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Article ; Online: Caspase-2 is required for DNA damage-induced expression of the CDK inhibitor p21(WAF1/CIP1).

Sohn, D / Budach, W / Jänicke, R U

2011 Volume 18, Issue 10, Page(s) 1664–1674

Abstract: Although caspase-2 represents the most conserved caspase across species and was the second caspase identified, its precise function remains enigmatic. In several cell types we show that knockdown of caspase-2 specifically impaired DNA damage-induced p21 ... ...

Abstract	Although caspase-2 represents the most conserved caspase across species and was the second caspase identified, its precise function remains enigmatic. In several cell types we show that knockdown of caspase-2 specifically impaired DNA damage-induced p21 expression, whereas overexpression of a caspase-2 mutant increased p21 levels. Caspase-2 did not influence p21 mRNA transcription; moreover, various inhibitors targeting proteasomal or non-proteasomal proteases, including caspases, could not restore p21 protein levels following knockdown of caspase-2. As, however, silencing of caspase-2 impaired exogenous expression of p21 constructs containing 3'-UTR sequences, our results strongly indicate that caspase-2 regulates p21 expression at the translational level. Intriguingly, unlike depletion of caspase-2, which prevented p21 expression and thereby reverted the γ-IR-induced senescent phenotype of wild-type HCT116 colon carcinoma cells into apoptosis, knockdown of none of the caspase-2-interacting components RAIDD, RIP or DNA-PKcs was able to mimic these processes. Together, our data suggest that this novel role of caspase-2 as a translational regulator of p21 expression occurs not only independently of its enzymatic activity but also does not require known caspase-2-activating platforms.
MeSH term(s)	3' Untranslated Regions/genetics ; Apoptosis/genetics ; Apoptosis/physiology ; Blotting, Western ; Caspase 2/genetics ; Caspase 2/metabolism ; Cell Cycle/genetics ; Cell Cycle/physiology ; Cyclin-Dependent Kinase Inhibitor p21/genetics ; Cyclin-Dependent Kinase Inhibitor p21/metabolism ; DNA Damage/genetics ; DNA Damage/physiology ; HCT116 Cells ; Humans
Chemical Substances	3' Untranslated Regions ; CDKN1A protein, human ; Cyclin-Dependent Kinase Inhibitor p21 ; Caspase 2 (EC 3.4.22.-)
Language	English
Publishing date	2011-04-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/cdd.2011.34
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: The dark side of a tumor suppressor: anti-apoptotic p53.

Jänicke, R U / Sohn, D / Schulze-Osthoff, K

Cell death and differentiation

2008 Volume 15, Issue 6, Page(s) 959–976

Abstract: Depending on multiple factors DNA damage leads either to cell cycle arrest or apoptosis. One of the main players deciding the fate of a cell is the tumor suppressor p53 that modulates these responses in a transcription-dependent and -independent manner. ... ...

Abstract	Depending on multiple factors DNA damage leads either to cell cycle arrest or apoptosis. One of the main players deciding the fate of a cell is the tumor suppressor p53 that modulates these responses in a transcription-dependent and -independent manner. Over the past few years, however, strong evidence accumulated that p53 engages also powerful pro-survival pathways by transcriptionally activating a multitude of genes whose products efficiently counteract apoptosis. Our review summarizes the current knowledge concerning approximately forty p53-regulated proteins that exert their anti-apoptotic potential by interfering with diverse cellular processes. These activities are surely essential for normal development and maintenance of a healthy organism, but may easily turn into the dark side of the tumor suppressor p53 contributing to tumorigenesis.
MeSH term(s)	Animals ; Apoptosis ; Apoptosis Regulatory Proteins/metabolism ; Cell Cycle ; DNA Repair ; MAP Kinase Signaling System ; Oxidative Stress ; Transcription Factors/metabolism ; Tumor Suppressor Protein p53/physiology
Chemical Substances	Apoptosis Regulatory Proteins ; Transcription Factors ; Tumor Suppressor Protein p53
Language	English
Publishing date	2008-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1225672-9
ISSN	1350-9047
ISSN	1350-9047
DOI	10.1038/cdd.2008.33
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Treatment, outcome and quality of life of 1239 patients with advanced non-small cell lung cancer - final results from the prospective German TLK cohort study.

von Verschuer, Ulla / Schnell, Roland / Tessen, Hans Werner / Eggert, Jochen / Binninger, Adrian / Spring, Lisa / Jänicke, Martina / Marschner, Norbert

Lung cancer (Amsterdam, Netherlands)

2017 Volume 112, Page(s) 216–224

Abstract: Objectives: Real-life data on advanced non-small cell lung cancer (NSCLC) are centrally important to complement the results from clinical trials and to improve the standard of care. We present data on the choice of systemic first- and second-line ... ...

