Ca2+-Dependent Binding of Calcyclin to Muscle Tropomyosin

Golitsina, Nina L.; Kordowska, Jolanta; Wang, C.-L.A.; Lehrer, Sherwin S.

doi:10.1006/bbrc.1996.0410

Cited by 50 publications

(37 citation statements)

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“…The interaction and the colocalisation of S100A6 and tropomyosin have been documented (Golitsina et al, 1996;Orre et al, 2007). Tropomyosins have been shown to regulate microfilament organisation and actin dynamics (Boyd et al, 1995;Gunning et al, 2008), with reduction in tropomyosin 1 levels leading to anchorage independent growth (Boyd et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

“…Protein spots observed on gels after immunoprecipitation with anti-S100A6 antibody ( Figure 1A Table 1). The identified proteins included the known binding partners annexin 11 (Mizutani et al, 1992), annexin 2 (Zeng et al, 1993), and tropomyosin (Golitsina et al, 1996) as well as a candidate novel interactor lamin B1. As both S100A6 and annexin 2 are overexpressed in pancreatic cancer, with expression occurring early in the development of the cancer in both cases (Sitek et al, 2005;Vimalachandran et al, 2005;Esposito et al, 2006;Ortiz-Zapater et al, 2007), we focused our attention particularly on annexin 2.…”

Section: Identification Of S100a6-binding Proteinsmentioning

confidence: 99%

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S100A6 binds to annexin 2 in pancreatic cancer cells and promotes pancreatic cancer cell motility

et al. 2009

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BACKGROUND: High levels of S100A6 have been associated with poor outcome in pancreatic cancer patients. The functional role of S100A6 is, however, poorly understood. METHODS: Immunoprecipitation followed by two-dimensional gel electrophoresis and mass spectrometry were undertaken to identify S100A6 interacting proteins in pancreatic cancer cells. Immunohistochemistry and coimmunofluorescence were performed to examine expression or colocalisation of proteins. siRNA was used to deplete specific proteins and effects on motility were measured using Boyden Chamber and wound healing assays. RESULTS: Our proteomic screen to identify S100A6 interacting proteins revealed annexin 11, annexin 2, tropomyosin b and a candidate novel interactor lamin B1. Of these, annexin 2 was considered particularly interesting, as, like S100A6, it is expressed early in the development of pancreatic cancer and overexpression occurs with high frequency in invasive cancer. Reciprocal immunoprecipitation confirmed the interaction between annexin 2 and S100A6 and the proteins colocalised, particularly in the plasma membrane of cultured pancreatic cancer cells and primary pancreatic tumour tissue. Analysis of primary pancreatic cancer specimens (n ¼ 55) revealed a strong association between high levels of cytoplasmic S100A6 and the presence of annexin 2 in the plasma membrane of cancer cells (P ¼ 0.009). Depletion of S100A6 was accompanied by diminished levels of membrane annexin 2 and caused a pronounced reduction in the motility of pancreatic cancer cells. CONCLUSION: These findings point towards a functional role for S100A6 that may help explain the link between S100A6 expression in pancreatic cancer and aggressive disease.

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Section: Discussionmentioning

confidence: 99%

Section: Identification Of S100a6-binding Proteinsmentioning

confidence: 99%

S100A6 binds to annexin 2 in pancreatic cancer cells and promotes pancreatic cancer cell motility

et al. 2009

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“…S100A6 belongs to the S100 family of calcium-binding protein, which is involved in the Ca 2+ -dependent regulation of a variety of intracellular activities including cell proliferation and di erentiation, intracellular Ca 2+ homeostasis and in¯ammation and protection from oxidative cell damage (SchaÈ fer and Heizmann, 1996;Donato, 1999). S100 proteins are also involved directly in the dynamic control of the actin cytoskeleton (SchaÈ fer and Heizmann, 1996;Donato, 1999) by modulating the activity of distinct tropomyosin isoforms (Golitsina et al, 1996), by direct linking to actin (Takenaga et al, 1994), or by modifying the microtubule cytoskeleton (SchaÈ fer and Heizmann, 1996; Donato, 1999) which, in turn, modi®es the organization of the actin cytoskeleton (WatermanStorer and Salmon, 1999). We showed recently that the level of expression of S100A6 protein relates directly to the level of malignancy in human astrocytic tumors (Camby et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Gastrin induces over-expression of genes involved in human U373 glioblastoma cell migration

et al. 2001

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Astrocytic tumors are the most common and the most malignant primary tumors of the central nervous system. We had previously observed that gastrin could signi®-cantly modulate both cell proliferation and migration of astrocytoma cells. We have investigated in the present study which genes could be targeted by gastrin in tumor astrocyte migration. Using a subtractive hybridization PCR technique we have cloned genes di erentially overexpressed in human astrocytoma U373 cells treated or not with gastrin. We found about 70 genes overexpressed by gastrin. Among the genes overexpressed by gastrin, we paid particular attention to tenascin-C, S100A6 and MLCK genes because their direct involvement in cell migration features. Their gastrin-induced overexpression was quantitatively determined by competitive RT ± PCR technique. We also showed by means of a reporter gene system that S100A6 and tenascin-C respective promoters were upregulated after gastrin treatment. These data show that gastrin-mediated e ects in glioblastoma cells occur through activation of a number of genes involved in cell migration and suggest that gastrin could be a target in new therapeutic strategies against malignant gliomas. Oncogene (2001) 20, 7021 ± 7028.

