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Alpha-syntrophin dependent expression of tubulin alpha 8 protein in hepatocytes
The scaffold protein alpha-syntrophin (SNTA) is a component of the dystrophin glycoprotein complex and has been comprehensively studied in skeletal muscle and adipocytes. SNTA is further expressed in the liver where its biological role remains unclear. Unpublished data from our group suggested that...
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Published in: | Journal of physiology and biochemistry 2018-11, Vol.74 (4), p.511-521 |
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description | The scaffold protein alpha-syntrophin (SNTA) is a component of the dystrophin glycoprotein complex and has been comprehensively studied in skeletal muscle and adipocytes. SNTA is further expressed in the liver where its biological role remains unclear. Unpublished data from our group suggested that SNTA deficiency is associated with altered tubulin alpha 8 (TUBA8) levels in fat. TUBA8 is highly expressed in different cell lines including hepatoma cells, and here we analyzed whether SNTA has a role herein. In Hepa1-6 cells, TUBA8 protein levels were increased upon SNTA knock down and were reduced upon overexpression of SNTA. This regulation was not identified when analyzing mRNA expression. In the liver of SNTA-deficient mice, TUBA8 protein was higher compared to the respective wild-type controls while RNA expression was even suppressed. Using the HaloTag platform, TUBA8 was found to form a complex with SNTA in Hepa1-6 cells. In the hepatic stellate cell line LX-2, the lack or overexpression of SNTA did, however, not change TUBA8 protein expression. SNTA and TUBA8 are described to regulate cell proliferation. Yet, knock down of SNTA did neither affect proliferation nor viability of Hepa1-6 cells. The present study shows that SNTA protein levels are inversely related to TUBA8 protein expression in the hepatocyte cell line Hepa1-6. |
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SNTA is further expressed in the liver where its biological role remains unclear. Unpublished data from our group suggested that SNTA deficiency is associated with altered tubulin alpha 8 (TUBA8) levels in fat. TUBA8 is highly expressed in different cell lines including hepatoma cells, and here we analyzed whether SNTA has a role herein. In Hepa1-6 cells, TUBA8 protein levels were increased upon SNTA knock down and were reduced upon overexpression of SNTA. This regulation was not identified when analyzing mRNA expression. In the liver of SNTA-deficient mice, TUBA8 protein was higher compared to the respective wild-type controls while RNA expression was even suppressed. Using the HaloTag platform, TUBA8 was found to form a complex with SNTA in Hepa1-6 cells. In the hepatic stellate cell line LX-2, the lack or overexpression of SNTA did, however, not change TUBA8 protein expression. SNTA and TUBA8 are described to regulate cell proliferation. Yet, knock down of SNTA did neither affect proliferation nor viability of Hepa1-6 cells. The present study shows that SNTA protein levels are inversely related to TUBA8 protein expression in the hepatocyte cell line Hepa1-6.</description><identifier>ISSN: 1138-7548</identifier><identifier>EISSN: 1877-8755</identifier><identifier>DOI: 10.1007/s13105-018-0645-x</identifier><identifier>PMID: 30033487</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>3T3-L1 Cells ; Adipocytes ; Animal Physiology ; Animals ; Biomedical and Life Sciences ; Biomedicine ; Calcium-Binding Proteins - antagonists & inhibitors ; Calcium-Binding Proteins - chemistry ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Cell Line, Tumor ; Cell lines ; Cell Proliferation ; Cell Survival ; Dystrophin ; Gene expression ; Gene Expression Regulation ; Glycoproteins ; Hepatic Stellate Cells - cytology ; Hepatic Stellate Cells - metabolism ; Hepatocytes ; Hepatocytes - cytology ; Hepatocytes - metabolism ; Hepatoma ; Human Physiology ; Humans ; Immunoprecipitation ; Kinases ; Liver ; Male ; Membrane Proteins - antagonists & inhibitors ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Muscle Proteins - antagonists & inhibitors ; Muscle Proteins - chemistry ; Muscle Proteins - genetics ; Muscle Proteins - metabolism ; Muscles ; Original Article ; Protein expression ; Protein Multimerization ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Reproducibility of Results ; Ribonucleic acid ; RNA ; RNA Interference ; Skeletal muscle ; Tubulin ; Tubulin - chemistry ; Tubulin - genetics ; Tubulin - metabolism ; Viability</subject><ispartof>Journal of physiology and biochemistry, 2018-11, Vol.74 (4), p.511-521</ispartof><rights>University of Navarra 2018</rights><rights>Copyright Springer Science & Business Media 2018</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-3978480dcf8edc3dc3b7ff8ae954582a9b6cc4de18c26719d5d1df5c871415c33</citedby><cites>FETCH-LOGICAL-c372t-3978480dcf8edc3dc3b7ff8ae954582a9b6cc4de18c26719d5d1df5c871415c33</cites><orcidid>0000-0002-5635-3994</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30033487$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rein-Fischboeck, Lisa</creatorcontrib><creatorcontrib>Bajraktari, Ganimete</creatorcontrib><creatorcontrib>Pohl, Rebekka</creatorcontrib><creatorcontrib>Feder, Susanne</creatorcontrib><creatorcontrib>Eisinger, Kristina</creatorcontrib><creatorcontrib>Mages, Wolfgang</creatorcontrib><creatorcontrib>Haberl, Elisabeth M.</creatorcontrib><creatorcontrib>Buechler, Christa</creatorcontrib><title>Alpha-syntrophin dependent expression of tubulin alpha 8 protein in hepatocytes</title><title>Journal of physiology and biochemistry</title><addtitle>J Physiol Biochem</addtitle><addtitle>J Physiol Biochem</addtitle><description>The scaffold protein alpha-syntrophin (SNTA) is a component of the dystrophin glycoprotein complex and has been comprehensively studied in skeletal muscle and adipocytes. SNTA is further expressed in the liver where its biological role remains unclear. Unpublished data from our group suggested that SNTA deficiency is associated with altered tubulin alpha 8 (TUBA8) levels in fat. TUBA8 is highly expressed in different cell lines including hepatoma cells, and here we analyzed whether SNTA has a role herein. In Hepa1-6 cells, TUBA8 protein levels were increased upon SNTA knock down and were reduced upon overexpression of SNTA. This regulation was not identified when analyzing mRNA expression. In the liver of SNTA-deficient mice, TUBA8 protein was higher compared to the respective wild-type controls while RNA expression was even suppressed. Using the HaloTag platform, TUBA8 was found to form a complex with SNTA in Hepa1-6 cells. In the hepatic stellate cell line LX-2, the lack or overexpression of SNTA did, however, not change TUBA8 protein expression. SNTA and TUBA8 are described to regulate cell proliferation. Yet, knock down of SNTA did neither affect proliferation nor viability of Hepa1-6 cells. The present study shows that SNTA protein levels are inversely related to TUBA8 protein expression in the hepatocyte cell line Hepa1-6.</description><subject>3T3-L1 Cells</subject><subject>Adipocytes</subject><subject>Animal Physiology</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Calcium-Binding Proteins - antagonists & inhibitors</subject><subject>Calcium-Binding Proteins - chemistry</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Cell lines</subject><subject>Cell Proliferation</subject><subject>Cell Survival</subject><subject>Dystrophin</subject><subject>Gene expression</subject><subject>Gene Expression Regulation</subject><subject>Glycoproteins</subject><subject>Hepatic Stellate Cells - cytology</subject><subject>Hepatic Stellate Cells - metabolism</subject><subject>Hepatocytes</subject><subject>Hepatocytes - cytology</subject><subject>Hepatocytes - metabolism</subject><subject>Hepatoma</subject><subject>Human