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Extracellular stress stimuli alter galectin expression profiles and adhesion characteristics of HL-60 cells
Galectins, a family of soluble β-galactoside-binding proteins, are involved in the regulation of various cellular functions, which are essential for adaptive cellular stress responses (CSRs). Although expression patterns of galectins and galectin-binding glycans change during tissue development and...
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| Published in: | Molecular and cellular biochemistry 2016-02, Vol.413 (1-2), p.137-143 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c481t-cea951f9f2b9defeb0d9270440b2082e1555d51538711814cfa25b70d4e94f2e3 |
| container_end_page | 143 |
| container_issue | 1-2 |
| container_start_page | 137 |
| container_title | Molecular and cellular biochemistry |
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| creator | Timoshenko, A. V. Lanteigne, J. Kozak, K. |
| description | Galectins, a family of soluble β-galactoside-binding proteins, are involved in the regulation of various cellular functions, which are essential for adaptive cellular stress responses (CSRs). Although expression patterns of galectins and galectin-binding glycans change during tissue development and cancer, the requirement and role of galectin networks in the CSRs are not completely understood. In this study, we report that the treatment of human promyelocytic HL-60 cells with stimuli mimicking hypoxia (CoCl
2
), inducing the endoplasmic reticulum stress (tunicamycin), and stimulating cell differentiation, result in stress-specific differential expression of galectin transcripts. In addition, we show that CoCl
2
increases the expression of cell surface glycans recognized by both β-galactoside- and GlcNAc-binding lectins. Thus, microenvironmental stress changes the glycobiological status of cells representing expression profiles of endogenous lectins and corresponding glycans. These findings introduce a novel classification of galectins in HL-60 cells, which suggests diverse functions of galectin members in CSRs. |
| doi_str_mv | 10.1007/s11010-015-2647-0 |
| format | article |
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2
), inducing the endoplasmic reticulum stress (tunicamycin), and stimulating cell differentiation, result in stress-specific differential expression of galectin transcripts. In addition, we show that CoCl
2
increases the expression of cell surface glycans recognized by both β-galactoside- and GlcNAc-binding lectins. Thus, microenvironmental stress changes the glycobiological status of cells representing expression profiles of endogenous lectins and corresponding glycans. These findings introduce a novel classification of galectins in HL-60 cells, which suggests diverse functions of galectin members in CSRs.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/s11010-015-2647-0</identifier><identifier>PMID: 26738488</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Binding proteins ; Biochemistry ; Biomedical and Life Sciences ; Cardiology ; Cell adhesion & migration ; Cell Adhesion - drug effects ; Cell differentiation ; Cell Differentiation - drug effects ; Cell Hypoxia - drug effects ; Cell Size - drug effects ; Cellular biology ; Cobalt - pharmacology ; Endoplasmic Reticulum Stress - drug effects ; Galectins - genetics ; Galectins - metabolism ; Gene Expression Regulation - drug effects ; HL-60 Cells ; Humans ; Hypoxia ; Lectins ; Life Sciences ; Medical Biochemistry ; Oncology ; Polysaccharides ; Protein binding ; Stress ; Tunicamycin - pharmacology</subject><ispartof>Molecular and cellular biochemistry, 2016-02, Vol.413 (1-2), p.137-143</ispartof><rights>Springer Science+Business Media New York 2016</rights><rights>COPYRIGHT 2016 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c481t-cea951f9f2b9defeb0d9270440b2082e1555d51538711814cfa25b70d4e94f2e3</citedby><cites>FETCH-LOGICAL-c481t-cea951f9f2b9defeb0d9270440b2082e1555d51538711814cfa25b70d4e94f2e3</cites></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/26738488$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Timoshenko, A. V.</creatorcontrib><creatorcontrib>Lanteigne, J.</creatorcontrib><creatorcontrib>Kozak, K.</creatorcontrib><title>Extracellular stress stimuli alter galectin expression profiles and adhesion characteristics of HL-60 cells</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><addtitle>Mol Cell Biochem</addtitle><description>Galectins, a family of soluble β-galactoside-binding proteins, are involved in the regulation of various cellular functions, which are essential for adaptive cellular stress responses (CSRs). Although expression patterns of galectins and galectin-binding glycans change during tissue development and cancer, the requirement and role of galectin networks in the CSRs are not completely understood. In this study, we report that the treatment of human promyelocytic HL-60 cells with stimuli mimicking hypoxia (CoCl
2
), inducing the endoplasmic reticulum stress (tunicamycin), and stimulating cell differentiation, result in stress-specific differential expression of galectin transcripts. In addition, we show that CoCl
2
