Yu-Dong Cai , Xiao-Jun Liu , Xue-biao Xu , Kuo-Chen Chou
{"title":"Support Vector Machines for Prediction of Protein Subcellular Location","authors":"Yu-Dong Cai , Xiao-Jun Liu , Xue-biao Xu , Kuo-Chen Chou","doi":"10.1006/mcbr.2001.0285","DOIUrl":"https://doi.org/10.1006/mcbr.2001.0285","url":null,"abstract":"<div><p>Support Vector Machine (SVM), which is one kind of learning machines, was applied to predict the subcellular location of proteins from their amino acid composition. In this research, the proteins are classified into the following 12 groups: (1) chloroplast, (2) cytoplasm, (3) cytoskeleton, (4) endoplasmic reticulum, (5) extracall, (6) Golgi apparatus, (7) lysosome, (8) mitochondria, (9) nucleus, (10) peroxisome, (11) plasma membrane, and (12) vacuole, which have covered almost all the organelles and subcellular compartments in an animal or plant cell. The examination for the self-consistency and the jackknife test of the SVMs method was tested for the three sets: 2022 proteins, 2161 proteins, and 2319 proteins. As a result, the correct rate of self-consistency and jackknife test reaches 91 and 82% for 2022 proteins, 89 and 75% for 2161 proteins, and 85 and 73% for 2319 proteins, respectively. Furthermore, the predicting rate was tested by the three independent testing datasets containing 2240 proteins, 2513 proteins, and 2591 proteins. The correct prediction rates reach 82, 75, and 73% for 2240 proteins, 2513 proteins, and 2591 proteins, respectively.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 4","pages":"Pages 230-233"},"PeriodicalIF":0.0,"publicationDate":"2000-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0285","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90002236","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":"Complexes Formation between Insulin Receptor and Extracellular Signal-Regulated Kinases ERKs","authors":"Yea-Lih Lin , Clément Mettling , Chen-Kung Chou","doi":"10.1006/mcbr.2001.0286","DOIUrl":"10.1006/mcbr.2001.0286","url":null,"abstract":"<div><p>A property of signal transduction pathways that might explain their efficiency and specificity is the formation of signaling complexes. The recent demonstration that adaptor proteins can interact with many components of the extracellular signal-regulated kinases (ERKs) signaling cascade leads us to investigate whether such complexes may include the transmembrane receptor. The present work shows that in human hepatoma Hep3B cells, insulin receptor (IR) can be coimmunoprecipitated with other components of the ERKs cascade: insulin receptor substrate (IRS), Raf-1, and ERKs. Furthermore, these complexes formed near the cytoplasmic membrane even prior to insulin stimulation.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 4","pages":"Pages 234-238"},"PeriodicalIF":0.0,"publicationDate":"2000-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0286","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80529833","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}
M. Sukhai, A. Yong, J. Kalitsky, M. Piquette-Miller
{"title":"Inflammation and interleukin-6 mediate reductions in the hepatic expression and transcription of the mdr1a and mdr1b Genes.","authors":"M. Sukhai, A. Yong, J. Kalitsky, M. Piquette-Miller","doi":"10.1006/MCBR.2001.0288","DOIUrl":"https://doi.org/10.1006/MCBR.2001.0288","url":null,"abstract":"In order to elucidate the mechanisms involved in the downregulation of mdr 1 gene expression reported in experimentally-induced inflammation, we examined the effects of experimentally-induced inflammation and interleukin-(IL-) 6 on transcriptional control of the mdr1 genes in rats. RNA, nuclear extracts, and nuclear protein fractions were isolated from livers harvested from saline or turpentine-treated male Sprague-Dawley rats or from IL-6 treated or nontreated (controls) cultured rat hepatocytes. mdr gene expression and regulation was examined by RT-PCR, mRNA stability studies, nuclear run-on analysis of transcription, and gel shift analysis of promoter-transcription factor interaction. As compared to controls, significantly lower levels of mdr1a and mdr1b mRNA and significantly decreased mdr1a and mdr1b transcription rates were observed in livers isolated from the turpentine-treated rats. In vitro treatments of cultured hepatocytes with IL-6 also suppressed mdr1a and mdr1b mRNA expression and imposed similar reductions in mdr1a and mdr1b transcriptional activity. Significant effects of IL-6 on mdr1 mRNA stability were not seen. Our results indicate that reductions in mdr1 expression in experimental models of inflammation likely occurs through altered gene transcription. Furthermore, as IL-6 was found to decrease mdr1 expression and gene transcription rates in vitro, this cytokine