Abstract	Objectives: Real-life data on advanced non-small cell lung cancer (NSCLC) are centrally important to complement the results from clinical trials and to improve the standard of care. We present data on the choice of systemic first- and second-line treatment, number of treatment lines, survival and longitudinal data on health-related quality of life (HRQOL) of patients treated by medical oncologists in Germany. Materials and methods: 1239 patients with advanced NSCLC were recruited at start of first-line therapy into the prospective German clinical cohort study TLK (Tumour Registry Lung Cancer) by 107 sites between February 2010 and December 2013 and followed-up until January 2016. HRQOL was assessed using the EORTC QLQ-C30 and LC13 questionnaires. Results: Most patients receive carboplatin- or cisplatin-based doublet chemotherapy in first-line treatment. The choice of platinum agent did neither influence the outcome: median overall survival (OS) was 12.2 months for carboplatin combinations (95% confidence interval [CI] 10.0-13.8) and 11.9 months for cisplatin combinations (95% CI 10.2-13.8), nor did it have a marked impact on the HRQOL. Patients receiving cisplatin were younger and fitter at start of therapy than patients receiving carboplatin or mono-chemotherapy. The longitudinal HRQOL analysis revealed the main symptoms that need to be addressed in follow-up care, irrespective of the platinum agent: fatigue, nausea, dyspnoea and pain. The patients receiving targeted therapies with tyrosine kinase inhibitors (TKIs) had a median OS of 22.1 months (95% CI 15.0-35.1) and considerably superior HRQOL. Conclusion: There was no difference in outcome between the platinum compounds cisplatin and carboplatin in first-line treatment of advanced NSCLC in routine care. This is the first report of longitudinal HRQOL data comparing treatments, showing no difference between carboplatin and cisplatin.
MeSH term(s)	Aged ; Aged, 80 and over ; Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Biomarkers, Tumor ; Carcinoma, Non-Small-Cell Lung/epidemiology ; Carcinoma, Non-Small-Cell Lung/mortality ; Carcinoma, Non-Small-Cell Lung/pathology ; Carcinoma, Non-Small-Cell Lung/therapy ; Comorbidity ; Female ; Germany/epidemiology ; Health Care Surveys ; Humans ; Lung Neoplasms/epidemiology ; Lung Neoplasms/mortality ; Lung Neoplasms/pathology ; Lung Neoplasms/therapy ; Male ; Middle Aged ; Neoplasm Staging ; Patient Reported Outcome Measures ; Prospective Studies ; Quality of Life ; Survival Analysis ; Treatment Outcome
Chemical Substances	Biomarkers, Tumor
Language	English
Publishing date	2017-09-12
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632771-0
ISSN	1872-8332 ; 0169-5002
ISSN (online)	1872-8332
ISSN	0169-5002
DOI	10.1016/j.lungcan.2017.07.031
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Zs.A 2135: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Attention deficit hyperactivity disorder medications and BMI trajectories: The role of medication type, sex and age.

Gurka, Matthew J / Siddiqi, Siraj U / Filipp, Stephanie L / Mercado, Rebeccah / Thompson, Lindsay A / Janicke, David M / Shenkman, Elizabeth A

Pediatric obesity

2020 Volume 16, Issue 4, Page(s) e12738

Abstract: Objectives: Attention deficit hyperactivity disorder (ADHD) and the medications used to treat it are associated with obesity. Stimulants lead to weight loss, while antipsychotics and antidepressants lead to weight gain. Little is known, however, how ... ...

