Purification and characterization of a novel calcium-binding protein, S100C, from porcine heart

Naka, Michiko; Qing, Zhao; Sasaki, Takahiro; Kise, Hideaki; Tawara, Isao; Hamaguchi, Satoshi; Tanaka, Toshio

doi:10.1016/0167-4889(94)90094-9

Cited by 59 publications

(44 citation statements)

References 23 publications

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“…In fact, the secondary structure of the annexin I and II N-terminal domains may play an important role in S100 protein binding (45). The p11 binding site on annexin II (amino acids [1][2][3][4][5][6][7][8][9][10][11][12][13][14] has been shown to form an amphipathic ␣-helix with the hydrophobic amino acids Val-3, Ile-6, Leu-7, and Leu-10, which lie on one face of the helix, representing the major contact sites for p11 (44,46). Additionally, the S100C binding site on annexin I (amino acids 2-18) is predicted to form a similar helix with Met-2, Val-3, Phe-6, and Leu-7 providing potential contacts for S100C (10).…”

Section: Discussionmentioning

confidence: 99%

“…The conserved core region is thought to be responsible for the annexin Ca 2ϩ and lipid binding properties (4). The sequences of the N-terminal domains of this family are highly variable, leading to the hypothesis that the differences in the N-terminal domains may contribute to the specific cellular function of each annexin (9,10,45,46).…”

mentioning

confidence: 99%

“…In fact, several members of the annexin family have been shown to bind members of the S100 subfamily of EF-hand proteins. Annexin I binds S100C (9,10,45), annexin II binds p11 (11), and annexin XI binds calcyclin (12) with each interaction characterized by the S100 protein binding to the N-terminal domain of the respective annexin. The annexin I-S100C and annexin XI-calcyclin interactions are Ca 2ϩ -dependent, while the annexin II-p11 interaction is Ca 2ϩ -independent.…”

mentioning

confidence: 99%

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Calcium-dependent Binding of Sorcin to the N-terminal Domain of Synexin (Annexin VII)

Brownawell

Creutz

1997

Journal of Biological Chemistry

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-dependent manner. Sorcin is able to inhibit synexin-mediated chromaffin granule aggregation in a manner saturable with increasing sorcin concentrations, but does not influence the Ca 2؉ sensitivity of synexin-mediated granule aggregation. Therefore, the interaction between sorcin and synexin may serve to regulate the functions of these proteins on membrane surfaces in a Ca 2؉ -dependent manner.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Calcium-dependent Binding of Sorcin to the N-terminal Domain of Synexin (Annexin VII)

Brownawell

Creutz

1997

Journal of Biological Chemistry

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“…1B) containing FGF-1, p40 Syn-1, and S100A13, exhibited a distinct retention time, yet immunoblot analysis of this major absorption peak demonstrated the presence of low levels of FGF-1 and p40 Syn-1 (data not shown). Since members of the S100 gene family are known to self-associate (21) and to associate with membrane phospholipids (22), it is possible that the major absorption peak in Fig. 1B may contain S100A13 aggregates as well as other peptidic and non-protein components such as acidic phospholipids.…”

Section: And B)mentioning

confidence: 99%

S100A13 Is Involved in the Regulation of Fibroblast Growth Factor-1 and p40 Synaptotagmin-1 Release in Vitro

Carreira

LaVallee²,

Tarantini

et al. 1998

Journal of Biological Chemistry

116

112

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We have previously characterized the release of the signal peptide sequence-less fibroblast growth factor (FGF) prototype, FGF-1, in vitro as a stress-induced pathway in which FGF-1 is released as a latent homodimer with the p40 extravesicular domain of p65 synaptotagmin (Syn)-1. To determine the biologic relevance of the FGF-1 release pathway in vivo, we sought to resolve and characterize from ovine brain a purified fraction that contained both FGF-1 and p40 Syn-1 and report that the brain-derived FGF-1:p40 Syn-1 aggregate is associated with the calcium-binding protein, S100A13. Since S100A13 binds the anti-inflammatory compound amlexanox and FGF-1 is involved in inflammation, we examined the effects of amlexanox on the release of FGF-1 and p40 Syn-1 in response to stress in vitro. We report that while amlexanox was able to repress the heat shock-induced release of FGF-1 and p40 Syn-1 in a concentration-dependent manner, it had no effect on the constitutive release of p40 Syn-1 from p40 Syn-1 NIH 3T3 cell transfectants. These data suggest the following: (i) FGF-1 is associated with Syn-1 and S100A13 in vivo; (ii) S100A13 may be involved in the regulation of FGF-1 and p40 Syn-1 release in response to temperature stress in vitro; and (iii) the FGF-1 release pathway may be accessible to pharmacologic regulation.

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“…Immunoblotting was performed using an antibody raised against purified S100C, and monoclonal anti-HIF-1a antibody (Novus Biochemical) as described previously. 24 Amino-Acid Analysis Lung tissues were homogenized in distilled water, deproteinized with 20% sulfosalicylic acid and centrifuged to remove cellular debris. Samples were mixed with ninhydrin and analyzed by HPLC.…”

Section: Fdd and Real-time Rt-pcr Assaymentioning

confidence: 99%

Target validation in hypoxia-induced vascular remodeling using transcriptome/metabolome analysis

et al. 2003

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The present study describes combined transcriptome and metabolome analysis for therapeutic target validation in hypoxia-induced vascular remodeling. Exposure to hypoxic conditions resulted in the upregulation of S100C mRNA and increased taurine (2-aminoethanesulfonic acid) content in the rat lung, as demonstrated by differential display and amino-acid content analysis. Hypoxia resulted in transcriptional activation of the S100C promoter through hypoxia-inducible factor-1 (HIF-1). Taurine suppressed HIF-1-mediated increases in S100C transcription. Moreover, oral taurine administration attenuated vascular remodeling in hypoxic rat lung, whereas depletion of endogenous taurine by administration of beta-alanine resulted in increased vascular remodeling. Inhibition of HIF transcription by taurine may be of therapeutic benefit in preventing hypoxia-induced vascular remodeling. In conclusion, we used transcriptome and metabolome analysis to identify a therapeutic low-molecular-weight ligand that plays a critical role in hypoxia-induced vascular remodeling. These techniques provided an excellent strategy for screening and validation of targets.

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Purification and characterization of a novel calcium-binding protein, S100C, from porcine heart

Cited by 59 publications

References 23 publications

Calcium-dependent Binding of Sorcin to the N-terminal Domain of Synexin (Annexin VII)

Calcium-dependent Binding of Sorcin to the N-terminal Domain of Synexin (Annexin VII)

S100A13 Is Involved in the Regulation of Fibroblast Growth Factor-1 and p40 Synaptotagmin-1 Release in Vitro

Target validation in hypoxia-induced vascular remodeling using transcriptome/metabolome analysis

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