Allelic loss of cyclophilin 40, an estrogen receptor-associated immunophilin, in breast carcinomas

Ward, Bryan K.; Kumar, Premlata; Turbett, Gavin R.; Edmondston, Joanne; Papadimitriou, John; Laing, Nigel G.; Ingram, David; Minchin, Rodney F.; Ratajczak, Thomas

doi:10.1007/s004320000182

Cited by 18 publications

(14 citation statements)

References 15 publications

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“…Only two other groups have an S. cerevisiae member but both lack an apparent C. elegans orthologue (Table 4A). The cyclophilin 40 orthologues are a group of heat shock‐inducible (Lebeau et al , 1999; Mark et al , 2001; Mayr, 2000; Weisman et al , 1996), predominantly nuclear (Huh et al , 2003; Lebeau et al , 1999; Mark et al , 2001) cyclophilins that interact with the C‐terminal MEEVD pentapeptide of heat shock protein 90 (Hsp90) (Ward et al , 2002) and have been reported to function within the Hsp90 complex (Davies et al , 2005; Duina et al , 1998; Sykes et al , 1993), potentially regulating its ATPase activity (Prodromou et al , 1999) during its functions in cellular signalling pathways that regulate transcription (Pratt and Toft, 1997; Sanchez and Ning, 1996; Ward et al , 2001; Warth et al , 1997), the cellular heat shock response (Bharadwaj et al , 1999) and also in maintaining the cell cycle protein kinases Mik1, Wee1 and Swe1 (Goes and Martin, 2001). Interestingly, the Hsp90 complex is present within C. elegans (Birnby et al , 2000), making the absence of an associated cyclophilin surprising.…”

Section: Resultsmentioning

confidence: 99%

Identification and Comparative Analysis of the Peptidyl-Prolylcis/transIsomerase Repertoires ofH. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Pemberton

Kay

2005

Comparative and Functional Genomics

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The peptidyl-prolyl cis/trans isomerase (PPIase) class of proteins comprises three member families that are found throughout nature and are present in all the major compartments of the cell. Their numbers appear to be linked to the number of genes in their respective genomes, although we have found the human repertoire to be smaller than expected due to a reduced cyclophilin repertoire. We show here that whilst the members of the cyclophilin family (which are predominantly found in the nucleus and cytoplasm) and the parvulin family (which are predominantly nuclear) are largely conserved between different repertoires, the FKBPs (which are predominantly found in the cytoplasm and endoplasmic reticulum) are not. It therefore appears that the cyclophilins and parvulins have evolved to perform conserved functions, while the FKBPs have evolved to fill ever-changing niches within the constantly evolving organisms. Many orthologous subgroups within the different PPIase families appear to have evolved from a distinct common ancestor, whereas others, such as the mitochondrial cyclophilins, appear to have evolved independently of one another. We have also identified a novel parvulin within Drosophila melanogaster that is unique to the fruit fly, indicating a recent evolutionary emergence. Interestingly, the fission yeast repertoire, which contains no unique cyclophilins and parvulins, shares no PPIases solely with the budding yeast but it does share a majority with the higher eukaryotes in this study, unlike the budding yeast. It therefore appears that, in comparison with Schizosaccharomyces pombe, Saccharomyces cerevisiae is a poor representation of the higher eukaryotes for the study of PPIases.

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Section: Resultsmentioning

confidence: 99%

Identification and Comparative Analysis of the Peptidyl-Prolylcis/transIsomerase Repertoires ofH. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Pemberton

Kay

2005

Comparative and Functional Genomics

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“…The breast cancer cell line MCF-7 showed a 75-fold increase of Cyp40 mRNA expression in response to high temperature stress and marked redistribution of Cyp40 protein from a predominantly nuclear location to nuclear accumulation [15]. In addition to Cyp40 up-regulation, Ward et al [16] also reported that genetic analysis of breast cancer patients heterozygous for Cyp40 showed 30% Cyp40 allelic loss. This indicates that dysregulation of CyP40 either as up-regulation of CyP40 gene expression or as loss of function could have pro-tumorigenic effects.…”

Section: Introductionmentioning

confidence: 99%

Cyclophilin 40 alters UVA-induced apoptosis and mitochondrial ROS generation in keratinocytes

Jandova

Janda

Sligh

2013

Experimental Cell Research

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The CyP40 protein encoded by PPID gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. The CyP40 protein has been shown to possess PPIase activity and, similar to other family members, can bind to the immunosuppressant drug cyclosporin A (CsA). In this study, we created keratinocyte cell lines with CyP40 being stably knocked down using viral particles containing shRNA for CyP40 which knocked down the expression level of CyP40 transcripts by 90 to 99%. The proliferation rates of the cell lines with silenced CyP40 were decreased compared to the control cells. After UVA irradiation, the rate of apoptosis was found to be significantly lower in CyP40 silenced cell lines than it was in control cells. Moreover, mitochondrial membrane potential (MMP) was found to be less dissipated and mitochondrial permeability transition pore (MPTP) less active in cells with knocked down CyP40 than in control cells after UVA irradiation. Also, less mitochondrial superoxide was detected in the cells with silenced CyP40 compared to control cells after UVA exposure. Moreover, silencing of CyP40 partially modulates expression of key genes involved in mitochondrial pore formation including CyPD, ANTs and VDAC family members. The ability of CyP40 to regulate UV induced apoptosis implicates this protein as a potential target for therapy in cancer cells.