Abstract	Objectives: Attention deficit hyperactivity disorder (ADHD) and the medications used to treat it are associated with obesity. Stimulants lead to weight loss, while antipsychotics and antidepressants lead to weight gain. Little is known, however, how alpha-2-agonists impact weight, or the independent effect on BMI of these four classes of medications, which are often prescribed concurrently. We aimed to estimate the proximal change in BMI associated with start of medication and to assess whether medication-specific departures in BMI varied by age and sex. Study design: We analysed longitudinal electronic health records from children (4-19 years) with an ADHD diagnosis seen at one healthcare system (2011-2018). Their BMI z-scores were fit as a cubic function of age via a mixed model, separately by sex and adjusting for race/ethnicity. From this model, we estimated annual changes in BMI-z after medication, allowing changes to vary by age and sex. Results: Among the 22 714 children with ADHD (mean initial age = 10.0), 4335 (19.1%) were never prescribed ADHD medication. The others (80.9%) experienced departures in BMI-z after start of all four medication classes, which varied across age and sex (interaction P-values < .01). All medications had larger impacts at younger ages. As expected, decreased BMI-z was observed with stimulants, while antidepressants and antipsychotics led to BMI-z increases; alpha-agonists also were associated with BMI-z increases. Conclusions: This longitudinal study revealed that ADHD medications are independently associated with proximal changes in BMI-z after initiation, significantly varying by sex and age. Future research should study further the interactions of these medications on long-term impacts on obesity.
MeSH term(s)	Attention Deficit Disorder with Hyperactivity/drug therapy ; Attention Deficit Disorder with Hyperactivity/epidemiology ; Body Mass Index ; Central Nervous System Stimulants/therapeutic use ; Child ; Female ; Humans ; Longitudinal Studies ; Male ; Obesity/drug therapy
Chemical Substances	Central Nervous System Stimulants
Language	English
Publishing date	2020-10-16
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2655527-X
ISSN	2047-6310 ; 2047-6302
ISSN (online)	2047-6310
ISSN	2047-6302
DOI	10.1111/ijpo.12738
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Article: Many cuts to ruin: a comprehensive update of caspase substrates.

Fischer, U / Jänicke, R U / Schulze-Osthoff, K

Cell death and differentiation

2003 Volume 10, Issue 1, Page(s) 76–100

Abstract: Apoptotic cell death is executed by the caspase-mediated cleavage of various vital proteins. Elucidating the consequences of this endoproteolytic cleavage is crucial for our understanding of cell death and other biological processes. Many caspase ... ...

Abstract	Apoptotic cell death is executed by the caspase-mediated cleavage of various vital proteins. Elucidating the consequences of this endoproteolytic cleavage is crucial for our understanding of cell death and other biological processes. Many caspase substrates are just cleaved as bystanders, because they happen to contain a caspase cleavage site in their sequence. Several targets, however, have a discrete function in propagation of the cell death process. Many structural and regulatory proteins are inactivated by caspases, while other substrates can be activated. In most cases, the consequences of this gain-of-function are poorly understood. Caspase substrates can regulate the key morphological changes in apoptosis. Several caspase substrates also act as transducers and amplifiers that determine the apoptotic threshold and cell fate. This review summarizes the known caspase substrates comprising a bewildering list of more than 280 different proteins. We highlight some recent aspects inferred by the cleavage of certain proteins in apoptosis. We also discuss emerging themes of caspase cleavage in other forms of cell death and, in particular, in apparently unrelated processes, such as cell cycle regulation and cellular differentiation.
MeSH term(s)	Animals ; Apoptosis/physiology ; Binding Sites/physiology ; Caspases/metabolism ; Eukaryotic Cells/enzymology ; Humans ; Proteins/metabolism ; Signal Transduction/physiology
Chemical Substances	Proteins ; Caspases (EC 3.4.22.-)
Keywords	covid19
Language	English
Publishing date	2003-05-09
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1225672-9
ISSN	1350-9047
ISSN	1350-9047
DOI	10.1038/sj.cdd.4401160
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Emerging roles of caspase-3 in apoptosis.

Porter, A G / Jänicke, R U

Cell death and differentiation

1999 Volume 6, Issue 2, Page(s) 99–104

Abstract: Caspases are crucial mediators of programmed cell death (apoptosis). Among them, caspase-3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins. However, the specific requirements of this (or any other) ...

