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1
Advantages of Azithromycin Over Erythromycin in Improving the Gastric Emptying Half-Time in Adult Patients With Gastroparesis

( Jean M Larson ),( Anna Tavakkoli ),( Walter E Drane ),( Phillip P Toskes ),( Baharak Moshiree ) 대한소화관운동학회 2010 Journal of Neurogastroenterology and Motility (JNM Vol.16 No.4
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Background/Aims Current therapy for gastroparesis with prokinetic agents is limited by options and side effects. One macrolide, erythromycin (ERY), is associated with possible sudden cardiac death from QT prolongation due to P450 iso-enzyme inhibition. An alternative, azithromycin (AZI), lacks P450 inhibition. We compared the effect on gastric emptying half-times (t½) between AZI and ERY in patients diagnosed with gastroparesis by gastric emptying scintigraphy. Methods Patients stopped medications known to affect gastric emptying prior to the study, and then ingested 1 scrambled egg meal labeled with 18.5-37 MBq of technetium-99m sulfur colloid followed by continuous imaging for 120 minutes, at 1 minute per frame. A simple linear fit was applied to the rate of gastric emptying, and gastric emptying t½ was calculated (normal =45-90 minutes). At 75-80 minutes, if the stomach had clearly not emptied, patients were given either ERY (n=60) or AZI (n=60) 250 mg IV and a new post-treatment gastric emptying t½ was calculated. Results Comparison of gastric emptying t½ showed a similar positive effect (mean gastric emptying t½ for AZI=10.4±7.2 minutes; mean gastric emptying t½ for ERY=11.9±8.4 minutes; p=0.30). Conclusions AZI is equivalent to ERY in accelerating the gastric emptying of adult patients with gastroparesis. Given the longer duration of action, better side effect profile and lack of P450 interaction for AZI as compared with ERY, further research should evaluate the long term effectiveness and safety of AZI as a gastroparesis treatment. (J Neurogastroenterol Motil 2010;16:407-413)
2
Dephosphorylation Enables the Recruitment of 53BP1 to Double-Strand DNA Breaks

Lee, D.H.,Acharya, Sanket S.,Kwon, M.,Drane, P.,Guan, Y.,Adelmant, G.,Kalev, P.,Shah, J.,Pellman, D.,Marto, Jarrod A.,Chowdhury, D. Cell Press 2014 Molecular cell Vol.54 No.3
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Excluding 53BP1 from chromatin is required to attenuate the DNA damage response during mitosis, yet the functional relevance and regulation of this exclusion are unclear. Here we show that 53BP1 is phosphorylated during mitosis on two residues, T1609 and S1618, located in its well-conserved ubiquitination-dependent recruitment (UDR) motif. Phosphorylating these sites blocks the interaction of the UDR motif with mononuclesomes containing ubiquitinated histone H2A and impedes binding of 53BP1 to mitotic chromatin. Ectopic recruitment of 53BP1-T1609A/S1618A to mitotic DNA lesions was associated with significant mitotic defects that could be reversed by inhibiting nonhomologous end-joining. We also reveal that protein phosphatase complex PP4C/R3β dephosphorylates T1609 and S1618 to allow the recruitment of 53BP1 to chromatin in G1 phase. Our results identify key sites of 53BP1 phosphorylation during mitosis, identify the counteracting phosphatase complex that restores the potential for DDR during interphase, and establish the physiological importance of this regulation.