increases the expression of cell surface glycans recognized by both β-galactoside- and GlcNAc-binding lectins. Thus, microenvironmental stress changes the glycobiological status of cells representing expression profiles of endogenous lectins and corresponding glycans. These findings introduce a novel classification of galectins in HL-60 cells, which suggests diverse functions of galectin members in CSRs.</description><subject>Binding proteins</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cardiology</subject><subject>Cell adhesion & migration</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell differentiation</subject><subject>Cell Differentiation - drug effects</subject><subject>Cell Hypoxia - drug effects</subject><subject>Cell Size - drug effects</subject><subject>Cellular biology</subject><subject>Cobalt - pharmacology</subject><subject>Endoplasmic Reticulum Stress - drug effects</subject><subject>Galectins - genetics</subject><subject>Galectins - metabolism</subject><subject>Gene Expression Regulation - drug effects</subject><subject>HL-60 Cells</subject><subject>Humans</subject><subject>Hypoxia</subject><subject>Lectins</subject><subject>Life Sciences</subject><subject>Medical Biochemistry</subject><subject>Oncology</subject><subject>Polysaccharides</subject><subject>Protein binding</subject><subject>Stress</subject><subject>Tunicamycin - pharmacology</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNp1kUtr3TAQhUVpaG4eP6CbIuimG6czsmTJyxDSpnChm2YtZHuUKPXjVrIh-feV46SUQtFCoPnO0WEOY-8RLhBAf06IgFAAqkJUUhfwhu1Q6bKQNdZv2Q5KgMKg1sfsJKUHyDAgvmPHotKlkcbs2M_rxzm6lvp-6V3kaY6UUr7CsPSBu36myO9cT-0cRk6Ph3UcppEf4uRDT4m7seOuu6fn1_beZbOsCdmhTXzy_GZfVMDXD9IZO_KuT3T-cp-y2y_XP65uiv33r9-uLvdFKw3ORUuuVuhrL5q6I08NdLXQICU0AowgVEp1ClVpNKJB2XonVKOhk1RLL6g8ZZ823xzy10JptkNIawI30rQki7oSdWU0lBn9-A_6MC1xzOmeKa3RqCpTFxu1bsKG0U_rzvLpaAjtNNK6CnsppTA1oMQswE3QximlSN4eYhhcfLIIdq3ObtXZXJ1dq7OQNR9eoizNQN0fxWtXGRAbkPJovKP4V9b_uv4GrdCjlQ</recordid><startdate>20160201</startdate><enddate>20160201</enddate><creator>Timoshenko, A. 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V. ; Lanteigne, J. ; Kozak, K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c481t-cea951f9f2b9defeb0d9270440b2082e1555d51538711814cfa25b70d4e94f2e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Binding proteins</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cardiology</topic><topic>Cell adhesion & migration</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell differentiation</topic><topic>Cell Differentiation - drug effects</topic><topic>Cell Hypoxia - drug effects</topic><topic>Cell Size - drug effects</topic><topic>Cellular biology</topic><topic>Cobalt - pharmacology</topic><topic>Endoplasmic Reticulum Stress - drug effects</topic><topic>Galectins - genetics</topic><topic>Galectins - metabolism</topic><topic>Gene Expression Regulation - drug effects</topic><topic>HL-60 Cells</topic><topic>Humans</topic><topic>Hypoxia</topic><topic>Lectins</topic><topic>Life Sciences</topic><topic>Medical Biochemistry</topic><topic>Oncology</topic><topic>Polysaccharides</topic><topic>Protein binding</topic><topic>Stress</topic><topic>Tunicamycin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Timoshenko, A. 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V.</au><au>Lanteigne, J.</au><au>Kozak, K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Extracellular stress stimuli alter galectin expression profiles and adhesion characteristics of HL-60 cells</atitle><jtitle>Molecular and cellular biochemistry</jtitle><stitle>Mol Cell Biochem</stitle><addtitle>Mol Cell Biochem</addtitle><date>2016-02-01</date><risdate>2016</risdate><volume>413</volume><issue>1-2</issue><spage>137</spage><epage>143</epage><pages>137-143</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>Galectins, a family of soluble β-galactoside-binding proteins, are involved in the regulation of various cellular functions, which are essential for adaptive cellular stress responses (CSRs). Although expression patterns of galectins and galectin-binding glycans change during tissue development and cancer, the requirement and role of galectin networks in the CSRs are not completely understood. In this study, we report that the treatment of human promyelocytic HL-60 cells with stimuli mimicking hypoxia (CoCl
2
), inducing the endoplasmic reticulum stress (tunicamycin), and stimulating cell differentiation, result in stress-specific differential expression of galectin transcripts. In addition, we show that CoCl
2
increases the expression of cell surface glycans recognized by both β-galactoside- and GlcNAc-binding lectins. Thus, microenvironmental stress changes the glycobiological status of cells representing expression profiles of endogenous lectins and corresponding glycans. These findings introduce a novel classification of galectins in HL-60 cells, which suggests diverse functions of galectin members in CSRs.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>26738488</pmid><doi>10.1007/s11010-015-2647-0</doi><tpages>7</tpages></addata></record> |
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| ispartof | Molecular and cellular biochemistry, 2016-02, Vol.413 (1-2), p.137-143 |
| issn | 0300-8177 1573-4919 |
| language | eng |
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| subjects | Binding proteins Biochemistry Biomedical and Life Sciences Cardiology Cell adhesion & migration Cell Adhesion - drug effects Cell differentiation Cell Differentiation - drug effects Cell Hypoxia - drug effects Cell Size - drug effects Cellular biology Cobalt - pharmacology Endoplasmic Reticulum Stress - drug effects Galectins - genetics Galectins - metabolism Gene Expression Regulation - drug effects HL-60 Cells Humans Hypoxia Lectins Life Sciences Medical Biochemistry Oncology Polysaccharides Protein binding Stress Tunicamycin - pharmacology |
| title | Extracellular stress stimuli alter galectin expression profiles and adhesion characteristics of HL-60 cells |
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