{"title":"Potential negative effect of total parenteral nutrition on the human circadian clock.","authors":"Muneto Tatsumoto, Ritsuko Matsumura, Takuyuki Endo, Isao T Tokuda, Koichi Node, Makoto Akashi","doi":"10.1111/gtc.12976","DOIUrl":"https://doi.org/10.1111/gtc.12976","url":null,"abstract":"<p><p>When patients cannot eat on their own, total parenteral nutrition (TPN) is a clinically beneficial method of maintaining nutrition. However, many animal studies have demonstrated that circadian rhythms are strongly affected by feeding time, raising the concern that continuous TPN around the clock may have an unexpected negative impact on the circadian clock of patients. To investigate this concern, we compared clock gene expression of aged subjects with or without TPN using hair follicle cells and found that while none of the non-TPN subjects showed any obvious defects in circadian rhythms of peripheral clock gene expression, a portion of aged subjects receiving continuous TPN showed abnormal circadian rhythms in peripheral clocks. Continuous TPN around the clock may therefore potentially perturb peripheral circadian rhythms, giving rise to the proposal that TPN needs to be administered with consideration to time factors.</p>","PeriodicalId":520630,"journal":{"name":"Genes to cells : devoted to molecular & cellular mechanisms","volume":" ","pages":"613-620"},"PeriodicalIF":2.1,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40532054","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Piyali Sen, Annushree Kurmi, Suvendra Kumar Ray, Siddhartha Sankar Satapathy
{"title":"Machine learning approach identifies prominent codons from different degenerate groups influencing gene expression in bacteria.","authors":"Piyali Sen, Annushree Kurmi, Suvendra Kumar Ray, Siddhartha Sankar Satapathy","doi":"10.1111/gtc.12977","DOIUrl":"https://doi.org/10.1111/gtc.12977","url":null,"abstract":"<p><p>Unequal usage of synonymous codons is known as codon usage bias (CUB), which is generally different between the high-expression genes (HEG) and low-expression genes (LEG) in organisms is not yet adequately reported across different bacteria. In this study, a machine learning-based approach was implemented initially to find out codons that are significantly different between the HEG and LEG in Escherichia coli. It identified Cys codons such as UGU and UGC, Lys codons such as AAA and AAG that were least influenced by gene expression. Codons such as UCU (Ser), CUG (Leu), GGG (Gly), CGG (Arg) etc. were identified to be influenced maximum by the gene expression. The study was extended to analyze codon usage in 683 other bacterial species. Cys (UGU/UGC) and Ser (AGU/AGC) codons were identified being the least different between the two groups of genes across these bacterial species. Codons such as CGA, CUG, GGG, GCC, ACC, AUA, and AUC were identified to be influenced by the gene expression across majority of these species. This study supports the role of CUB on gene expression across bacteria and demonstrates a commonality among bacteria regarding behavior of certain codons with regard to gene expression.</p>","PeriodicalId":520630,"journal":{"name":"Genes to cells : devoted to molecular & cellular mechanisms","volume":" ","pages":"591-601"},"PeriodicalIF":2.1,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40419547","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Involvement of the centrosomal protein 55 (cep55) gene in zebrafish head formation.","authors":"Kanoko Yanagi, Ryota Sone, Rie Ohga, Atsuo Kawahara","doi":"10.1111/gtc.12715","DOIUrl":"https://doi.org/10.1111/gtc.12715","url":null,"abstract":"<p><p>Mammalian CEP55 (centrosomal protein 55 kDa) is a coiled-coil protein localized to the centrosome in interphase cells and is required for cytokinesis. A homozygous non-sense mutation in human CEP55 has been recently identified in perinatal lethal MARCH (multinucleated neurons, anhydramnios, renal dysplasia, cerebellar hypoplasia and hydranencephaly) syndrome. We have isolated zebrafish cep55 mutants defective in head morphology. The zebrafish cep55 gene was expressed in the head including the retina and the pectoral fin at 1 day post-fertilization (dpf), and extensive cell death was widely observed in the head and tail of the cep55 mutant. In the cep55 mutant, the anterior-posterior distance of the ventral pharyngeal arches was short, and retinal lamination was disorganized. Neural cells, such as islet1-positive cells and pax2-positive cells, and fli1b-positive vascular cells were reduced in the head of the cep55 mutant. Thus, we propose that the zebrafish cep55 mutant is a model organism for human MARCH syndrome.