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{{short description|Lectin (carbohydrate-binding protein) originally extracted from the jack-bean}}
{{short description|Lectin (carbohydrate-binding protein) originally extracted from the jack-bean}}
{{redirect|ConA|other uses|Cona (disambiguation){{!}}Cona}}
{{Infobox nonhuman protein
{{Infobox nonhuman protein
| Name = Concanavalin A
| Name = Concanavalin A
| image = 3CNA_Concanavalin_A.png
| image = 3CNA_Concanavalin_A.png
| width =
| width =
| caption = Crystallographic structure of a tetramer of [[Canavalia|jack bean]] concanavalin A (the monomers are colored cyan, green, red, and magenta respectively). [[Calcium in biology|Calcium]] (gold) and [[Manganese#Biological role|manganese]] [[Ion#Ions|cation]]s (grey) are depicted as spheres.<ref name="pmid4638345">{{PDB|3CNA}}; {{cite journal | vauthors = Hardman KD, Ainsworth CF | title = Structure of concanavalin A at 2.4-A resolution | journal = Biochemistry | volume = 11 | issue = 26 | pages = 4910–9 | date = December 1972 | pmid = 4638345 | doi = 10.1021/bi00776a006 }}</ref>
| caption = Crystallographic structure of a tetramer of [[Canavalia|jack bean]] concanavalin A (the monomers are colored cyan, green, red, and magenta respectively). [[Calcium in biology|Calcium]] (gold) and [[Manganese#Biological role|manganese]] [[Ion#Ions|cation]]s (grey) are depicted as spheres.<ref name="pmid4638345">{{PDB|3CNA}}; {{cite journal | vauthors = Hardman KD, Ainsworth CF | title = Structure of concanavalin A at 2.4-A resolution | journal = Biochemistry | volume = 11 | issue = 26 | pages = 4910–4919 | date = December 1972 | pmid = 4638345 | doi = 10.1021/bi00776a006 }}</ref>
| Symbol = ConA
| Symbol = ConA
| AltSymbols =
| AltSymbols =
| Organism = ''Canavalia virosa'' (jackbean)
| Organism = ''Canavalia ensiformis'' (jackbean)
| TaxID = 28958
| ATC_prefix=
| ATC_prefix=
| ATC_suffix=
| ATC_suffix=
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}}
}}


'''Concanavalin A''' ('''ConA''') is a [[lectin]] ([[carbohydrate]]-binding [[protein]]) originally extracted from the [[jack-bean]] (''Canavalia ensiformis''). It is a member of the [[legume lectin]] family. It binds specifically to certain structures found in various [[sugar]]s, [[glycoprotein]]s, and [[glycolipid]]s, mainly internal and nonreducing terminal α-D-[[Mannose|mannosyl]] and α-D-glucosyl groups.<ref name="isbn0-12-449945-7">{{cite book |first1=Irwin J. |last1=Goldstein |first2=Ronald D. |last2=Poretz |editor1-first=Irvin E. |editor1-last=Liener |editor2-first=Nathan |editor2-last=Sharon |editor3-first=Irwin J. |editor3-last=Goldstein | title = The Lectins Properties, Functions and Applications in Biology and Medicine | publisher = Elsevier | year = 2012 | chapter = Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins |chapter-url=https://books.google.com/books?id=uiwd4XqOLbMC&pg=PA33 | pages = 33–247 | isbn = 978-0-323-14444-5 }}</ref><ref name="Sumner_1938">{{cite journal | vauthors = Sumner JB, Gralën N, Eriksson-Quensel IB | title = The Molecular Weights of Urease, Canavalin, Concanavalin a and Concanavalin B | journal = Science | volume = 87 | issue = 2261 | pages = 395–6 | date = April 1938 | pmid = 17746464 | doi = 10.1126/science.87.2261.395 | bibcode = 1938Sci....87..395S }}</ref> Its physiological function in plants, however, is still unknown. ConA is a plant [[mitogen]], and is known for its ability to stimulate mouse T-cell subsets giving rise to four functionally distinct T cell populations, including precursors to [[regulatory T cell]]s;<ref name="pmid6461456">{{cite journal | vauthors = Dwyer JM, Johnson C | title = The use of concanavalin A to study the immunoregulation of human T cells | journal = Clinical and Experimental Immunology | volume = 46 | issue = 2 | pages = 237–49 | date = November 1981 | pmid = 6461456 | pmc = 1536405 | author-link1 = John Dwyer (medicine) }}</ref> a subset of human suppressor T-cells is also sensitive to ConA.