Calcyclin—Ca2+-binding protein homologous to glial S-100β is present in neurones

Filipek, Anna; Puzianowska, Monika; Cieślak, Beata; Kuźnicki, Jacek

doi:10.1097/00001756-199304000-00010

Cited by 50 publications

(27 citation statements)

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“…Nonetheless, for both genes a significant frequency of tumour-specific methylation was observed in primary tumours, which was associated with transcriptional silencing in medulloblastoma cell lines, indicating epigenetic inactivation and candidate tumour suppressor roles for S100A6 and S100A10 in primary medulloblastoma development. S100A6 has been shown to be expressed in a cell type-specific manner in the brain, with expression present in subsets of neurons including granule cells of the cerebellum (Filipek et al, 1993). Consistent with this observation, the S100A6 promoter was unmethylated in the normal cerebellum in the present study.…”

Section: Discussionsupporting

confidence: 89%

Epigenetic deregulation of multiple S100 gene family members by differential hypomethylation and hypermethylation events in medulloblastoma

et al. 2007

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Deregulated expression of genes encoding members of the S100 family of calcium-binding proteins has been associated with the malignant progression of multiple tumour types. Using a pharmacological expression reactivation approach, we screened 16 S100 genes for evidence of epigenetic regulation in medulloblastoma, the most common malignant brain tumour of childhood. Four family members (S100A2, S100A4, S100A6 and S100A10) demonstrated evidence of upregulated expression in multiple medulloblastoma cell lines, following treatment with the DNA methyltransferase inhibitor, 5 0 -aza-2 0 -deoxycytidine. Subsequent analysis revealed methylation of critical CpG sites located within these four genes in an extended cell line panel. Assessment of these genes in the nonneoplastic cerebellum (from which medulloblastomas develop) revealed strong somatic methylation affecting S100A2 and S100A4, whereas S100A6 and S100A10 were unmethylated. Assessed against these normal tissue-specific methylation states, S100A6 and S100A10 demonstrated tumour-specific hypermethylation in medulloblastoma primary tumours (5 out of 40 and 4 out of 35, respectively, both 12%) and cell lines (both 7 out of 9, 78%), which was associated with their transcriptional silencing. Moreover, S100A6 hypermethylation was significantly associated with the aggressive large cell/anaplastic morphophenotype (P ¼ 0.026). In contrast, pro-metastatic S100A4 displayed evidence of hypomethylation relative to the normal cerebellum in a significant proportion primary tumours (7 out of 41, 17%) and cell lines (3 out of 9, 33%), which was associated with its elevated expression. In summary, these data characterise complex patterns of somatic methylation affecting S100 genes in the normal cerebellum and demonstrate their disruption causing epigenetic deregulation of multiple S100 family members in medulloblastoma development. Epigenetic events affecting S100 genes have potential clinical utility and merit further investigation as molecular biomarkers for this disease.

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Section: Discussionsupporting

confidence: 89%

Epigenetic deregulation of multiple S100 gene family members by differential hypomethylation and hypermethylation events in medulloblastoma

et al. 2007

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“…The presence of CacyBP mRNA in some mouse tissues established by northern hybridization is in agreement with the localization of CacyBP reported earlier using the gel overlay method . The CacyBP localization also matches the calcyclin distribution (Ku~nicki et al, 1989b;Filipek et al, 1993). As both proteins are present in the brain and the interaction between them is strong and calcium-dependent, we believe that they might be involved in calcium signaling pathways in the neuronal tissue.…”

Section: Discussionsupporting

confidence: 67%

“…The level of calcyclin mRNA was also increased in PC12 cells that were activated by nerve growth factor (Leonard et al, 1987;Thompson and Ziff, 1989), in neuroblastoma cell lines activated by retinoic acid (Tonini et al, 1991), and in some human cell lines after transformation (Guo et al, 1990;Chambers and Tuck, 1993). It was later established that calcyclin is expressed preferentially in fibroblasts, epithelial cells, and some neurons (Ku~-nicki et al, 1992;Filipek et al, 1993;Timmons et al, 1993) and that no direct correlation exists between the cell cycle progression and calcyclin distribution. It has been suggested that calcyclin expression might be related to a high secretory activity (Celis et al, 1990;Thordarson et al, 1991;Ku~nickiet al, 1992;Timmons et al, 1993;Wo~niewicz et al, 1993;Kordowska et al, 1994;Okazaki et al, 1994).…”

mentioning

confidence: 99%

Molecular Cloning and Expression of a Mouse Brain cDNA Encoding a Novel Protein Target of Calcyclin

Filipek

Kuźnicki

1998

Journal of Neurochemistry

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A protein target of mouse calcyclin, p30, which we call calcyclin-binding protein (CacyBP), was identified in mouse brain and Ehrlich ascites tumor (EAT) cells. The amino acid sequence of the CacyBP chymotryptic peptide was used to prepare synthetic oligonucleotides that served as a probe to screen the mouse brain cDNA library. A 1.4-kb positive clone was detected, isolated, and sequenced. The analyzed clone contains an open reading frame encoding a protein of a molecular mass of~-~26 kDa. The nucleotide and predicted amino acid sequences indicate that CacyBP is a novel protein. The results obtained from northern blots show that the CacyBP gene is expressed predominantly in mouse brain and EAT cells. Using a pGEX vector the recombinant CacyBP was expressed in Escherichia co/i, and its properties were analyzed. The recombinant protein interacts with calcyclin at a physiologically relevant range of Ca 2ĩ n solution during affinity chromatography and on blots. Because CacyBP, like calcyclin, is present in the brain, the interaction of these two proteins might be involved in calcium signaling pathways in neuronal tissue.

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“…However, in other cells or tissues the amount of each protein is significantly different. For instance, we showed that in the brain S100A6 is expressed at a very low level (25,26), but CacyBP/SIP is expressed at a very high level (20,23). Therefore, in the present work we looked for other S100-like protein ligands of CacyBP/ SIP in the brain.…”

Section: Identification Of S100b As a Cacybp/sip Ligand In Thementioning

confidence: 88%

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

Filipek¹,

Jastrzębska²,

Nowotny³

et al. 2002

Journal of Biological Chemistry

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135

107

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Recently, a human ortholog of mouse calcyclin (S100A6)-binding protein (CacyBP) called SIP (Siah-1-interacting protein) was shown to be a component of a novel ubiquitinylation pathway regulating ␤-catenin degradation (Matsuzawa, S., and Reed, J. C. (2001) Mol. Cell 7, 915-926). In murine brain, CacyBP/SIP is expressed at a high level, but S100A6 is expressed at a very low level. Consequently we carried out experiments to determine if CacyBP/SIP binds to other S100 proteins in this tissue. Using CacyBP/SIP affinity chromatography, we found that S100B from the brain extract binds to CacyBP/SIP in a Ca 2؉ -dependent manner. Using a nitrocellulose overlay assay with 125 I-CacyBP/SIP and CacyBP/SIP affinity chromatography, we found that this protein binds purified S100A1, S100A6, S100A12, S100B, and S100P but not S100A4, calbindin D 9k , parvalbumin, and calmodulin.

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Calcyclin—Ca2+-binding protein homologous to glial S-100β is present in neurones

Cited by 50 publications

References 0 publications

Epigenetic deregulation of multiple S100 gene family members by differential hypomethylation and hypermethylation events in medulloblastoma

Epigenetic deregulation of multiple S100 gene family members by differential hypomethylation and hypermethylation events in medulloblastoma

Molecular Cloning and Expression of a Mouse Brain cDNA Encoding a Novel Protein Target of Calcyclin

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

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