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“…Calcyclin cDNA (nucleotides 51-327) was subcloned into the EcoRI site of the Bluescript KS vector. Sense and antisense cRNAs were synthesized after linearization using 35 S-labeled UTP (specific activity of 1000 Ci/mmol; Amersham Biosciences) and the Riboprobe ® Combination System T3/T7 kit (Promega). Other reagents used for the experiments (adenosine, guanosine, cytosine 5Ј-triphosphate, ribonucleasin, dithiothreitol, and RNA polymerases) were from Promega.…”

Section: Methodsmentioning

confidence: 99%

Calcyclin Is an Early Vasopressin-induced Gene in the Renal Collecting Duct

Courtois-Coutry

Moellic

Boulkroun

et al. 2002

Journal of Biological Chemistry

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Long-term effects of arginine vasopressin (AVP) in the kidney involve the transcription of unidentified genes. By subtractive hybridization experiments performed on the RCCD 1 cortical collecting duct cell line, we identified calcyclin as an early AVP-induced gene (1 h). Calcyclin is a calcium-binding protein involved in the transduction of intracellular signals. In the kidney, calcyclin was localized at the mRNA level in the glomerulus, all along the collecting duct, and in the epithelium lining the papilla. In RCCD 1 cells and in m-IMCD 3 inner medullary collecting duct cells, calcyclin was evidenced in the cytoplasm. Calcyclin mRNA levels were progressively increased by AVP treatment in RCCD 1 (1.7-fold at 4 h) and m-IMCD 3 (2-fold at 7.5 h) cells. In RCCD 1 cells, calcyclin protein levels were increased by 4 h of AVP treatment. In vivo, treatment of genetically vasopressindeficient Brattleboro rats with AVP for 4 days induced an increase in both calcyclin and aquaporin-2 mRNA expression. Finally, introduction of anti-calcyclin antibodies into RCCD 1 cells by permeabilizing the plasma membrane prevented the long-term (but not short-term) increase in short-circuit current induced by AVP. Taken together, these results suggest that calcyclin is an early vasopressin-induced gene that participates in the late phase of the hormone response in transepithelial ion transport. Arginine vasopressin (AVP)1 is a polypeptide hormone involved in the regulation of renal water and ion transport. In the collecting duct, AVP coordinately increases water and NaCl reabsorption by a two-step mechanism. The first mechanism is responsible for the short-term effects of AVP. These effects consist of the translocation of aquaporin-2 (AQP2) water channels and amiloride-sensitive sodium channels from intracellular pools to the apical membrane, promoting an increase in both sodium and water entry (1-4). This increase induces, in turn, a coordinate rise in transepithelial water and sodium reabsorption (5-10). These effects are rapid and transient because the effect is down-regulated after ϳ1 h in the rat collecting duct (11). In addition to this short-term effect, AVP induces a long-term effect. This effect consists of a late increase in transepithelial water, sodium, and chloride transport after several hours. This late effect is mediated through a transcriptional/translational mechanism and involves an increase in the mRNA and de novo synthesis of different proteins such as AQP2; the ␤ and ␥ (but not ␣) subunits of ENaC (epithelial Na ϩ channel); the ␣ 1 (but not ␤ 1 ) subunit of Na ϩ /K ϩ -ATPase; and CFTR (cystic fibrosis transmembrane conductance regulator) (12-15). This long-term effect may involve the genomic pathway by activation of cAMP-responsive elements in the promoter region of these genes and may ensure a sustained increase in sodium, chloride, and water transport in this segment of the nephron. A recent study has focused on the effects of 4 h of treatment with vasopressin on the transcriptome of a mouse kidney cortical colle...

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Ca2+-Dependent Binding of Calcyclin to Muscle Tropomyosin

Cited by 50 publications

References 0 publications

S100A6 binds to annexin 2 in pancreatic cancer cells and promotes pancreatic cancer cell motility

S100A6 binds to annexin 2 in pancreatic cancer cells and promotes pancreatic cancer cell motility

Gastrin induces over-expression of genes involved in human U373 glioblastoma cell migration

Calcyclin Is an Early Vasopressin-induced Gene in the Renal Collecting Duct

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