<ref name="pmid6461456"/> ConA was the first lectin to be available on a commercial basis, and is widely used in [[biology]] and [[biochemistry]] to characterize [[glycoprotein]]s and other sugar-containing entities on the surface of various cells.<ref name="pmid1104592">{{cite journal | vauthors = Schiefer HG, Krauss H, Brunner H, Gerhardt U | title = Ultrastructural visualization of surface carbohydrate structures on mycoplasma membranes by concanavalin A | journal = Journal of Bacteriology | volume = 124 | issue = 3 | pages = 1598–600 | date = December 1975 | doi = 10.1128/JB.124.3.1598-1600.1975 | pmid = 1104592 | pmc = 236075 }}</ref> It is also used to purify glycosylated macromolecules in [[lectin affinity chromatography]],<ref>[http://www.gelifesciences.com/aptrix/upp01077.nsf/Content/protein_purification~affinity~immobilized_lectin GE Healthcare Life Sciences, Immobilized lectin] {{Webarchive|url=https://web.archive.org/web/20120303220910/http://www.gelifesciences.com/aptrix/upp01077.nsf/Content/protein_purification~affinity~immobilized_lectin |date=2012-03-03 }}{{full citation needed|date=November 2017}}</ref> as well as to study immune regulation by various immune cells.<ref name="pmid6461456"/>
'''Concanavalin A''' ('''ConA''') is a [[lectin]] ([[carbohydrate]]-binding [[protein]]) originally extracted from the [[jack-bean]] (''Canavalia ensiformis''). It is a member of the [[legume lectin]] family. It binds specifically to certain structures found in various [[sugar]]s, [[glycoprotein]]s, and [[glycolipid]]s, mainly internal and nonreducing terminal α-D-[[Mannose|mannosyl]] and α-D-glucosyl groups.<ref name="isbn0-12-449945-7">{{cite book |first1=Irwin J. |last1=Goldstein |first2=Ronald D. |last2=Poretz |editor1-first=Irvin E. |editor1-last=Liener |editor2-first=Nathan |editor2-last=Sharon |editor3-first=Irwin J. |editor3-last=Goldstein | title = The Lectins Properties, Functions and Applications in Biology and Medicine | publisher = Elsevier | year = 2012 | chapter = Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins |chapter-url=https://books.google.com/books?id=uiwd4XqOLbMC&pg=PA33 | pages = 33–247 | isbn = 978-0-323-14444-5 }}</ref><ref name="Sumner_1938">{{cite journal | vauthors = Sumner JB, Gralën N, Eriksson-Quensel IB | title = The Molecular Weights of Urease, Canavalin, Concanavalin a and Concanavalin B | journal = Science | volume = 87 | issue = 2261 | pages = 395–396 | date = April 1938 | pmid = 17746464 | doi = 10.1126/science.87.2261.395 | bibcode = 1938Sci....87..395S }}</ref> Its physiological function in plants, however, is still unknown. ConA is a plant [[mitogen]], and is known for its ability to stimulate mouse T-cell subsets giving rise to four functionally distinct T cell populations, including precursors to [[regulatory T cell]]s;<ref name="pmid6461456">{{cite journal | vauthors = Dwyer JM, Johnson C | title = The use of concanavalin A to study the immunoregulation of human T cells | journal = Clinical and Experimental Immunology | volume = 46 | issue = 2 | pages = 237–249 | date = November 1981 | pmid = 6461456 | pmc = 1536405 | author-link1 = John Dwyer (medicine) }}</ref> a subset of human suppressor T-cells is also sensitive to ConA.