Abstract	Caspases are crucial mediators of programmed cell death (apoptosis). Among them, caspase-3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins. However, the specific requirements of this (or any other) caspase in apoptosis have remained largely unknown until now. Pathways to caspase-3 activation have been identified that are either dependent on or independent of mitochondrial cytochrome c release and caspase-9 function. Caspase-3 is essential for normal brain development and is important or essential in other apoptotic scenarios in a remarkable tissue-, cell type- or death stimulus-specific manner. Caspase-3 is also required for some typical hallmarks of apoptosis, and is indispensable for apoptotic chromatin condensation and DNA fragmentation in all cell types examined. Thus, caspase-3 is essential for certain processes associated with the dismantling of the cell and the formation of apoptotic bodies, but it may also function before or at the stage when commitment to loss of cell viability is made.
MeSH term(s)	Animals ; Apoptosis/physiology ; Caspase 3 ; Caspases/metabolism ; Chromatin/genetics ; Cytochrome c Group/metabolism ; DNA Fragmentation/genetics ; Enzyme Activation ; Mice ; Mice, Knockout
Chemical Substances	Chromatin ; Cytochrome c Group ; Casp3 protein, mouse (EC 3.4.22.-) ; Caspase 3 (EC 3.4.22.-) ; Caspases (EC 3.4.22.-)
Language	English
Publishing date	1999-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1225672-9
ISSN	1350-9047
ISSN	1350-9047
DOI	10.1038/sj.cdd.4400476
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Article ; Online: The p90 ribosomal S6 kinase (RSK) inhibitor BI-D1870 prevents gamma irradiation-induced apoptosis and mediates senescence via RSK- and p53-independent accumulation of p21WAF1/CIP1.

Neise, D / Sohn, D / Stefanski, A / Goto, H / Inagaki, M / Wesselborg, S / Budach, W / Stühler, K / Jänicke, R U

Cell death & disease

2013 Volume 4, Page(s) e859

Abstract: The p90 ribosomal S6 kinase (RSK) family is a group of highly conserved Ser/Thr kinases that promote cell proliferation, growth, motility and survival. As they are almost exclusively activated downstream of extracellular signal-regulated kinases 1 and 2 ( ...

Abstract	The p90 ribosomal S6 kinase (RSK) family is a group of highly conserved Ser/Thr kinases that promote cell proliferation, growth, motility and survival. As they are almost exclusively activated downstream of extracellular signal-regulated kinases 1 and 2 (ERK1/2), therapeutic intervention by RSK inhibition is less likely to produce such severe side effects as those observed following inhibition of the upstream master regulators Raf, MEK and ERK1/2. Here, we report that BI-D1870, a potent small molecule inhibitor of RSKs, induces apoptosis, although preferentially, in a p21-deficient background. On the other hand, BI-D1870 also induces a strong transcription- and p53-independent accumulation of p21 protein and protects cells from gamma irradiation (γIR)-induced apoptosis, driving them into senescence even in the absence of γIR. Although we identified p21 in in vitro kinase assays as a novel RSK substrate that specifically becomes phosphorylated by RSK1-3 at Ser116 and Ser146, RNA-interference, overexpression and co-immunoprecipitation studies as well as the use of SL0101, another specific RSK inhibitor, revealed that BI-D1870 mediates p21 accumulation via a yet unknown pathway that, besides its off-site targets polo-like kinase-1 and AuroraB, also does also not involve RSKs. Thus, this novel off-target effect of BI-D1870 should be taken into serious consideration in future studies investigating the role of RSKs in cellular signaling and tumorigenesis.
MeSH term(s)	Apoptosis/drug effects ; Apoptosis/radiation effects ; Aurora Kinases/metabolism ; Benzopyrans/pharmacology ; Cell Cycle Proteins/metabolism ; Cellular Senescence/drug effects ; Cellular Senescence/radiation effects ; Cyclin-Dependent Kinase Inhibitor p21/metabolism ; Cyclin-Dependent Kinase Inhibitor p21/pharmacology ; Gamma Rays ; Gene Knockdown Techniques ; HCT116 Cells ; Humans ; Isoenzymes/metabolism ; Monosaccharides/pharmacology ; Phosphorylation/drug effects ; Phosphorylation/radiation effects ; Phosphoserine/metabolism ; Protein Kinase Inhibitors/pharmacology ; Protein Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Pteridines/pharmacology ; Ribosomal Protein S6 Kinases, 90-kDa/antagonists & inhibitors ; Ribosomal Protein S6 Kinases, 90-kDa/metabolism ; Stress, Physiological/drug effects ; Stress, Physiological/radiation effects ; Substrate Specificity/drug effects ; Substrate Specificity/radiation effects ; Transcription, Genetic/drug effects ; Transcription, Genetic/radiation effects ; Tumor Suppressor Protein p53/metabolism ; Polo-Like Kinase 1
Chemical Substances	BI D1870 ; Benzopyrans ; Cell Cycle Proteins ; Cyclin-Dependent Kinase Inhibitor p21 ; Isoenzymes ; Monosaccharides ; Protein Kinase Inhibitors ; Proto-Oncogene Proteins ; Pteridines ; SL0101 ; Tumor Suppressor Protein p53 ; Phosphoserine (17885-08-4) ; Aurora Kinases (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Ribosomal Protein S6 Kinases, 90-kDa (EC 2.7.11.1)
Language	English
Publishing date	2013-10-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/cddis.2013.386
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Article ; Online: Pifithrin-alpha protects against DNA damage-induced apoptosis downstream of mitochondria independent of p53.

