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Apoptosis is a major pathophysiological change following myocardial ischemia/reperfusion (I/R) injury. Glucagon-like peptide 1 (GLP-1) and its receptor GLP-1R are widely expressed in the cardiovascular system and GLP-1/GLP-1R activates the protein kinase G (PKG)-related signaling pathway. Therefore, this study tested whether semaglutide, a new GLP-1 analog, inhibits I/R injury-induced cardiomyocyte apoptosis by activating the PKG/PKCε/ERK1/2 pathway. We induced myocardial I/R injury in rats and hypoxia/reoxygenation (H/R) injury in H9C2 cells and detected the effects of semaglutide, a PKG analog (8-Br-cGMP), and a PKG inhibitor (KT-5823) on the PKG/PKCε/ERK1/2 pathway and cardiomyocyte apoptosis. We found that semaglutide upregulated GLP-1R levels, and both semaglutide and 8-Br-cGMP activated the PKG/PKCε/ERK1/2 pathway, inhibited myocardial infarction (MI), decreased hs-cTNT levels, increased NT-proBNP levels, and suppressed cardiomyocyte apoptosis in I/R rats and H/R H9C2 cells. However, KT-5823 exerted contrasting effects with semaglutide and 8-Br-cGMP, and KT-5823 weakened the cardioprotective effects of semaglutide. In conclusion, semaglutide inhibits I/R injury-induced cardiomyocyte apoptosis by activating the PKG/PKCε/ERK1/2 pathway. The beneficial effect of GLP-1/GLP-1R, involved in the activation of the PKG/PKCε/ERK1/2 pathway, may provide a novel treatment method for myocardial I/R injury. • Semaglutide could increase GLP-1R level in the ischemic/reperfusion rats and hypoxia/reoxygenation H9C2 cells. • Both semaglutide and 8-Br-cGMP play a protective role in the ischemic/reperfusion rats and hypoxia/reoxygenation H9C2 cells. • KT-5823 could weaken the cardioprotective effects of semaglutide. [ABSTRACT FROM AUTHOR]

Abstract: We have generated a quantitative transcription profile of human bocavirus type 1 (HBoV1) by transfecting a nearly full-length clone in human lung epithelial A549 cells as well as in a replication competent system in 293 cells. The overall transcription profile of HBoV1 is similar to that of two other members of genus Bocavirus, minute virus of canines and bovine parvovirus 1. In particular, a spliced NS1-transcript that was not recognized previously expressed the large non-structural protein NS1 at approximately 100kDa; and the NP1-encoding transcripts were expressed abundantly. In addition, the protein expression profile of human bocavirus type 2 (HBoV2) was examined in parallel by transfection of a nearly full-length clone in A549 cells, which is similar to that of HBoV1. Moreover, our results showed that, unlike human parvovirus B19 infection, expression of the HBoV1 proteins only does not induce cell cycle arrest and apoptosis of A549 cells. [Copyright &y& Elsevier]