Interventions about physical activity and diet and their impact on adolescent and young adult cancer survivors: a Prisma systematic review.

PURPOSE: Over the past few decades, the incidence of cancer among adolescents and young adults (AYA) has been increasing. The impact of behaviors, such as physical activity (PA) and nutrition, on disease progression, prognosis, and overall health and quality of life for AYA cancer survivors is of significant importance. This systematic review aims to evaluate the effectiveness of PA and diet interventions for AYA cancer survivors and to critically evaluate existing literature, gaps, and limitations. METHODS: A search of literature was conducted in PubMed, Science Direct, Scopus, and Google Scholar following the PRISMA guidelines. Twenty-two studies were included from online databases from 2012 to 2022, 13 of which were randomized controlled trials. RESULTS: Most interventions were related to PA, with only four studies including nutrition or Diet interventions. The interventions were generally feasible and acceptable to AYA cancer survivors, and digitally based PA interventions were commonly used. PA interventions mainly comprised aerobic and resistance training and were individualized. Overall, this review found various PA and diet interventions for AYA cancer survivors that were feasible and well-accepted, but gaps in knowledge and design still exist. CONCLUSIONS: This systematic review underscores the importance of conducting more research on diet interventions for YCS. PROSPERO REGISTRATION: https://www.crd.york.ac.uk/prospero/#aboutregpage.

Enteric bacteria counteract lipopolysaccharide induction of antimicrobial peptide genes.

The humoral immunity of Drosophila involves the production of antimicrobial peptides, which are induced by evolutionary conserved microbial molecules, like LPS. By using Drosophila mbn-2 cells, we found that live bacteria, including E. coli, Salmonella typhimurium, Erwinia carotovora, and Pseudomonas aeruginosa, prevented LPS from inducing antimicrobial peptide genes, while Micrococcus luteus and Streptococcus equi did not. The inhibitory effect was seen at bacterial levels from 20 per mbn-2 cell, while antimicrobial peptides were induced at lower bacterial concentrations (< or =2 bacteria per cell) also in the absence of added LPS. Gel shift experiment suggests that the inhibitory effect is upstream or at the level of the activation of the transcription factor Relish, a member of the NF-kappaB/Rel family. The bacteria have to be in physical contact with the cells, but not phagocytosed, to prevent LPS induction. Interestingly, the inhibiting mechanism is, at least for E. coli, independent of the type III secretion system, indicating that the inhibitory mechanism is unrelated to the one earlier described for YopJ from Yersinia.

A Drosophila IkappaB kinase complex required for Relish cleavage and antibacterial immunity.

Here we report the identification of a Drosophila IkappaB kinase complex containing DmIKKbeta and DmIKKgamma, homologs of the human IKKbeta and IKKgamma proteins. We show that this complex is required for the signal-dependent cleavage of Relish, a member of the Rel family of transcriptional activator proteins, and for the activation of antibacterial immune response genes. In addition, we find that the activated DmIKK complex, as well as recombinant DmIKKbeta, can phosphorylate Relish in vitro. Thus, we propose that the Drosophila IkappaB kinase complex functions, at least in part, by inducing the proteolytic cleavage of Relish. The N terminus of Relish then translocates to the nucleus and activates the transcription of antibacterial immune response genes. Remarkably, this Drosophila IkappaB kinase complex is not required for the activation of the Rel proteins Dif and Dorsal through the Toll signaling pathway, which is essential for antifungal immunity and dorsoventral patterning during early development. Thus, a yet to be identified IkappaB kinase complex must be required for Rel protein activation via the Toll signaling pathway.

Activation of the Drosophila NF-kappaB factor Relish by rapid endoproteolytic cleavage.

The Rel/NF-kappaB transcription factor Relish plays a key role in the humoral immune response in Drosophila. We now find that activation of this innate immune response is preceded by rapid proteolytic cleavage of Relish into two parts. An N-terminal fragment, containing the DNA-binding Rel homology domain, translocates to the nucleus where it binds to the promoter of the Cecropin A1 gene and probably to the promoters of other antimicrobial peptide genes. The C-terminal IkappaB-like fragment remains in the cytoplasm. This endoproteolytic cleavage does not involve the proteasome, requires the DREDD caspase, and is different from previously described mechanisms for Rel factor activation.

Drosophila salivary glands exhibit a regional reprogramming of gene expression during the third larval instar.

In D. virilis salivary glands transcripts of two early gland protein genes, Egp-1 and Egp-2, which encode putative secretory proteins, accumulate in all cells from the first to mid third larval instar. Subsequently the transcripts disappear from the cytoplasm of the corpus cells, but not from their nuclei, where they accumulate at the chromosomal site of their synthesis. In the collum cells, however, Egp-transcripts continue to be detectable in the cytoplasm until the end of larval life. In the salivary glands of transgenic D. melanogaster the presence of a Egp-1/lacZ fusion protein shows the same regional shift as the cytoplasmic Egp-transcripts in D. virilis. We predict that the expression of Egp-genes is related to an early secretory function of the larval salivary glands which is executed by all cells during earlier larval stages but becomes restricted exclusively to the collum cells during the third larval instar.