Structure and expression of the human creatine kinase B gene

Mariman, E.C.M.; Broers, Cees A.M.; Claesen, C. A. A.; Tesser, G. I.; Wieringa, Bé

doi:10.1016/0888-7543(87)90004-8

Cited by 38 publications

(24 citation statements)

References 42 publications

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“…Two cytosolic isoforms of creatine kinase, the brain (B) isoform and the muscle (M) isoform, which randomly associate to form three isozymes, MM, MB, and BB, have been described. Separate genes for the two cytosolic isoforms have been cloned from several species and appear to be the products of single-copy, unlinked genes (3,32,39,45,58). There is also a mitochondrial isoform that self-associates into octameric structures (47).…”

mentioning

confidence: 99%

Identification of cis-acting regulatory elements in the promoter region of the rat brain creatine kinase gene.

Hobson¹,

Molloy²,

Benfield³

1990

Mol. Cell. Biol.

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The functional organization of the rat brain creatine kinase (ckb) Initiation of transcription by RNA polymerase II is a major point at which regulation of gene expression occurs (15). The unique pattern of transcription characteristic of each gene is largely due to the interactions among all the various regulatory factors that bind the gene in its promoter and enhancer regions and to the further interaction of these factors with the transcriptional machinery. The transcriptional machinery is thus able to detect and integrate the regulatory information imposed on the gene.We have been studying transcriptional regulation of the creatine kinase genes. Creatine kinase (adenosine 5'-triphosphate-creatine phosphotransferase; EC 2.7.3.2) is an enzyme that catalyzes the reversible transfer of a phosphoryl group between ATP and creatine (for reviews, see references 35 and 59). Two cytosolic isoforms of creatine kinase, the brain (B) isoform and the muscle (M) isoform, which randomly associate to form three isozymes, MM, MB, and BB, have been described. Separate genes for the two cytosolic isoforms have been cloned from several species and appear to be the products of single-copy, unlinked genes (3,32,39,45,58). There is also a mitochondrial isoform that self-associates into octameric structures (47). A human mitochondrial gene has been isolated and characterized (25).The variety of modes of expression for the ck genes that must exist to accommodate the widely varying energy needs of cells make this gene family an interesting system in which to examine the molecular mechanisms involved in differential gene expression. The two cytosolic isoforms of creatine kinase, the muscle isoform and the brain isoform, have different tissue-specific patterns of expression (56). The muscle isoform is expressed predominantly in skeletal and cardiac muscle. The brain isoform, while being expressed at highest levels in brain, has a much broader range of expression than the muscle isoform has. Regulatory phenomena associated with brain isoform expression include up-regulation during differentiation of monocytes into macrophages * Corresponding author.(37), induction by peptide and steroid hormones (22 and references therein), high levels of expression in transformed cells (20), and stimulation by viral infection (11). Differential expression of the ckb gene in liver and brain (42) and up-regulation of the ckm gene during skeletal muscle differentiation (E. Arpaia and T. Smith, unpublished results; 32) have been shown to be regulated at least in part at the level of transcription.We previously reported evidence that a nonconsensus TTAA sequence at -28 bp appears to provide the principal TATA box function for the ckb promoter in vivo, even though there is a consensus TATAAATA sequence at -66 bp relative to the transcription start site (28). Under certain conditions in vitro, however, the upstream consensus TATA AATA sequence can function as a TATA box to mediate transcription from an upstream start site (28,42). In addition, we previously ...

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confidence: 99%

Identification of cis-acting regulatory elements in the promoter region of the rat brain creatine kinase gene.

Hobson¹,

Molloy²,

Benfield³

1990

Mol. Cell. Biol.

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“…GGATCC sequences (bold print) were included in the primers to bracket the segment between flanking Bam HI restriction sites. For PCR amplification, alkaline denatured [16] plasmid pCKB-131 DNA [17] served as template and standard conditions were used for genera tion and isolation o f the D N A product [18]. Next, the 1158 bp B am H I fragment (including primer sequences) was cloned downstream o f the polyhedrin promoter in the baculovirus transfer vector pA cD Z l which contains an E.…”

Section: Construction O F the Recom Binant Expression Vectormentioning

confidence: 99%

“…The peptide immunogen BW-17 (Ser-Asn-Ser-His-Asn-AlaLeu-Lys-Leu-Arg-Phe-Pro-Ala-Glu-Asp-Glu-Phe) corre sponding to a unique stretch o f amino acids (residues [4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] from the N-terminal end of the human B-CK was produced by standard solid phase synthesis [24], The purity of the peptide was assessed by determination of its amino acid com position and by routine HPLC analysis. Next, activated BW-17 peptide was coupled to BSA using MHS as described (25), yielding a ratio o f 16 moles of peptide per mole of BSA.…”

