Amino Acid Sequence Determination of Human S100A12 (P6, Calgranulin C, CGRP, CAAF1) by Tandem Mass Spectrometry

Ilg, Evelyn C.; Troxler, Heinz; Bürgisser, Daniel; Kuster, Thomas; Markert, Michèle; Guignard, Florence; Hunziker, Peter; Birchler, Neil E.; Heizmann, Claus W.

doi:10.1006/bbrc.1996.1144

Cited by 46 publications

(36 citation statements)

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“…Slides were incubated with the following antibodies: monoclonal anti-p53-DO1 at a dilution of 1:100 and polyclonal anti-S100A2 at a dilution of 1:500 for 1 h at 37°C. Samples were washed with phosphate-buffered saline and incubated with the secondary CY2-and CY5-conjugated anti-mouse and the CY3-conjugated anti-rabbit antibody (Dianova, Hamburg, Germany) both at a dilution of 1:200 as described previously (37). Nuclear stainings were performed using 4Ј,6-diamidino-2-phenylindole.…”

Section: Methodsmentioning

confidence: 99%

The Calcium-binding Protein S100A2 Interacts with p53 and Modulates Its Transcriptional Activity

Mueller¹,

Schäfer²,

Ferrari

et al. 2005

Journal of Biological Chemistry

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129

126

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Head and neck squamous cell carcinoma express high levels of the EF-hand calcium-binding protein S100A2 in contrast to other tumorigenic tissues and cell lines where the expression of this protein is reduced. Subtractive hybridization of tumorigenic versus normal tumor-derived mammary epithelial cells has previously identified the S100A2 protein as potential tumor suppressor. The biological function of S100A2 in carcinogenesis, however, has not been elucidated to date. Here, we report for the first time that during recovery from hydroxyurea treatment, the S100A2 protein translocated from the cytoplasm to the nucleus and co-localized with the tumor suppressor p53 in two different oral carcinoma cells (FADU and SCC-25). Co-immunoprecipitation experiments and electrophoretic mobility shift assay showed that the interaction between S100A2 and p53 is Ca 2؉ -dependent. Preliminary characterization of this interaction indicated that the region in p53 involved with binding to S100A2 is located at the C terminus of p53. Finally, luciferase-coupled transactivation assays, where a p53-reporter construct was used, indicated that interaction with S100A2 increased p53 transcriptional activity. Our data suggest that in oral cancer cells the Ca 2؉ -and cell cycle-dependent p53-S100A2 interaction might modulate proliferation.

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Section: Methodsmentioning

confidence: 99%

The Calcium-binding Protein S100A2 Interacts with p53 and Modulates Its Transcriptional Activity

Mueller¹,

Schäfer²,

Ferrari

et al. 2005

Journal of Biological Chemistry

Self Cite

129

126

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“…Synonyms of S100A12 are calgranulin C, calgranulin-related protein (22), and calcium-binding protein in amniotic fluid-1 (25,26). Human S100A12 shows highest homologies to MRP14 (46%) and to MRP8 (40%) (21). Upon calcium binding, S100A12 from porcine granulocytes undergoes a gross conformational change, supporting the idea that this protein is involved in Ca 2ϩ -dependent signal transduction events (23).…”

mentioning

confidence: 88%

“…For example, only the complex of MRP8 and MRP14 has been described to inhibit casein kinases I and II, two enzymes involved in regulation of gene expression via mediation of RNA polymerase activity (20). Recently, a third S100 protein (S100A12) was identified in human and porcine granulocytes (21)(22)(23). The primary structure of human S100A12 consists of 91 amino acids with a molecular mass of 10,444 Da confirmed by ESI-MS (21).…”

mentioning

confidence: 99%

“…Recently, a third S100 protein (S100A12) was identified in human and porcine granulocytes (21)(22)(23). The primary structure of human S100A12 consists of 91 amino acids with a molecular mass of 10,444 Da confirmed by ESI-MS (21). S100A12 has been also found in small amounts in lysates of monocytes (24) and lymphocytes (23), but the amounts of S100A12 detected in these cells were in the range of contaminations by granulocytes in these mononuclear preparations.…”

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confidence: 99%

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S100A12 Is Expressed Exclusively by Granulocytes and Acts Independently from MRP8 and MRP14