is likely involved in the reduction of mdr1 expression that is seen in vivo during an acute inflammatory response.","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"58 1","pages":"248-56"},"PeriodicalIF":0.0,"publicationDate":"2000-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83949448","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":"Genetic and Molecular Mechanisms of Cell Size Control","authors":"Jacques Montagne","doi":"10.1006/mcbr.2001.0284","DOIUrl":"https://doi.org/10.1006/mcbr.2001.0284","url":null,"abstract":"<div><p>Since the discovery of the cell as the minimal indivisible living entity, scientists have tried to understand how all the various physiological aspects were assumed within this single functional unit. One fascinating question concerns the role of cell size and cell number in determining the overall size of an organism. During the past century, increasing knowledge in molecular genetics has allowed the characterization of a number of molecular events that influence the size of a cell. However, in spite of recent progress, precise molecular mechanisms governing cell size remain unclear. Although the existence of a master regulator is still possible, cell size may be primarily controlled by an interactive network linking gene expression with translational capacity and cell proliferation.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 4","pages":"Pages 195-202"},"PeriodicalIF":0.0,"publicationDate":"2000-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0284","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91635267","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":"Oligomeric Status of the Dihydropyridine Receptor in Aged Skeletal Muscle","authors":"Michelle Ryan , Bruce M. Carlson , Kay Ohlendieck","doi":"10.1006/mcbr.2001.0282","DOIUrl":"https://doi.org/10.1006/mcbr.2001.0282","url":null,"abstract":"<div><p>A prominent feature of aging is represented by a decrease in muscle mass and strength. Abnormalities in Ca<sup>2+</sup>-regulatory membrane complexes are involved in many muscular disorders. In analogy, we determined potential age-related changes in a key component of excitation-contraction coupling, the dihydropyridine receptor. Immunoblotting of the microsomal fraction from aged rabbit muscle revealed a drastic decline in the voltage-sensing α<sub>1</sub>-subunit of this transverse-tubular receptor, but only marginally altered expression of its auxiliary α<sub>2</sub>-subunit and the Na<sup>+</sup>/K<sup>+</sup>-ATPase. A shift to slower fibre type characteristics was indicated by an age-related increase in the slow calsequestrin isoform. Chemical crosslinking analysis showed that the triad receptor complex has a comparable tendency of protein–protein interactions in young and aged muscles. Hence, a reduced expression and not modified oligomerization of the principal dihydropyridine receptor subunit might be involved in triggering impaired triadic signal transduction and abnormal Ca<sup>2+</sup>-homeostasis resulting in a progressive functional decline of skeletal muscles.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 4","pages":"Pages 224-229"},"PeriodicalIF":0.0,"publicationDate":"2000-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0282","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91635131","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":"Interactions between Phosphatidylinositol 3-Kinase and Nitric Oxide: Explaining the Paradox","authors":"Karen L. Wright, Stephen G. Ward","doi":"10.1006/mcbr.2001.0289","DOIUrl":"https://doi.org/10.1006/mcbr.2001.0289","url":null,"abstract":"","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 4","pages":"Pages 257-258"},"PeriodicalIF":0.0,"publicationDate":"2000-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0289","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91635271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Author Index for Volume 4, Number 4","authors":"","doi":"10.1006/mcbr.2001.0292","DOIUrl":"https://doi.org/10.1006/mcbr.2001.0292","url":null,"abstract":"","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 4","pages":"Page iii"},"PeriodicalIF":0.0,"publicationDate":"2000-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0292","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91635272","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":"Interactions between Phosphatidylinositol 3-Kinase and Nitric Oxide: Explaining the Paradox","authors":"Karen L. Wright, Stephen G. Ward","doi":"10.1006/mcbr.2001.0273","DOIUrl":"10.1006/mcbr.2001.0273","url":null,"abstract":"<div><p>Nitric oxide (NO) and the many derivatives and reactive oxygen intermediates thereof are all molecules that are utilised by mammalian cells in the war