Physiology</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Kinases</subject><subject>Liver</subject><subject>Male</subject><subject>Membrane Proteins - antagonists & inhibitors</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Muscle Proteins - antagonists & inhibitors</subject><subject>Muscle Proteins - chemistry</subject><subject>Muscle Proteins - genetics</subject><subject>Muscle Proteins - metabolism</subject><subject>Muscles</subject><subject>Original Article</subject><subject>Protein expression</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Reproducibility of Results</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA Interference</subject><subject>Skeletal muscle</subject><subject>Tubulin</subject><subject>Tubulin - chemistry</subject><subject>Tubulin - genetics</subject><subject>Tubulin - metabolism</subject><subject>Viability</subject><issn>1138-7548</issn><issn>1877-8755</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp1kE1LAzEQhoMoWqs_wIssePESzeRjkz1K8QsKveg5bJNZ27LdXZNdaP-9Ka0KgjCQhHnedyYvIVfA7oAxfR9BAFOUgaEsl4pujsgIjNbUaKWO0x2EoVpJc0bOY1wxJjlwdkrOBGNCSKNHZPZQd4uSxm3Th7ZbLJvMY4eNx6bPcNMFjHHZNllbZf0wH-rUL3eCzGRdaHtM71QL7Mq-ddse4wU5qco64uXhHJP3p8e3yQudzp5fJw9T6oTmPRWFNtIw7yqD3olUc11VpsRCSWV4Wcxz56RHMI7nGgqvPPhKOaNBgnJCjMnt3jet8Tlg7O16GR3WddlgO0TLmZbp9zkvEnrzB121Q2jSdpaDyLkolIZEwZ5yoY0xYGW7sFyXYWuB2V3adp-2TWnbXdp2kzTXB-dhvkb_o_iONwF8D8TUaj4w_I7-3_UL3T-K_A</recordid><startdate>20181101</startdate><enddate>20181101</enddate><creator>Rein-Fischboeck, Lisa</creator><creator>Bajraktari, Ganimete</creator><creator>Pohl, Rebekka</creator><creator>Feder, Susanne</creator><creator>Eisinger, Kristina</creator><creator>Mages, Wolfgang</creator><creator>Haberl, Elisabeth M.</creator><creator>Buechler, Christa</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-5635-3994</orcidid></search><sort><creationdate>20181101</creationdate><title>Alpha-syntrophin dependent expression of tubulin alpha 8 protein in hepatocytes</title><author>Rein-Fischboeck, Lisa ; Bajraktari, Ganimete ; Pohl, Rebekka ; Feder, Susanne ; Eisinger, Kristina ; Mages, Wolfgang ; Haberl, Elisabeth M. ; Buechler, Christa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c372t-3978480dcf8edc3dc3b7ff8ae954582a9b6cc4de18c26719d5d1df5c871415c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>3T3-L1 Cells</topic><topic>Adipocytes</topic><topic>Animal Physiology</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Calcium-Binding Proteins - antagonists & inhibitors</topic><topic>Calcium-Binding Proteins - chemistry</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Cell Line, Tumor</topic><topic>Cell lines</topic><topic>Cell Proliferation</topic><topic>Cell Survival</topic><topic>Dystrophin</topic><topic>Gene expression</topic><topic>Gene Expression Regulation</topic><topic>Glycoproteins</topic><topic>Hepatic Stellate Cells - cytology</topic><topic>Hepatic Stellate Cells - metabolism</topic><topic>Hepatocytes</topic><topic>Hepatocytes - cytology</topic><topic>Hepatocytes - metabolism</topic><topic>Hepatoma</topic><topic>Human Physiology</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Kinases</topic><topic>Liver</topic><topic>Male</topic><topic>Membrane Proteins - antagonists & inhibitors</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Muscle Proteins - antagonists & inhibitors</topic><topic>Muscle Proteins - chemistry</topic><topic>Muscle Proteins - genetics</topic><topic>Muscle Proteins - metabolism</topic><topic>Muscles</topic><topic>Original Article</topic><topic>Protein expression</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Reproducibility of Results</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA Interference</topic><topic>Skeletal muscle</topic><topic>Tubulin</topic><topic>Tubulin - chemistry</topic><topic>Tubulin - genetics</topic><topic>Tubulin - metabolism</topic><topic>Viability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rein-Fischboeck, Lisa</creatorcontrib><creatorcontrib>Bajraktari, Ganimete</creatorcontrib><creatorcontrib>Pohl, Rebekka</creatorcontrib><creatorcontrib>Feder, Susanne</creatorcontrib><creatorcontrib>Eisinger, Kristina</creatorcontrib><creatorcontrib>Mages, Wolfgang</creatorcontrib><creatorcontrib>Haberl, Elisabeth M.