<ref name="pmid6461456"/> ConA was the first lectin to be available on a commercial basis, and is widely used in [[biology]] and [[biochemistry]] to characterize [[glycoprotein]]s and other sugar-containing entities on the surface of various cells.<ref name="pmid1104592">{{cite journal | vauthors = Schiefer HG, Krauss H, Brunner H, Gerhardt U | title = Ultrastructural visualization of surface carbohydrate structures on mycoplasma membranes by concanavalin A | journal = Journal of Bacteriology | volume = 124 | issue = 3 | pages = 1598–1600 | date = December 1975 | pmid = 1104592 | pmc = 236075 | doi = 10.1128/JB.124.3.1598-1600.1975 }}</ref> It is also used to purify glycosylated macromolecules in [[lectin affinity chromatography]],<ref>[http://www.gelifesciences.com/aptrix/upp01077.nsf/Content/protein_purification~affinity~immobilized_lectin GE Healthcare Life Sciences, Immobilized lectin] {{Webarchive|url=https://web.archive.org/web/20120303220910/http://www.gelifesciences.com/aptrix/upp01077.nsf/Content/protein_purification~affinity~immobilized_lectin |date=2012-03-03 }}{{full citation needed|date=November 2017}}</ref> as well as to study immune regulation by various immune cells.<ref name="pmid6461456"/>


== Structure and properties ==
== Structure and properties ==


Like most lectins, ConA is a [[homotetramer]]: each sub-unit (26.5[[kDa]], 235 [[amino-acid]]s, heavily glycated) binds a metallic atom (usually Mn<sup>2+</sup> and a Ca<sup>2+</sup>). It has the [[Point groups in three dimensions|''D''<sub>2</sub>]] symmetry.<ref name="pmid4638345"/> Its tertiary structure has been elucidated,<ref name="pmid1563347">{{cite journal | vauthors = Min W, Dunn AJ, Jones DH | title = Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage | journal = The EMBO Journal | volume = 11 | issue = 4 | pages = 1303–7 | date = April 1992 | pmid = 1563347 | pmc = 556578 | doi = 10.1002/j.1460-2075.1992.tb05174.x }}</ref> as have the molecular basis of its interactions with metals as well as its affinity for the sugars [[mannose]] and [[glucose]]<ref name="pmid9546043">{{cite journal | vauthors = Loris R, Hamelryck T, Bouckaert J, Wyns L | title = Legume lectin structure | journal = Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology | volume = 1383 | issue = 1 | pages = 9–36 | date = March 1998 | pmid = 9546043 | doi = 10.1016/S0167-4838(97)00182-9 }}</ref> are well known.
Like most lectins, ConA is a [[homotetramer]]: each sub-unit (26.5[[kDa]], 235 [[amino-acid]]s, heavily glycated) binds a metallic atom (usually Mn<sup>2+</sup> and a Ca<sup>2+</sup>). It has the [[Point groups in three dimensions|''D''<sub>2</sub>]] symmetry.<ref name="pmid4638345"/> Its tertiary structure has been elucidated,<ref name="pmid1563347">{{cite journal | vauthors = Min W, Dunn AJ, Jones DH | title = Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage | journal = The EMBO Journal | volume = 11 | issue = 4 | pages = 1303–1307 | date = April 1992 | pmid = 1563347 | pmc = 556578 | doi = 10.1002/j.1460-2075.1992.tb05174.x }}</ref> as have the molecular basis of its interactions with metals as well as its affinity for the sugars [[mannose]] and [[glucose]]<ref name="pmid9546043">{{cite journal | vauthors = Loris R, Hamelryck T, Bouckaert J, Wyns L | title = Legume lectin structure | journal = Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology | volume = 1383 | issue = 1 | pages = 9–36 | date = March 1998 | pmid = 9546043 | doi = 10.1016/S0167-4838(97)00182-9 }}</ref> are well known.


