase

Cited by 55 publications

References 15 publications

cDNA cloning and complete primary structure of skeletal muscle phosphorylase kinase (alpha subunit).

cDNA cloning and complete primary structure of skeletal muscle phosphorylase kinase (alpha subunit).

Phosphorylase Kinase Isoenzymes in Deficient ICR/IAn Mice

Phosphorylase kinase deficiency in mice

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