Axitinib acting as a receptor tyrosine kinase inhibitor could interfere with TGFβR and other growth factor receptors signaling involved in fibrogenesis to inhibit the cascade of Apoptosis Compound Library events leading to fibroblast activation and fibrosis that is triggered by radiation [48]. Alternatively, axitinib may act like sunitinib and inhibit myeloid derived suppressor cells which could be involved

in the inflammatory response caused by radiation [49]. Further studies are warranted to investigate these mechanisms. Overall, our data demonstrate that axitinib is a potent and safe drug to use in conjunction with radiotherapy for lung cancer that could also act as a radioprotector for lung tissue by reducing pneumonitis and fibrosis. This study was supported anti-PD-1 antibody by Pfizer grant IIR # WS832344. We thank Mohit Agarwal for excellent technical assistance. “
“Ovarian cancer is characterized by a multisequential process, which involves multiple gains in cell functions, conferring to the transformed cells the capacity for

increased proliferation and metastasis. These changes are partially mediated by alterations in genetic and protein expression levels, thus allowing for increased cell division, tissue invasion, and cell adhesion as well as colonization in new microenvironments [1]. Among the newest recognized molecular actors involved, the proprotein convertases (PCs) are important in cancer progression through their processing and activation of cancer-associated proteins [2]. Although numerous cancer-associated proteins are likely involved, proprotein processing can still be considered as a limiting step that cancer cells require to gain

their full self-sustaining capabilities [2]. PCs are a family of serine proteases responsible for protein processing within D-malate dehydrogenase the secretory pathway. Nine family members have been identified in mammalian cells, including furin, PACE4, PC1/3, PC2, PC4, PC5/6, PC7, PCSK9, and substilisin-kexin isoenzyme 1 (SKI-1) [3]. Only the first seven PCs cleave their substrates in the C terminus at the R-X-X-R consensus motif. Among these PCs, furin is ubiquitous, whereas PC1/3 and PC2 are categorized as endocrine specific. Despite the well-accepted identity of PC substrates, which are largely known from their consensus cleavage site in their primary sequences, the cleavage specificity among the enzyme family is still fragmentary and remains difficult to establish because the PC catalytic domain is highly conserved [4]. The role of PCs has been described in breast cancer [5], head and neck cancer [6], and recently prostate cancer [7]. Various PC substrates have recognized roles in cell growth, tumor angiogenesis, invasion, and metastasis, including secreted growth factors, matrix metalloproteinases, and adhesion molecules [8].