ConA binds specifically α-D-mannosyl and α-D-glucosyl residues (two hexoses differing only in the alcohol on carbon 2) in terminal position of ramified structures from B-Glycans (rich in α-mannose, or hybrid and bi-antennary glycan complexes). It has 4 binding sites, corresponding to the 4 sub-units.<ref name="Sumner_1938" /> The [[molecular weight]] is 104-112[[kDa]] and the [[isoelectric point]] (pI) is in the range of 4.5-5.5.
ConA binds specifically α-D-mannosyl and α-D-glucosyl residues (two hexoses differing only in the alcohol on carbon 2) in terminal position of ramified structures from B-Glycans (rich in α-mannose, or hybrid and bi-antennary glycan complexes). It has 4 binding sites, corresponding to the 4 sub-units.<ref name="Sumner_1938" /> The [[molecular weight]] is 104–112 [[kDa]] and the [[isoelectric point]] (pI) is in the range of 4.5–5.5.


ConA can also initiate cell division (mitogenesis), primarily acting on T-lymphocytes, by stimulating their energy metabolism within seconds of exposure.<ref name="pmid10393256">{{cite journal | vauthors = Krauss S, Buttgereit F, Brand MD | title = Effects of the mitogen concanavalin A on pathways of thymocyte energy metabolism | journal = Biochimica et Biophysica Acta (BBA) - Bioenergetics | volume = 1412 | issue = 2 | pages = 129–38 | date = June 1999 | pmid = 10393256 | doi = 10.1016/S0005-2728(99)00058-4 | doi-access = free }}</ref>
ConA can also initiate cell division (mitogenesis), primarily acting on T-lymphocytes, by stimulating their energy metabolism within seconds of exposure.<ref name="pmid10393256">{{cite journal | vauthors = Krauss S, Buttgereit F, Brand MD | title = Effects of the mitogen concanavalin A on pathways of thymocyte energy metabolism | journal = Biochimica et Biophysica Acta (BBA) - Bioenergetics | volume = 1412 | issue = 2 | pages = 129–138 | date = June 1999 | pmid = 10393256 | doi = 10.1016/S0005-2728(99)00058-4 | doi-access = free }}</ref>


{{for|biotechnological uses|Fluorescent glucose biosensors}}
{{for|biotechnological uses|Fluorescent glucose biosensors}}


==Maturation process==
==Maturation process==
ConA and its variants (found in closely-related plants) are the only proteins known to undergo a post-translational sequence arrangement known as [[Circular permutation in proteins]] whereby the N-terminal half of the conA precursor is swapped to become the C-terminal half in the mature form; all other known circular permutations occur at the genetic level <ref>{{cite journal |last1=Carrington |title=Polypeptide ligation occurs during post-translational modification of concanavalin A |doi=10.1038/313064a0 |pmid=3965973}}</ref> <ref>{{cite journal |last1=Hendrix |first1=Roger |title=Protein Carpentry |doi=10.1016/0960-9822(91)90280-a |pmid=15336168 |url=https://doi.org/10.1016/0960-9822(91)90280-A}}</ref>. ConA circular permutation is carried out by jack bean asparaginyl endopeptidase <ref>{{cite journal |last1=Nonis |first1=Samuel |title=Structural and biochemical analyses of concanavalin A circular permutation by jack bean asparaginyl endopeptidase |journal=The Plant Cell |doi=10.1093/plcell/koab130 |pmid=34235541 |url=https://doi.org/10.1093/plcell/koab130}}</ref>, a versatile enzyme capable of cleaving and ligating peptide substrates at a single active site <ref>{{cite journal |last1=Nonis |first1=Samuel |title=Plant asparaginyl endopeptidases and their structural determinants of function |journal=Biochemical Society Transactions |doi=10.1042/BST20200908 |pmid=33666219 |url=https://doi.org/10.1042/BST20200908}}</ref>. To convert conA to the mature form, jack bean asparaginyl endopeptidase cleaves the precursor of conA in the middle and ligates the two original termini.
