Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a beta-galactoside-binding lectin
β-Galactoside-binding lectins or galectins are a family of closely related carbohydrate-binding proteins which functions still remain to be elucidated. Several evidence suggest they could play a role in different biological processes, such as cell growth regulation and immunomodulation. In the prese...
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Veröffentlicht in: | Journal of biochemistry (Tokyo) 1997-08, Vol.122 (2), p.365-373 |
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description | β-Galactoside-binding lectins or galectins are a family of closely related carbohydrate-binding proteins which functions still remain to be elucidated. Several evidence suggest they could play a role in different biological processes, such as cell growth regulation and immunomodulation. In the present study we report that affinity-purified CLL-I (chicken lactose lectin-I), an acidic 16-kDa galectin exhibits specific growth regulatory properties. Con A-stimulated rat spleen mononuclear cells showed a marked dose-dependent growth inhibition upon incubation with the galectin protein. Cell growth arrest was highly prevented by galectin-specific sugars. In addition, biochemical, cytofluorometrical, and morphological evidence are also provided to show that these inhibitory properties are related to a positive control in the apoptotic threshold of spleen mononuclear cells. Flow cytometric analysis showed a dose- and time-dependent increase of cells with hypodiploid DNA content upon exposure to CLL-I. Moreover, cells treated with CLL-I displayed the typical ultrastructural changes compatible with apoptosis, mainly chromatin condensation and margination along the inner surface of the nuclear envelope. Finally, the highly characteristic “ladder” pattern of DNA fragmentation into oligonucleosome-length fragments of ∼180–200 bp could be found within 6 h of cell culture with CLL-I, mainly in the T cell-enriched population. Induction of apoptosis by a β-galactoside-binding protein highlights a potentially novel mechanism for regulating the immune response and points to a rational basis for the postulated immunomodulatory properties of this protein family. |
doi_str_mv | 10.1093/oxfordjournals.jbchem.a021762 |
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Several evidence suggest they could play a role in different biological processes, such as cell growth regulation and immunomodulation. In the present study we report that affinity-purified CLL-I (chicken lactose lectin-I), an acidic 16-kDa galectin exhibits specific growth regulatory properties. Con A-stimulated rat spleen mononuclear cells showed a marked dose-dependent growth inhibition upon incubation with the galectin protein. Cell growth arrest was highly prevented by galectin-specific sugars. In addition, biochemical, cytofluorometrical, and morphological evidence are also provided to show that these inhibitory properties are related to a positive control in the apoptotic threshold of spleen mononuclear cells. Flow cytometric analysis showed a dose- and time-dependent increase of cells with hypodiploid DNA content upon exposure to CLL-I. Moreover, cells treated with CLL-I displayed the typical ultrastructural changes compatible with apoptosis, mainly chromatin condensation and margination along the inner surface of the nuclear envelope. Finally, the highly characteristic “ladder” pattern of DNA fragmentation into oligonucleosome-length fragments of ∼180–200 bp could be found within 6 h of cell culture with CLL-I, mainly in the T cell-enriched population. Induction of apoptosis by a β-galactoside-binding protein highlights a potentially novel mechanism for regulating the immune response and points to a rational basis for the postulated immunomodulatory properties of this protein family.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a021762</identifier><identifier>PMID: 9378715</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; apoptosis ; B-lymphocytes ; Cell Division ; Cells, Cultured ; cellular proliferation ; Chickens ; chromatin ; chromatin condensation ; CLL-I ; Concanavalin A - pharmacology ; DNA Fragmentation ; dna modification ; Female ; Galectins ; growth ; Hemagglutinins - isolation & purification ; Hemagglutinins - pharmacology ; immunomodulators ; inhibition ; lectins ; Leukocytes, Mononuclear - immunology ; Leukocytes, Mononuclear - ultrastructure ; liver ; Liver - chemistry ; Lymphocyte Activation - physiology ; lymphocyte proliferation ; mononuclear cells ; purification ; Rats ; Rats, Wistar ; Spleen - immunology ; splenocytes ; stimulation ; T-lymphocytes</subject><ispartof>Journal of biochemistry (Tokyo), 1997-08, Vol.122 (2), p.365-373</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9378715$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rabinovich, G.A</creatorcontrib><creatorcontrib>Modesti, N.M</creatorcontrib><creatorcontrib>Castagna, L.F</creatorcontrib><creatorcontrib>Landa, C.A</creatorcontrib><creatorcontrib>Riera, C.M</creatorcontrib><creatorcontrib>Sotomayor, C.E</creatorcontrib><title>Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a beta-galactoside-binding lectin</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>β-Galactoside-binding lectins or galectins are a family of closely related carbohydrate-binding proteins which functions still remain to be elucidated. Several evidence suggest they could play a role in different biological processes, such as cell growth regulation and immunomodulation. In the present study we report that affinity-purified CLL-I (chicken lactose lectin-I), an acidic 16-kDa galectin exhibits specific growth regulatory properties. Con A-stimulated rat spleen mononuclear cells showed a marked dose-dependent growth inhibition upon incubation with the galectin protein. Cell growth arrest was highly prevented by galectin-specific sugars. In addition, biochemical, cytofluorometrical, and morphological evidence are also provided to show that these inhibitory properties are related to a positive control in the apoptotic threshold of spleen mononuclear cells. Flow cytometric analysis showed a dose- and time-dependent increase of cells with hypodiploid DNA content upon exposure to CLL-I. Moreover, cells treated with CLL-I displayed the typical ultrastructural changes compatible with apoptosis, mainly chromatin condensation and margination along the inner surface of the nuclear envelope. Finally, the highly characteristic “ladder” pattern of DNA fragmentation into oligonucleosome-length fragments of ∼180–200 bp could be found within 6 h of cell culture with CLL-I, mainly in the T cell-enriched population. Induction of apoptosis by a β-galactoside-binding protein highlights a potentially novel mechanism for regulating the immune response and points to a rational basis for the postulated immunomodulatory properties of this protein family.</description><subject>Animals</subject><subject>apoptosis</subject><subject>B-lymphocytes</subject><subject>Cell Division</subject><subject>Cells, Cultured</subject><subject>cellular proliferation</subject><subject>Chickens</subject><subject>chromatin</subject><subject>chromatin condensation</subject><subject>CLL-I</subject><subject>Concanavalin A - pharmacology</subject><subject>DNA Fragmentation</subject><subject>dna modification</subject><subject>Female</subject><subject>Galectins</subject><subject>growth</subject><subject>Hemagglutinins - isolation & purification</subject><subject>Hemagglutinins - pharmacology</subject><subject>immunomodulators</subject><subject>inhibition</subject><subject>lectins</subject><subject>Leukocytes, Mononuclear - immunology</subject><subject>Leukocytes, Mononuclear - ultrastructure</subject><subject>liver</subject><subject>Liver - chemistry</subject><subject>Lymphocyte Activation - physiology</subject><subject>lymphocyte proliferation</subject><subject>mononuclear cells</subject><subject>purification</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Spleen - immunology</subject><subject>splenocytes</subject><subject>stimulation</subject><subject>T-lymphocytes</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtvEzEQgC1EVULhJyB8gRNO_dhd20eIoKkUqapaRMXF8jNx2F1v17uo-fe4JHAazXzfjGYGgA8ELwmW7DI9hTS6fZrHXrd5uTd257ulxpTwhr4AC8LrBtGmJi_BApcqkrR6eAVe57x_Tilj5-BcMi44qRfg993gbQzRwtjvoolTTD1MAbaHbtgle5g8HMbUxuBH_Zfp3hXVzfafqYc0TCnHDM0BrjYbdP0Jamj8pNFWt9o-M-eRKU2x38LWl87-DTgLZXv_9hQvwP23r_erNdrcXF2vPm9QYBWZEBHBMl6RynLcYM0lbxzHnBPHaiqFp8IIUXlGbXCVIJKRYBzFnhpeYWbYBfh4HFtueJx9nlQXs_Vtq3uf5qy4ZIJhzIr47iTOpvNODWPs9HhQpz8Vjo485sk__cd6_KUaznit1g8_1Rcsbn_UV1yti__-6AedlN6OMavvdxQThqkQsmaS_QHfb4ne</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>Rabinovich, G.A</creator><creator>Modesti, N.M</creator><creator>Castagna, L.F</creator><creator>Landa, C.A</creator><creator>Riera, C.M</creator><creator>Sotomayor, C.E</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19970801</creationdate><title>Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a beta-galactoside-binding lectin</title><author>Rabinovich, G.A ; Modesti, N.M ; Castagna, L.F ; Landa, C.A ; Riera, C.M ; Sotomayor, C.E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f341t-18fc37414c7060a7976d70771d35298e28b884e32cfd481931fbd20e2b7403b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>apoptosis</topic><topic>B-lymphocytes</topic><topic>Cell Division</topic><topic>Cells, Cultured</topic><topic>cellular proliferation</topic><topic>Chickens</topic><topic>chromatin</topic><topic>chromatin condensation</topic><topic>CLL-I</topic><topic>Concanavalin A - pharmacology</topic><topic>DNA Fragmentation</topic><topic>dna modification</topic><topic>Female</topic><topic>Galectins</topic><topic>growth</topic><topic>Hemagglutinins - isolation & purification</topic><topic>Hemagglutinins - pharmacology</topic><topic>immunomodulators</topic><topic>inhibition</topic><topic>lectins</topic><topic>Leukocytes, Mononuclear - immunology</topic><topic>Leukocytes, Mononuclear - ultrastructure</topic><topic>liver</topic><topic>Liver - chemistry</topic><topic>Lymphocyte Activation - physiology</topic><topic>lymphocyte proliferation</topic><topic>mononuclear cells</topic><topic>purification</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Spleen - immunology</topic><topic>splenocytes</topic><topic>stimulation</topic><topic>T-lymphocytes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rabinovich, G.A</creatorcontrib><creatorcontrib>Modesti, N.M</creatorcontrib><creatorcontrib>Castagna, L.F</creatorcontrib><creatorcontrib>Landa, C.A</creatorcontrib><creatorcontrib>Riera, C.M</creatorcontrib><creatorcontrib>Sotomayor, C.E</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rabinovich, G.A</au><au>Modesti, N.M</au><au>Castagna, L.F</au><au>Landa, C.A</au><au>Riera, C.M</au><au>Sotomayor, C.E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a beta-galactoside-binding lectin</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>122</volume><issue>2</issue><spage>365</spage><epage>373</epage><pages>365-373</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>β-Galactoside-binding lectins or galectins are a family of closely related carbohydrate-binding proteins which functions still remain to be elucidated. Several evidence suggest they could play a role in different biological processes, such as cell growth regulation and immunomodulation. In the present study we report that affinity-purified CLL-I (chicken lactose lectin-I), an acidic 16-kDa galectin exhibits specific growth regulatory properties. Con A-stimulated rat spleen mononuclear cells showed a marked dose-dependent growth inhibition upon incubation with the galectin protein. Cell growth arrest was highly prevented by galectin-specific sugars. In addition, biochemical, cytofluorometrical, and morphological evidence are also provided to show that these inhibitory properties are related to a positive control in the apoptotic threshold of spleen mononuclear cells. Flow cytometric analysis showed a dose- and time-dependent increase of cells with hypodiploid DNA content upon exposure to CLL-I. Moreover, cells treated with CLL-I displayed the typical ultrastructural changes compatible with apoptosis, mainly chromatin condensation and margination along the inner surface of the nuclear envelope. Finally, the highly characteristic “ladder” pattern of DNA fragmentation into oligonucleosome-length fragments of ∼180–200 bp could be found within 6 h of cell culture with CLL-I, mainly in the T cell-enriched population. Induction of apoptosis by a β-galactoside-binding protein highlights a potentially novel mechanism for regulating the immune response and points to a rational basis for the postulated immunomodulatory properties of this protein family.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>9378715</pmid><doi>10.1093/oxfordjournals.jbchem.a021762</doi><tpages>9</tpages></addata></record> |
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subjects | Animals apoptosis B-lymphocytes Cell Division Cells, Cultured cellular proliferation Chickens chromatin chromatin condensation CLL-I Concanavalin A - pharmacology DNA Fragmentation dna modification Female Galectins growth Hemagglutinins - isolation & purification Hemagglutinins - pharmacology immunomodulators inhibition lectins Leukocytes, Mononuclear - immunology Leukocytes, Mononuclear - ultrastructure liver Liver - chemistry Lymphocyte Activation - physiology lymphocyte proliferation mononuclear cells purification Rats Rats, Wistar Spleen - immunology splenocytes stimulation T-lymphocytes |
title | Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a beta-galactoside-binding lectin |
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