against microbial pathogens and tumours. They are potentially toxic molecules and, with damage control being crucial, the production and metabolism of nitric oxide is a tightly regulated process. The duality of NO is well documented. On the one hand, beneficial effects include normal healing in the skin and intestinal mucosa, killing of certain bacteria, regulating T cell proliferation and differentiation (Th1 vs Th2), and regulating leukocyte recruitment, by affecting adhesion molecule expression. On the other hand, persistent high levels of NO can lead to the production of toxic metabolites (peroxynitrite and hydroxyls), which can have detrimental effects, such as increased microvascular and epithelial permeability, increased oxidative stress (which can damage DNA), and damage to iron–sulphur proteins in mitochondria. NO has been reported to modulate its own production and the mechanisms involved in this self-regulation are being hotly pursued. The purpose of this review is to update recent intriguing advances in our understanding of the interaction of the phosphatidylinositol (PI) 3-kinase-dependent signal transduction pathway in regulating the activity of the enzymes that generate NO, namely, the nitric oxide synthases.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 3","pages":"Pages 137-143"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0273","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82002181","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}
Gijs R. van den Brink , Tom O'Toole , James C.H. Hardwick, Daniëlle E.M. van den Boogaardt, Henri H. Versteeg, Sander J.H. van Deventer, Maikel P. Peppelenbosch
{"title":"Leptin Signaling in Human Peripheral Blood Mononuclear Cells, Activation of p38 and p42/44 Mitogen-Activated Protein (MAP) Kinase and p70 S6 Kinase","authors":"Gijs R. van den Brink , Tom O'Toole , James C.H. Hardwick, Daniëlle E.M. van den Boogaardt, Henri H. Versteeg, Sander J.H. van Deventer, Maikel P. Peppelenbosch","doi":"10.1006/mcbr.2001.0270","DOIUrl":"10.1006/mcbr.2001.0270","url":null,"abstract":"<div><p>The adipocyte-derived hormone leptin plays an important role as a relayer of nutritional status to several organ systems. Evidence is accumulating that leptin plays an important role in the adequate functioning and maintenance of the immune system. Here we show that leptin induces sustained phosphorylation of p38 MAP kinase in human peripheral blood mononuclear cells (PBMCs). We show furthermore that leptin induces two routes to phosphorylation of the 40S ribosomal protein S6, one is activation of the p90 ribosomal S6 kinase (RSK) via the MEK/p42/p44 MAP kinase pathway, the other is via activation of p70 S6 kinase. Thus, these results give new insight in the mechanism that underlies the immunomodulatory effects of leptin.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 3","pages":"Pages 144-150"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0270","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89486791","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}
Yup Kang , Jae Sook Park , Sung Hye Kim , Yoo Jung Shin , Wankee Kim , Hee-Jae Joo , Jang-Soo Chun , Hyon Ju Kim , Mahn Joon Ha
{"title":"Overexpression of Protein Kinase C δ Represses Expression of Proliferin in NIH3T3 Cells That Regulates Cell Proliferation","authors":"Yup Kang , Jae Sook Park , Sung Hye Kim , Yoo Jung Shin , Wankee Kim , Hee-Jae Joo , Jang-Soo Chun , Hyon Ju Kim , Mahn Joon Ha","doi":"10.1006/mcbr.2001.0276","DOIUrl":"https://doi.org/10.1006/mcbr.2001.0276","url":null,"abstract":"<div><p>Protein kinase C (PKC) δ is known to inhibit proliferation of many cell types. In this study we found that overexpression of PKCδ reduced proliferation of NIH3T3 cells. To identify specific genes regulated by PKCδ in regulation of cell proliferation, we used differential display–polymerase chain reaction in PKCδ-overexpressing NIH3T3 cells and found that the expression of proliferin, a secreted protein known to stimulate cell proliferation, was significantly repressed. Transient transfection study indicated that the repression of proliferin expression was inversely proportional to the expression levels of PKCδ. Addition of an anti-proliferin antibody to culture medium to neutralize the secreted proliferin decreased cell proliferation in a dose-dependent manner. Our results, therefore, suggest that overexpression of PKCδ induces transcriptional repression of proliferin, thereby resulting in inhibition of cell proliferation.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 3","pages":"Pages 181-187"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0276","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137406181","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}