ConA and its variants (found in closely related plants) are the only proteins known to undergo a post-translational sequence arrangement known as [[Circular permutation in proteins]] whereby the N-terminal half of the conA precursor is swapped to become the C-terminal half in the mature form; all other known circular permutations occur at the genetic level.<ref>{{cite journal | vauthors = Carrington DM, Auffret A, Hanke DE | title = Polypeptide ligation occurs during post-translational modification of concanavalin A | journal = Nature | year = 1985 | volume = 313 | issue = 5997 | pages = 64–67 | pmid = 3965973 | doi = 10.1038/313064a0 | bibcode = 1985Natur.313...64C | s2cid = 4359482 }}</ref><ref>{{cite journal | vauthors = Hendrix RW | title = Protein carpentry | journal = Current Biology | volume = 1 | issue = 2 | pages = 71–73 | date = April 1991 | pmid = 15336168 | doi = 10.1016/0960-9822(91)90280-a | s2cid = 45963307 }}</ref> ConA circular permutation is carried out by jack bean asparaginyl endopeptidase,<ref>{{cite journal | vauthors = Nonis SG, Haywood J, Schmidberger JW, Mackie ER, Soares da Costa TP, Bond CS, Mylne JS | title = Structural and biochemical analyses of concanavalin A circular permutation by jack bean asparaginyl endopeptidase | journal = The Plant Cell | volume = 33 | issue = 8 | pages = 2794–2811 | date = August 2021 | pmid = 34235541 | doi = 10.1093/plcell/koab130 | pmc = 8408470 }}</ref> a versatile enzyme capable of cleaving and ligating peptide substrates at a single active site.<ref>{{cite journal | vauthors = Nonis SG, Haywood J, Mylne JS | title = Plant asparaginyl endopeptidases and their structural determinants of function | journal = Biochemical Society Transactions | volume = 49 | issue = 2 | pages = 965–976 | date = April 2021 | pmid = 33666219 | doi = 10.1042/BST20200908 | pmc = 8106488 }}</ref> To convert conA to the mature form, jack bean asparaginyl endopeptidase cleaves the precursor of conA in the middle and ligates the two original termini.


==Biological activity==
==Biological activity==
Concanavalin A interacts with diverse receptors containing mannose carbohydrates, notably rhodopsin, [[blood group]] [[biomarker|marker]]s, insulin-receptor<ref>{{cite journal | vauthors = Cuatrecasas P, Tell GP | title = Insulin-like activity of concanavalin A and wheat germ agglutinin--direct interactions with insulin receptors | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 70 | issue = 2 | pages = 485–9 | date = February 1973 | pmid = 4510292 | pmc = 433288 | doi = 10.1073/pnas.70.2.485 | bibcode = 1973PNAS...70..485C | jstor = 62526 | doi-access = free }}</ref> the [[Immunoglobulin]]s and the [[Carcinoembryonic antigen|carcino-embryonary antigen]] (CEA). It also interacts with [[lipoprotein]]s.<ref>{{cite journal | vauthors = Harmony JA, Cordes EH | title = Interaction of human plasma low density lipoprotein with concanavalin A and with ricin | journal = The Journal of Biological Chemistry | volume = 250 | issue = 22 | pages = 8614–7 | date = November 1975 | doi = 10.1016/S0021-9258(19)40714-X | pmid = 171260 | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=171260 | doi-access = free }}{{Dead link|date=March 2022 |bot=InternetArchiveBot |fix-attempted=yes }}</ref>