</creatorcontrib><creatorcontrib>Buechler, Christa</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of physiology and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rein-Fischboeck, Lisa</au><au>Bajraktari, Ganimete</au><au>Pohl, Rebekka</au><au>Feder, Susanne</au><au>Eisinger, Kristina</au><au>Mages, Wolfgang</au><au>Haberl, Elisabeth M.</au><au>Buechler, Christa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alpha-syntrophin dependent expression of tubulin alpha 8 protein in hepatocytes</atitle><jtitle>Journal of physiology and biochemistry</jtitle><stitle>J Physiol Biochem</stitle><addtitle>J Physiol Biochem</addtitle><date>2018-11-01</date><risdate>2018</risdate><volume>74</volume><issue>4</issue><spage>511</spage><epage>521</epage><pages>511-521</pages><issn>1138-7548</issn><eissn>1877-8755</eissn><abstract>The scaffold protein alpha-syntrophin (SNTA) is a component of the dystrophin glycoprotein complex and has been comprehensively studied in skeletal muscle and adipocytes. SNTA is further expressed in the liver where its biological role remains unclear. Unpublished data from our group suggested that SNTA deficiency is associated with altered tubulin alpha 8 (TUBA8) levels in fat. TUBA8 is highly expressed in different cell lines including hepatoma cells, and here we analyzed whether SNTA has a role herein. In Hepa1-6 cells, TUBA8 protein levels were increased upon SNTA knock down and were reduced upon overexpression of SNTA. This regulation was not identified when analyzing mRNA expression. In the liver of SNTA-deficient mice, TUBA8 protein was higher compared to the respective wild-type controls while RNA expression was even suppressed. Using the HaloTag platform, TUBA8 was found to form a complex with SNTA in Hepa1-6 cells. In the hepatic stellate cell line LX-2, the lack or overexpression of SNTA did, however, not change TUBA8 protein expression. SNTA and TUBA8 are described to regulate cell proliferation. Yet, knock down of SNTA did neither affect proliferation nor viability of Hepa1-6 cells. The present study shows that SNTA protein levels are inversely related to TUBA8 protein expression in the hepatocyte cell line Hepa1-6.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>30033487</pmid><doi>10.1007/s13105-018-0645-x</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-5635-3994</orcidid></addata></record> |
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subjects | 3T3-L1 Cells Adipocytes Animal Physiology Animals Biomedical and Life Sciences Biomedicine Calcium-Binding Proteins - antagonists & inhibitors Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Cell Line, Tumor Cell lines Cell Proliferation Cell Survival Dystrophin Gene expression Gene Expression Regulation Glycoproteins Hepatic Stellate Cells - cytology Hepatic Stellate Cells - metabolism Hepatocytes Hepatocytes - cytology Hepatocytes - metabolism Hepatoma Human Physiology Humans Immunoprecipitation Kinases Liver Male Membrane Proteins - antagonists & inhibitors Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Mice Mice, Inbred C57BL Mice, Knockout Muscle Proteins - antagonists & inhibitors Muscle Proteins - chemistry Muscle Proteins - genetics Muscle Proteins - metabolism Muscles Original Article Protein expression Protein Multimerization Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Reproducibility of Results Ribonucleic acid RNA RNA Interference Skeletal muscle Tubulin Tubulin - chemistry Tubulin - genetics Tubulin - metabolism Viability |
title | Alpha-syntrophin dependent expression of tubulin alpha 8 protein in hepatocytes |
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