</p>","PeriodicalId":520630,"journal":{"name":"Genes to cells : devoted to molecular & cellular mechanisms","volume":" ","pages":"642-649"},"PeriodicalIF":2.1,"publicationDate":"2019-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/gtc.12715","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40452368","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"miR-214 and hypoxia down-regulate Necl-2/CADM1 and enhance ErbB2/ErbB3 signaling.","authors":"Kenji Momose, Akihiro Minami, Yohei Shimono, Kiyohito Mizutani, Kentaro Nobutani, Takeshi Azuma, Yoshimi Takai","doi":"10.1111/gtc.12027","DOIUrl":"https://doi.org/10.1111/gtc.12027","url":null,"abstract":"<p><p>Necl-2/CADM1 is down-regulated by the promoter hypermethylation and/or the loss of heterozygosity at chromosome 11q23.2 in many types of cancers and serves as a tumor suppressor by interacting in cis with ErbB3 and suppressing the ligand-induced ErbB2/ErbB3 signaling for cell movement and death. However, the incidence of these epigenetic and genetic abnormalities of Necl-2 is 30-60% in these cancers. We investigated here other mechanisms that down-regulate Necl-2. miR-214, that is frequently up-regulated in a variety of cancers, targeted the 3'UTR of the Necl-2 mRNA directly, suppressed the translation of Necl-2 and enhanced the ligand-induced ErbB2/ErbB3 signaling in human colon cancer Caco-2 cells. Hypoxia reduced the Necl-2 protein level in a manner independent of miR-214 or hypoxia-inducible factor-1α in Caco-2 cells. These results indicate that miR-214 and hypoxia are novel regulators that down-regulate Necl-2 and enhance ErbB2/ErbB3 signaling.</p>","PeriodicalId":520630,"journal":{"name":"Genes to cells : devoted to molecular & cellular mechanisms","volume":" ","pages":"195-202"},"PeriodicalIF":2.1,"publicationDate":"2013-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/gtc.12027","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40222110","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Motohiko Takenaka, Hideki Inoue, Atsushi Takeshima, Tomonori Kakura, Toshiyuki Hori
{"title":"C. elegans Rassf homolog, rasf-1, is functionally associated with rab-39 Rab GTPase in oxidative stress response.","authors":"Motohiko Takenaka, Hideki Inoue, Atsushi Takeshima, Tomonori Kakura, Toshiyuki Hori","doi":"10.1111/gtc.12028","DOIUrl":"https://doi.org/10.1111/gtc.12028","url":null,"abstract":"<p><p>The Ras association domain family (Rassf) is one of the Ras effectors, which can bind to several GTP-charged Ras-like GTPases. The Rassf proteins are widely conserved beyond species from nematode to human. To explore the novel functions of Rassf proteins, we took advantage of nematode C. elegans as a model animal with only one Rassf homolog, T24F1.3 (rasf-1). The rasf-1-mutant as well as rasf-1-knockdown animals were found to be more sensitive to oxidative stress of arsenite than in wild type, indicating that rasf-1 is involved in oxidative stress response. We next screened for proteins that interact with RASF-1 by the yeast two-hybrid system and identified RAB-39 Rab GTPase as an interacting partner of RASF-1. We not only confirmed specific binding between these molecules but also demonstrated that RASF-1 binds to GTP-bound form but not GDP-bound form of RAB-39. Importantly, rab-39 mutant animals were also sensitive to oxidative stress, which was dependent on rasf-1 according to the epistasis analysis. Moreover, Rassf1 and Rab39, mammalian homologs of rasf-1 and rab-39, respectively, were shown to interact with each other in vitro. These results indicate that the RASF-1 functionally interacts with RAB-39 and that the interaction between their homologs is conserved in mammals.</p>","PeriodicalId":520630,"journal":{"name":"Genes to cells : devoted to molecular & cellular mechanisms","volume":" ","pages":"203-10"},"PeriodicalIF":2.1,"publicationDate":"2013-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/gtc.12028","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40216414","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Transcriptionally active nuclei are selective in mature multinucleated osteoclasts.","authors":"Min-Young Youn, Ichiro Takada, Yuuki Imai, Hisataka Yasuda, Shigeaki Kato","doi":"10.1111/j.1365-2443.2010.01441.x","DOIUrl":"https://doi.org/10.1111/j.1365-2443.2010.01441.x","url":null,"abstract":"<p><p>Multinucleation is indispensable for the bone-resorbing activity of mature osteoclasts. Although multinucleation is evident in mature osteoclasts and certain other cell types, putative regulatory networks among nuclei remain poorly characterized. To address this issue, transcriptional activity of each nucleus in a multinucleated osteoclast was assessed by detecting the distributions of nuclear proteins by immunocytochemistry and primary transcripts by RNA FISH. Patterns of epigenetic histone markers governing transcription as well as localization of tested nuclear receptor proteins appeared indistinguishable among nuclei in differentiated Raw264 cells and mouse mature osteoclasts. However, RNAPII-Ser5P/2P and NFATc1 proteins were selectively distributed in certain nuclei in the same cell. Similarly, the distributions of primary transcripts for osteoclast-specific genes (Nfatc1, Ctsk and Acp5) as well as a housekeeping gene (beta-tubulin) were limited in certain nuclei within individual cells. By fusing two Raw264 cell lines that stably expressed ZsGreen-NLS and DsRed-NLS proteins, transmission of nuclear proteins across all of the nuclei in a cell could be observed, presumably through the shared cytoplasm. Taken together, we conclude that although nuclear proteins are diffusible among nuclei, only certain nuclei within a multinucleated osteoclast are transcriptionally active.</p>","PeriodicalId":520630,"journal":{"name":"Genes to cells : devoted to molecular & cellular mechanisms","volume":" ","pages":"1025-35"},"PeriodicalIF":2.1,"publicationDate":"2010-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1365-2443.2010.01441.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40060784","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}