Sohn, D / Graupner, V / Neise, D / Essmann, F / Schulze-Osthoff, K / Jänicke, R U

Cell death and differentiation

2009 Volume 16, Issue 6, Page(s) 869–878

Abstract: Pifithrin-alpha (PFT-alpha) was shown to specifically block transcriptional activity of the tumor suppressor p53 and was therefore proposed to be useful in preventing the severe side effects often associated with chemo- and radiotherapy. We report here ... ...

Abstract	Pifithrin-alpha (PFT-alpha) was shown to specifically block transcriptional activity of the tumor suppressor p53 and was therefore proposed to be useful in preventing the severe side effects often associated with chemo- and radiotherapy. We report here that although PFT-alpha efficiently protected different cell types from DNA damage-induced apoptosis, it mediated this effect regardless of the presence or absence of p53. Interestingly, PFT-alpha blocked the apoptosome-mediated processing and activation of caspase-9 and -3 without interfering with the activation of mitochondria. Neither the DNA damage-induced activation of Bax or Bak nor the loss of the mitochondrial membrane potential or the final release of cytochrome c were inhibited by this compound. Instead, the ability of PFT-alpha to protect p53-deficient cells from DNA damage-induced caspase activation and apoptosis was greatly diminished after siRNA-mediated downregulation of cyclin-D1 expression. In contrast, downregulation of other proteins involved in cell-cycle progression, such as the retinoblastoma protein, cyclin D3, as well as the cyclin-dependent kinases, 2, 4 and 6, could not abolish this protection. Thus, our data show that PFT-alpha protects cells from DNA damage-induced apoptosis also by a p53-independent mechanism that takes place downstream of mitochondria and that might involve cyclin D1.
MeSH term(s)	Apoptosis ; Apoptosomes/metabolism ; Benzothiazoles/pharmacology ; Caspase 3/metabolism ; Caspase 9/metabolism ; Cell Line ; Cyclin D1/deficiency ; Cyclin D1/metabolism ; Cyclin-Dependent Kinases/metabolism ; DNA Damage ; Humans ; Mitochondria/physiology ; RNA, Small Interfering/metabolism ; Radiation, Ionizing ; Retinoblastoma Protein/metabolism ; Toluene/analogs & derivatives ; Toluene/pharmacology ; Tumor Suppressor Protein p53/deficiency ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	Apoptosomes ; Benzothiazoles ; RNA, Small Interfering ; Retinoblastoma Protein ; Tumor Suppressor Protein p53 ; Cyclin D1 (136601-57-5) ; Toluene (3FPU23BG52) ; pifithrin (D213B92S1Y) ; Cyclin-Dependent Kinases (EC 2.7.11.22) ; Caspase 3 (EC 3.4.22.-) ; Caspase 9 (EC 3.4.22.-)
Language	English
Publishing date	2009-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/cdd.2009.17
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Synthesis of hyaluronan in oesophageal cancer cells is uncoupled from the prostaglandin-cAMP pathway.

Twarock, S / Röck, K / Sarbia, M / Weber, A A / Jänicke, R U / Fischer, J W

British journal of pharmacology

2009 Volume 157, Issue 2, Page(s) 234–243

Abstract: Background and purpose: Cyclooxygenase-2 (COX2) and hyaluronic acid (HA) are common in tumours and both independently promote tumour progression. Furthermore, COX2-dependent synthesis of prostaglandins (PGs) stimulates HA synthase-1 (HAS1) and HAS2 mRNA ...

