{"title":"Pathophysiological Impacts of Diplomonad Flagellate Spironucleus salmonis Infection on Seawater Adaptability of Juvenile Chum Salmon Oncorhynchus keta","authors":"Khadijeh Khanaliha","doi":"10.52305/azuh8043","DOIUrl":"https://doi.org/10.52305/azuh8043","url":null,"abstract":"","PeriodicalId":90418,"journal":{"name":"Advances in medicine and biology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70889236","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}
Haploinsufficiency of tumor suppressor genes (TSGs) indicates that the reduced levels of proteins in cells that lack one allele of the genomic locus results in the inability of the cell to execute normal cellular functions contributing to tumor development. Representative cases of haploinsufficient TSGs are p27Kip1, p53, DMP1, NF1, and PTEN. Tumor development is significantly accelerated in both mice with homozygous and heterozygous gene deletion, with expression of the wild type allele in the latter. Newly characterized TSGs such as AML1, EGR1, TGFβR1/2, and SMAD4 have also shown haploid insufficiency for tumor suppression. This phenotype has typically been demonstrated in gene knockout mouse models, but analyses of human samples have been conducted in some cases. Recent studies suggest collaboration of multiple haploinsufficient TSGs in 5q-, 7q-, and 8q- syndromes, which is called compound haploinsufficiency. Although ARF is a classical TSG, it also belongs to this category since Arf+/- accelerates tumor development when both alleles for Ink4a are inactivated. Haploid insufficiency of Arf was also reported in myeloid leukemogenesis in the presence of inv(16). In case of p53, p53+/- cells achieve only ~25% of p53 mRNA and protein levels as compared to those in wild type, which could explain the mechanism. TGFβR1+/- collaborates with ApcMin+/- in colorectal cancer development; TGFβR2+/- and Smad4+/- collaborates with K-Ras mutation in pancreatic ductal adenocarcinomagenesis, demonstrating the synergism of haploinsufficient TSGs and other oncogenic events. These TSGs can be targets for activation therapy in cancer since they retain a functional allele even in tumor cells.
{"title":"Haploinsufficient tumor suppressor genes.","authors":"Kazushi Inoue, Elizabeth A Fry","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Haploinsufficiency of tumor suppressor genes (TSGs) indicates that the reduced levels of proteins in cells that lack one allele of the genomic locus results in the inability of the cell to execute normal cellular functions contributing to tumor development. Representative cases of haploinsufficient TSGs are <i>p27<sup>Kip1</sup>, p53, DMP1, NF1,</i> and <i>PTEN</i>. Tumor development is significantly accelerated in both mice with homozygous and heterozygous gene deletion, with expression of the wild type allele in the latter. Newly characterized TSGs such as <i>AML1, EGR1, TGFβR1/2,</i> and <i>SMAD4</i> have also shown haploid insufficiency for tumor suppression. This phenotype has typically been demonstrated in gene knockout mouse models, but analyses of human samples have been conducted in some cases. Recent studies suggest collaboration of multiple haploinsufficient TSGs in 5q-, 7q-, and 8q- syndromes, which is called compound haploinsufficiency. Although <i>ARF</i> is a classical TSG, it also belongs to this category since <i>Arf<sup>+/-</sup></i> accelerates tumor development when both alleles for <i>Ink4a</i> are inactivated. Haploid insufficiency of <i>Arf</i> was also reported in myeloid leukemogenesis in the presence of inv(16). In case of p53, <i>p53<sup>+/-</sup></i> cells achieve only ~25% of p53 mRNA and protein levels as compared to those in wild type, which could explain the mechanism. <i>TGFβR1<sup>+/-</sup></i> collaborates with <i>Apc<sup>Min+/-</sup></i> in colorectal cancer development; <i>TGFβR2<sup>+/-</sup></i> and <i>Smad4<sup>+/-</sup></i> collaborates with <i>K-Ras</i> mutation in pancreatic ductal adenocarcinomagenesis, demonstrating the synergism of haploinsufficient TSGs and other oncogenic events. These TSGs can be targets for activation therapy in cancer since they retain a functional allele even in tumor cells.</p>","PeriodicalId":90418,"journal":{"name":"Advances in medicine and biology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5494974/pdf/nihms864444.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35145089","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}
Lipoproteins such as high-density lipoprotein (HDL) and low-density lipoprotein (LDL) are known to interact with drugs and other solutes in blood. These interactions have been examined in the past by methods such as equilibrium dialysis and capillary electrophoresis. This chapter describes an alternative approach that has recently been developed for examining these interactions by using high-performance affinity chromatography. In this method, lipoproteins are covalently immobilized to a solid support and used within a column as a stationary phase for binding studies. This approach allows the same lipoprotein preparation to be used for a large number of binding studies, leading to precise estimates of binding parameters. This chapter will discuss how this technique can be applied to the identification of interaction models and be used to differentiate between systems that have interactions based on partitioning, adsorption or mixed-mode interactions. It is also shown how this approach can then be used for the measurement of binding parameters for HDL and LDL with drugs. Examples of these studies are provided, with particular attention being given to the use of frontal analysis to examine the interactions of R- and S-propranolol with HDL and LDL. The advantages and possible limitations of this method are described. The extension of this approach to other types of drug-lipoprotein interactions is also considered.
{"title":"Analysis of Drug Interactions with Lipoproteins by High-Performance Affinity Chromatography.","authors":"Matthew R Sobansky, David S Hage","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Lipoproteins such as high-density lipoprotein (HDL) and low-density lipoprotein (LDL) are known to interact with drugs and other solutes in blood. These interactions have been examined in the past by methods such as equilibrium dialysis and capillary electrophoresis. This chapter describes an alternative approach that has recently been developed for examining these interactions by using high-performance affinity chromatography. In this method, lipoproteins are covalently immobilized to a solid support and used within a column as a stationary phase for binding studies. This approach allows the same lipoprotein preparation to be used for a large number of binding studies, leading to precise estimates of binding parameters. This chapter will discuss how this technique can be applied to the identification of interaction models and be used to differentiate between systems that have interactions based on partitioning, adsorption or mixed-mode interactions. It is also shown how this approach can then be used for the measurement of binding parameters for HDL and LDL with drugs. Examples of these studies are provided, with particular attention being given to the use of frontal analysis to examine the interactions of <i>R</i>- and <i>S</i>-propranolol with HDL and LDL. The advantages and possible limitations of this method are described. The extension of this approach to other types of drug-lipoprotein interactions is also considered.</p>","PeriodicalId":90418,"journal":{"name":"Advances in medicine and biology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4225721/pdf/nihms-403295.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32811621","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}
Ebany J Martinez-Finley, Sudipta Chakraborty, Sam Caito, Stephanie Fretham, Michael Aschner
{"title":"<i>C. elegans</i> and Neurodegeneration <i>In Caenorhabditis Elegans: Anatomy, Life Cycles and Biological Functions</i>.","authors":"Ebany J Martinez-Finley, Sudipta Chakraborty, Sam Caito, Stephanie Fretham, Michael Aschner","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":90418,"journal":{"name":"Advances in medicine and biology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7188451/pdf/nihms-1555137.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37882245","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}
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