Vogl¹,

Pröpper²,

Hartmann³

et al. 1999

Journal of Biological Chemistry

193

157

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Changes in cytosolic calcium concentrations regulate a wide variety of cellular processes, and calcium-binding proteins are the key molecules in signal transduction, differentiation, and cell cycle control. S100A12, a recently described member of the S100 protein family, has been shown to be coexpressed in granulocytes and monocytes together with two other S100 proteins, MRP8 (S100A8) and MRP14 (S100A9), and a functional relationship between these three S100 proteins has been suggested. Using Western blotting, calcium overlays, intracellular flow cytometry, and cytospin preparations, we demonstrate that S100A12 expression in leukocytes is specifically restricted to granulocytes and that S100A12 represents one of the major calcium-binding proteins in these cells. S100A12, MRP8, and MRP14 translocate simultaneously from the cytosol to cytoskeletal and membrane structures in a calcium-dependent manner. However, no evidence for direct protein-protein interactions of S100A12 with either MRP8 or MRP14 or the heterodimer was found by chemical cross-linking, density gradient centrifugation, mass spectrometric measurements, or yeast two hybrid detection. Thus, S100A12 acts individually during calcium-dependent signaling, independent of MRP8, MRP14, and the heterodimer MRP8/ MRP14. This granulocyte-specific signal transduction pathway may offer attractive targets for therapeutic intervention with exaggerated granulocyte activity in pathological states.Granulocytes and monocytes are major effector cells during inflammatory processes. Undue activation of these cells is a pathophysiological factor in many diseases, e.g. rheumatoid arthritis and chronic inflammatory bowel disease (1-4). In monocytes and granulocytes, intracellular Ca 2ϩ regulates various acute response activities, such as respiratory burst, phagocytosis, degranulation, and release of degrading enzymes (5-8). One molecular pathway of calcium signal transduction is calcium-binding proteins of the S100 multigene family, which comprises a group of small, acidic proteins with a tissue-and cell cycle-specific expression (9 -11). S100 proteins contain two calcium-binding sites per molecule (12). Two members of this family have been found in human granulocytes and monocytes, called macrophage migration inhibitory factor-related protein 8 (MRP8) 1 (S100A8) and MRP14 (S100A9), which represent up to 40% of the calcium binding capacity in monocytes (13,14). Both proteins form noncovalently associated complexes in a calciumdependent manner (15, 16). These complexes translocate from cytoplasm to membranes, as well as to intermediate filaments, after elevation of intracellular Ca 2ϩ levels, and this correlates with the induction of inflammatory actions of granulocytes and monocytes. Thus, MRP8 and MRP14 seem to be important regulators of cytoskeletal/membrane interactions during phagocyte activation (17-19).The calcium-induced change in the complex pattern of these two proteins has been considered to be important for their biological function (15,19). For example, only the ...

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“…These proteins constitute a subfamily of S100 proteins, of which 3 have been characterized: S100A8, S100A9, and S100A12 (18)(19)(20). These small proteins of 10-14 kd are constitutively expressed at high levels in the cytosol of neutrophils, monocytes, and activated macrophages (20)(21)(22).…”

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confidence: 99%

Role of S100A8 and S100A9 in neutrophil recruitment in response to monosodium urate monohydrate crystals in the air‐pouch model of acute gouty arthritis

Ryckman¹,

McColl²,

Vandal³

et al. 2003

Arthritis & Rheumatism

167

150

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Objective. To examine the role of chemokines, S100A8, and S100A9 in neutrophil accumulation induced by the causative agent of gout, monosodium urate monohydrate (MSU) crystals.Methods. MSU crystal-induced neutrophil migration was studied in the murine air-pouch model. Release of chemokines, S100A8, S100A9, and S100A8/A9 in response to MSU crystals was quantified by enzymelinked immunosorbent assays. Recruited cells were counted following acetic blue staining, and the subpopulations were characterized by Wright-Giemsa staining of cytospins.Results. MSU crystals induced the accumulation of neutrophils following injection in the air pouch, which correlated with the release of the chemokines CXCL1, CXCL2, CCL2, and CCL3. However, none of these was found to play an important role in neutrophil migration induced by MSU crystals by passive immunization with antibodies directed against each chemokine. S100A8, S100A9, and S100A8/A9 were also found at high levels in the pouch exudates following injection of MSU crystals. In addition, injection of S100A8, S100A9, or S100A8/A9 led to the accumulation of neutrophils in the murine air pouch, demonstrating their proinflammatory activities in vivo. Passive immunization with anti-S100A8 and anti-S100A9 led to a total inhibition of the accumulation of neutrophils. Finally, S100A8/A9 was found at high concentrations in the synovial fluid of patients with gout.Conclusion. S100A8 and S100A8/A9 are essential to neutrophil migration induced by MSU crystals. These results suggest that they might be involved in the pathogenesis of gout.

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Amino Acid Sequence Determination of Human S100A12 (P6, Calgranulin C, CGRP, CAAF1) by Tandem Mass Spectrometry

Cited by 46 publications

References 0 publications

The Calcium-binding Protein S100A2 Interacts with p53 and Modulates Its Transcriptional Activity

The Calcium-binding Protein S100A2 Interacts with p53 and Modulates Its Transcriptional Activity

S100A12 Is Expressed Exclusively by Granulocytes and Acts Independently from MRP8 and MRP14

Role of S100A8 and S100A9 in neutrophil recruitment in response to monosodium urate monohydrate crystals in the air‐pouch model of acute gouty arthritis

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