Abstract	Background and purpose: Cyclooxygenase-2 (COX2) and hyaluronic acid (HA) are common in tumours and both independently promote tumour progression. Furthermore, COX2-dependent synthesis of prostaglandins (PGs) stimulates HA synthase-1 (HAS1) and HAS2 mRNA expression, together with HA synthesis via the cAMP/protein kinase A pathway in vascular smooth muscle cells. Therefore, the aim of the present study was to elucidate whether COX2-mediated PGs induce transcription of HAS isoforms in cancer cells as well. Experimental approach: Human oesophageal squamous cell (OSC) carcinoma specimens were characterized with respect to HA, COX2 and CD44 expression by immunohistochemistry. OSC cell lines (OSC1, OSC2) and HeLa cell lines (D98, H21) were exposed to exogenous PG analoques (100 nmol.L(-1)), etoricoxib (10 micromol.L(-1)) and forskolin (10 micromol.L(-1)). Subsequently, cAMP levels, HA secretion and HAS isoform expression were determined by elisa and real-time RT-PCR (reverse transcriptase polymerase chain reaction) respectively. Key results: COX2, HA and CD44 were detected immunohistochemically in >90% of human oesophageal tumour samples. Under basal conditions, OSC1 and OSC2 cells express HAS2 and HAS3, COX2 and Galpha(s)-coupled EP(2) and EP(4) PG receptors. Neither stimulation with the PGI(2) analogue, iloprost, addition of exogenous PGE(2) nor forskolin induced HAS1 or HAS2 mRNA expression in OSC1 and OSC2 cells. Furthermore, in HeLa cells after induction of COX2 by tumour necrosis factor alpha and subsequent PGE(2) release, inhibition of COX2 by etoricoxib did not affect HAS expression or HA secretion. Conclusions and implications: We conclude that in oesophageal and HeLa cancer cells, HAS1/2 expression was not responsive to the PG/cAMP pathway.
MeSH term(s)	Base Sequence ; Carcinoma, Squamous Cell/enzymology ; Carcinoma, Squamous Cell/metabolism ; Carcinoma, Squamous Cell/pathology ; Cell Line, Tumor ; Cyclic AMP/metabolism ; Cyclooxygenase 2/metabolism ; DNA Primers ; Esophageal Neoplasms/enzymology ; Esophageal Neoplasms/metabolism ; Esophageal Neoplasms/pathology ; Humans ; Hyaluronic Acid/biosynthesis ; Immunohistochemistry ; Prostaglandins/metabolism ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	DNA Primers ; Prostaglandins ; Hyaluronic Acid (9004-61-9) ; Cyclic AMP (E0399OZS9N) ; Cyclooxygenase 2 (EC 1.14.99.1)
Language	English
Publishing date	2009-03-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80081-8
ISSN	1476-5381 ; 0007-1188
ISSN (online)	1476-5381
ISSN	0007-1188
DOI	10.1111/j.1476-5381.2009.00138.x
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Article ; Online: The platypnea-orthodeoxia syndrome.

Akin, E / Krüger, U / Braun, P / Stroh, E / Janicke, I / Rezwanian, R / Akin, I / Schöls, W H

European review for medical and pharmacological sciences

2014 Volume 18, Issue 18, Page(s) 2599–2604

Abstract: The platypnea orthodeoxia syndrome (POS) is a rare condition characterized by dyspnea and hypoxia in upright position. Pathopysiologic underlying mechanisms are determined by an atrial right-to-left shunt. Coexisting conditions that evolve POS can be of ... ...

Abstract	The platypnea orthodeoxia syndrome (POS) is a rare condition characterized by dyspnea and hypoxia in upright position. Pathopysiologic underlying mechanisms are determined by an atrial right-to-left shunt. Coexisting conditions that evolve POS can be of anatomical nature causing interatrial communication or of functional nature producing a deformity of the atrial septum in upright position. Diagnosis is difficult, as it needs to mention about POS. Classically, transthoracic and transesophageal echocardiography in supine and upright position with use of contrast medium and/or Doppler will point the diagnosis. Treatment is predominantly carried out by interventional closure of atrial septal defect that promptly resolves clinical symptoms.
MeSH term(s)	Dyspnea/diagnosis ; Dyspnea/physiopathology ; Echocardiography, Transesophageal/methods ; Humans ; Hypoxia/diagnosis ; Hypoxia/physiopathology ; Posture/physiology ; Syndrome
Language	English
Publishing date	2014
Publishing country	Italy
Document type	Journal Article
ZDB-ID	605550-3
ISSN	2284-0729 ; 1128-3602 ; 0392-291X
ISSN (online)	2284-0729
ISSN	1128-3602 ; 0392-291X
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