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“…Cyclophilins have been reported to catalyse protein folding both within (Baker et al , 1994; Colley et al , 1991; Klappa et al , 1995; Price et al , 1994; Price et al , 1991; Schneuwly et al , 1989; Shieh et al , 1989; Stamnes et al , 1991; Zhang and Herscovitz, 2003) and without (Bruns et al , 2003; Davis et al , 1989; Di Luccio et al , 2001; Kern et al , 1995; Reader et al , 2001) the vesicular pathway, with some interactions potentially being regulatory (Ansari et al , 2002; Brazin et al , 2002; Coaker et al , 2005; Obata et al , 2005; Yurchenko et al , 2005). Roles for cyclophilins within receptor signalling pathways (Allain et al , 1994; Bukrinsky, 2002; Clevenger, 2003; Davies et al , 2005; Huang et al , 2002; Nagata et al , 2000; Obata et al , 2005; Pushkarsky et al , 2001; Ratajczak et al , 1993; Rycyzyn and Clevenger, 2000, 2002; Sanchez and Ning, 1996; Schiene‐Fischer and Yu, 2001; Tran et al , 2003; Ward et al , 1999, 2001; Warth et al , 1997; Yurchenko et al , 2001, 2002, 2005), in the mitochondrial permeability transition pore (Baines et al , 2005; Basso et al , 2005; Berardini et al , 2001; Clarke et al , 2002; Crompton, 1999; Lin and Lechleiter, 2002; Nakagawa et al , 2005; Scorrano et al , 1997; Sullivan et al , 1999; Waldmeier et al , 2002), in transcriptional regulation (Anderson et al , 2002; Pijnappel et al , 2001), in pre‐mRNA splicing (Bourquin et al , 1997; Dubourg et al , 2004; Horowitz and Krainer, 1997; Horowitz et al , 2002; Mortillaro and Berezney, 1998; Nestel et al , 1996; Teigelkamp et al , 1998), in translation (Ansari et al , 2002) and in cell cycle regulation (Arevalo‐Rodriguez and Heitman, 2005) have also been reported. Cyclophilins have also been reported to fu...…”

Section: Introductionmentioning

confidence: 99%

The cyclophilin repertoire of the fission yeastSchizosaccharomyces pombe

Pemberton

Kay

2005

Yeast

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The cyclophilin repertoire of the fission yeast Schizosaccharomyces pombe is comprised of nine members that are distributed over all three of its chromosomes and range from small single-domain to large multi-domain proteins. Each cyclophilin possesses only a single prolyl-isomerase domain, and these vary in their degree of consensus, including at positions that are likely to affect their drug-binding ability and catalytic activity. The additional identified motifs are involved in putative protein or RNA interactions, while a novel domain that is specific to SpCyp7 and its orthologues may have functions that include an interaction with hnRNPs. The Sz. pombe cyclophilins are found throughout the cell but appear to be absent from the mitochondria, which is unique among the characterized eukaryotic repertoires. SpCyp5, SpCyp6 and SpCyp8 have exhibited significant upregulation of their expression during the meiotic cycle and SpCyp5 has exhibited significant upregulation of its expression during heat stress. All nine have identified members in the repertoires of H. sapiens, D. melanogaster and A. thaliana. However, only three identified members in the cyclophilin repertoire of S. cerevisiae with SpCyp7 identifying a fourth protein that is not a member of the recognized repertoire due to its possession of a degenerate prolyl-isomerase domain. The cyclophilin repertoire of Sz. pombe therefore represents a better model group for the study of cyclophilin function in the higher eukaryotes.

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Allelic loss of cyclophilin 40, an estrogen receptor-associated immunophilin, in breast carcinomas

Cited by 18 publications

References 15 publications

Identification and Comparative Analysis of the Peptidyl-Prolylcis/transIsomerase Repertoires ofH. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Identification and Comparative Analysis of the Peptidyl-Prolylcis/transIsomerase Repertoires ofH. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Cyclophilin 40 alters UVA-induced apoptosis and mitochondrial ROS generation in keratinocytes

The cyclophilin repertoire of the fission yeastSchizosaccharomyces pombe

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