Section: Production O F a P Ep Tid E Immunogen And O F A Monoclonal Amentioning

confidence: 99%

Production of native creatine kinase B in insect cells using a baculovirus expression vector

et al. 1995

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A full-length human creatine kinase B (B-CK) cDNA was used to produce a recombinant baculovirus (AcDZl-BCK). Sf9 cells infected with this recombinant expressed a homodimeric protein composed o f 43 kDa subunits which, under optimal condi tions, formed up to 30% o f the total soluble cellular protein. Upon analysis by PAGE, zymogram assay and gel filtration chro matography the recombinant protein behaved like authentic dimeric human BB-CK protein. Studies with a newly produced monoclonal antibody (CK-BYK/21E10) directed against an epitope in the N-terminus o f the protein confirmed the identity o f the product. The recombinant BB-CK protein was purified to over 99% homogeneity from the total protein extract o f A cD Zl-CKB infected cells in one single step involving anion exchange column chromatography on MonoQ in FPLC. Dialysed pro tein had a specific activity o f 239 U/mg protein. (Mol Cell Biochem 143: 59-65, 1995)

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“…No reaction was observed when the cells were treated with sense probes (not shown). , 1997), and Drosophila melanogaster (AK_DROME, AAA68172), glycocyamine kinase from Nereis virens (GLYCAM_NEREIS, AAL26699) and human creatine kinase (CK_HUMAN, AAC31758; Mariman et al, 1987). Residues conserved (similar or related with respect to their physico-chemical properties) in all sequences are shown in white on black and those in at least three sequences in black on gray.…”

Section: In Situ Hybridization Analysesmentioning

confidence: 99%

“…The twodomain kinases identified in the Cnidarian Anthopleura japonica (Suzuki et al, 1997) and the mollusks (Bivalvia) Solen strictus (Suzuki et al, 2002), Corbicula japonica (Suzuki et al, 2002) and Ensis directus (Compaan and Ellington, 2003), were dissected into two parts and both parts were aligned in parallel with the mono-domain guanidino kinases from mollusks, oyster Crassostrea gigas and Solen strictus, crustaceans Homarus gammarus (KARG_HOMGA, 538542), Eriocheir sinensis and Artemia franciscana, and insects, Drosophila melanogaster and Schistocerca americana. In addition, glycocyamine kinase from the annelid Nereis virens, human creatine kinase (Mariman et al, 1987) and the holothurian enzyme from Stichopus japonicus were included in the alignment. The tree shows very strikingly that the duplication of the arginine kinases occurred in some mollusk species (e.g.…”

Section: Cloning Of the Cdna Encoding Arginine Kinase Frommentioning

confidence: 99%

Arginine kinase in the demosponge Suberites domuncula:regulation of its expression and catalytic activity by silicic acid

Perović-Ottstadt

Wiens

Schröder

et al. 2005

Journal of Experimental Biology

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SUMMARY In Demospongiae (phylum Porifera) the formation of the siliceous skeleton,composed of spicules, is an energetically expensive reaction. The present study demonstrates that primmorphs from the demosponge Suberites domuncula express the gene for arginine kinase after exposure to exogenous silicic acid. The deduced sponge arginine kinase sequence displays the two characteristic domains of the ATP:guanido phosphotransferases; it can be grouped to the `usual' mono-domain 40 kDa guanidino kinases (arginine kinases). Phylogenetic studies indicate that the metazoan guanidino kinases evolved from this ancestral sponge enzyme; among them are also the `unusual'two-domain 80 kDa guanidino kinases. The high expression level of the arginine kinase gene was already measurable 1 day after addition of silicic acid by northern blot, as well as by in situ hybridization analysis. Parallel determinations of enzyme activity confirmed that high levels of arginine kinase are present in primmorphs that had been exposed for 1-5 days to silicic acid. Finally, transmission electron-microscopical studies showed that primmorphs containing high levels of arginine kinase also produce siliceous spicules. These data highlight that silicic acid is an inorganic morphogenetic factor that induces the expression of the arginine kinase, which in turn probably catalyzes the reversible transfer of high-energy phosphoryl groups.

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Structure and expression of the human creatine kinase B gene

Cited by 38 publications

References 42 publications

Identification of cis-acting regulatory elements in the promoter region of the rat brain creatine kinase gene.

Identification of cis-acting regulatory elements in the promoter region of the rat brain creatine kinase gene.

Production of native creatine kinase B in insect cells using a baculovirus expression vector

Arginine kinase in the demosponge Suberites domuncula:regulation of its expression and catalytic activity by silicic acid

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