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12. Brown HK, Ottewell PD, Evans CA, Coleman RE, Holen I. A single administration of combination therapy inhibits breast tumour progression in bone and modifies both osteoblasts and osteoclasts. J Bone Oncol 2012;1:47-56.
15. Ottewell PD, Lefley DV, Cross SS, Evans CA, Coleman RE, et al. Sustained inhibition of tumor growth and prolonged survival following sequential administration of doxorubicin and zoledronic acid in a breast cancer model. Int J Cancer 2010;126:522-32.
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This annual report template has five main sections for a foreword, quick facts, contribution and upcoming projects. The data visualization on the pages is minimal, with the spirit of showing qualitative data more than quantitative.
Disturbed calcium cycling plays a major role in the pathogenesis of DOX-induced cardiomyopathy [12]. DOX alters deleteriously the expression of many genes specific for cardiac calcium handling including ryanodine receptor (RyR2), sarcoplasmic reticulum Ca2+ ATPase (Serca2a), and phospholamban (Pln), a SERCA2a inhibitor [12,13,14]. DOX leads to decreased Serca2a expression thus inhibiting SERCA2a pump, decreases RyR2 expression, and induces inappropriate opening of the ryanodine receptors [12, 15, 16]. In the failing heart, a decrease in SERCA2a expression and activity results in myocardial dysfunction due to diminished calcium uptake and release by sarcoplasmic reticulum [17]. Y-receptor activation inhibits adenylate cyclase and decreases cAMP/PKA stimulation of L-type Ca2+ currents. On the other hand, Y1-receptor has been shown to couple also to Gq protein to modulate calcium transients [18] and increase intracellular Ca2+ level [19, 20] in cardiomyocytes. Thus, NPY could have an impact on the disturbed calcium handling induced by DOX.
DOX treatment with the dosing regimen used in the study, consisting of a single intraperitoneal injection at a dose of 20 mg/kg, induced a tendency of decrease in ejection fraction suggesting impaired heart function, but did not lead to severe heart failure as indicated by e.g., unchanged lung and liver weights. However, it affected the general well-being of the animals as weight gain and fat mass gain were significantly hampered, which fits with the previous reports using different doses of DOX [40,41,42,43,44,45]. Furthermore, higher expression of the rate-limiting enzyme of noradrenaline synthesis (Th) suggested that cardiac SNS activity was increased in DOX-treated mice, and the result fits with previous work showing DOX to upregulate TH protein level and linking DOX-induced cardiomyopathy to increased SNS activity [3, 4, 46]. On molecular level, DOX affected several previously well-described mechanisms of DOX-induced cardiotoxicity including decreases in the expression of genes involved in intracellular calcium metabolism, Serca2a and RyR2 [13, 14, 16] and increases in Anp and Mmp2 levels, consistent with observations in the human heart failure [47,48,49,50]. DOX-treated mice tended to have lower left ventricular mass in echocardiography and this was supported by the heart weights. Fitting with this, increased Mmp2 expression points to cellular level activation of degradation of structural proteins. Although heart weights or histology did not reveal myocyte hypertrophy, increased Anp indicates that the cellular mechanisms driving hypertrophy were recruited. The histology revealed hypertrophy of the myocardial cell nuclei, cytoplasmic degeneration, and mild fibrosis in DOX-treated animals, even though the statistical significance was lacking. However, these findings are supported by previous reports of DOX treatment leading to cardiomyocyte disorganization and myofibrillar loss [40, 43, 44, 51, 52]. Thus, the DOX administration protocol used in the current study did not induce severe heart failure during the study period, but led to significant cardiotoxicity, resulting in a decline in the general condition of the mice, a slight decline in the myocardial function and mass, and affecting several well-described components of DOX-induced cardiotoxicity.
Cardiomyocytes were seeded in 25-mm coverslips after incubation with Dox for 24 h. The cells were loaded with Fura 2-AM (2 μmol/L) in Krebs solution (in mmol/L: 119 NaCl, 2.5 KCl, 1 NaH2PO4, 1.3 MgCl2, 20 HEPES, 11 glucose, 0.5 EGTA, pH 7.4) for 30 min at 37°C. Tg (1 μmol/L) was used to deplete Ca2+ stores followed by the addition of 1.8 μmol/L of Ca2+. [Ca2+]i was analyzed with Cell^R software when examined using a model IX81 wide-field inverted microscope (Olympus, Tokyo, Japan) at wavelengths of 340 nm and 380 nm. The average fluorescence was calculated by counting 10 random fields (20 cells in each field) per group in six independent experiments.
Cardiomyocyte apoptosis was measured by the TUNEL assay using an In Situ Cell Death Detection kit (Roche, Mannheim, Germany). The frozen sections were incubated with primary antibody against α-actinin overnight at 4°C, followed by incubation with Cy3-labeled secondary antibody (Invitrogen) for 1 h at room temperature. The sections were incubated with TUNEL reaction mixture for 1 h at 37°C in the dark. 4ʹ,6-Diamidino-2-phenylindole (DAPI) staining was performed for total nuclei quantification. Images were observed and captured using a model LSM710 confocal microscope (Zeiss Microsystems, Mannheim, Germany). The percentage of TUNEL-positive cells (green fluorescence) in the total cells of the cross-sectional area was used to quantify cardiomyocyte apoptosis using ImageJ software (NIH).
To determine the function of SOCCs in cardiotoxicity, we initially examined whether the expression of SOCCs was altered in the myocardium in response to Dox treatment. Although the expression of Orai1 and Trpc1 was unchanged in the myocardium of mice treated with Dox for 14 days, a marked decrease in Stim1 expression was observed in Dox-treated mice when compared with vehicle-treated mice (Figures 1A and S1A). Interestingly, Dox administration did not alter the mRNA levels of Stim1 in the myocardium, suggesting the involvement of post-translational regulation by Dox (Figure S1B). In addition, when cardiomyocytes were treated with Dox for different time periods, STIM1 protein expression was gradually decreased by Dox. This finding further supported the in vivo results (Figure 1B). STIM1 is a key Ca2+ movement regulator that interacts with ORAI1 and TRPC1 upon store depletion to initiate Ca2+ entry via SOCE.22,23 Therefore, we investigated the functional interaction between Stim1 and Orai1 or Trpc1. Immunoprecipitation results showed that Dox treatment led to a sharp decrease in the binding of Stim1 to Orai1 and Trpc1 in myocardial tissues (Figure 1C and D). Given the importance of STIM1 expression and its interaction with ORAI1 or TRPC1, we next investigated whether SOCE was altered by Dox in cardiomyocytes. In the absence of extracellular Ca2+, the thapsigargin (Tg)-induced increase in store Ca2+ release (first peak) was inhibited by Dox treatment. Furthermore, SOCE induced by the addition of 2 mmol/L extracellular Ca2+ was also inhibited by Dox treatment (Figure 1E and F). Importantly, Dox treatment significantly decreased store-operated Ca2+ currents in cardiomyocytes (Figure 1G and H). Taken together, these results indicate that Dox inhibits Ca2+ release and SOCE, at least in part by decreasing STIM1 expression and its interaction with ORAI1 or TRPC1.Figure 1 Dox treatment reduces Stim1 expression and SOCE in cardiomyocytes. (A) Western blotting analysis of Stim1 expression in myocardium of mice after vehicle or Dox treatment for 14 days. **P 2b1af7f3a8