Concanavalin A interacts with diverse receptors containing mannose carbohydrates, notably rhodopsin, [[blood group]] [[biomarker|marker]]s, insulin receptors,<ref>{{cite journal | vauthors = Cuatrecasas P, Tell GP | title = Insulin-like activity of concanavalin A and wheat germ agglutinin--direct interactions with insulin receptors | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 70 | issue = 2 | pages = 485–489 | date = February 1973 | pmid = 4510292 | pmc = 433288 | doi = 10.1073/pnas.70.2.485 | doi-access = free | bibcode = 1973PNAS...70..485C | jstor = 62526 }}</ref> the [[immunoglobulin]]s and the [[Carcinoembryonic antigen|carcino-embryonary antigen]] (CEA). It also interacts with [[lipoprotein]]s.<ref>{{cite journal | vauthors = Harmony JA, Cordes EH | title = Interaction of human plasma low density lipoprotein with concanavalin A and with ricin | journal = The Journal of Biological Chemistry | volume = 250 | issue = 22 | pages = 8614–8617 | date = November 1975 | pmid = 171260 | doi = 10.1016/S0021-9258(19)40714-X | doi-access = free }}{{Dead link|date=March 2022 |bot=InternetArchiveBot |fix-attempted=yes }}</ref>


ConA strongly agglutinates [[erythrocyte]]s irrespective of blood-group, and various cancerous cells.<ref>{{cite journal | vauthors = Betton GR | title = Agglutination reactions of spontaneous canine tumour cells, induced by concanavalin A, demonstrated by an isotopic assay | journal = International Journal of Cancer | volume = 18 | issue = 5 | pages = 687–96 | date = November 1976 | pmid = 992901 | doi = 10.1002/ijc.2910180518 | s2cid = 36612952 }}</ref><ref>{{cite journal | vauthors = Kakizoe T, Komatsu H, Niijima T, Kawachi T, Sugimura T | title = Increased agglutinability of bladder cells by concanavalin A after administration of carcinogens | journal = Cancer Research | volume = 40 | issue = 6 | pages = 2006–9 | date = June 1980 | pmid = 7371036 }}</ref><ref>{{cite journal | vauthors = Becker FF, Shurgin A | title = Concanavalin A agglutination of cells from primary hepatocellular carcinomas and hepatic nodules induced by N-2-fluorenylacetamide | journal = Cancer Research | volume = 35 | issue = 10 | pages = 2879–83 | date = October 1975 | pmid = 168971 }}</ref> It was demonstrated that transformed cells and [[trypsin]]-treated normal cells do not agglutinate at 4&nbsp;°C, thereby suggesting that there is a temperature-sensitive step involved in ConA-mediated agglutination.<ref>{{cite journal | vauthors = Inbar M, Ben-Bassat H, Sachs L | title = A specific metabolic activity on the surface membrane in malignant cell-transformation | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 68 | issue = 11 | pages = 2748–51 | date = November 1971 | pmid = 4330939 | pmc = 389516 | doi = 10.1073/pnas.68.11.2748 | bibcode = 1971PNAS...68.2748I | jstor = 61219 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Sela BA, Lis H, Sharon N, Sachs L | title = Quantitation of N-acetyl-D-galactosamine-like sites on the surface membrane of normal and transformed mammalian cells | journal = Biochimica et Biophysica Acta (BBA) - Biomembranes | volume = 249 | issue = 2 | pages = 564–8 | date = December 1971 | pmid = 4332414 | doi = 10.1016/0005-2736(71)90132-5 }}</ref>
ConA strongly agglutinates [[erythrocyte]]s irrespective of blood-group, and various cancerous cells.<ref>{{cite journal | vauthors = Betton GR | title = Agglutination reactions of spontaneous canine tumour cells, induced by concanavalin A, demonstrated by an isotopic assay | journal = International Journal of Cancer | volume = 18 | issue = 5 | pages = 687–696 | date = November 1976 | pmid = 992901 | doi = 10.1002/ijc.2910180518 | s2cid = 36612952 }}</ref><ref>{{cite journal | vauthors = Kakizoe T, Komatsu H, Niijima T, Kawachi T, Sugimura T | title = Increased agglutinability of bladder cells by concanavalin A after administration of carcinogens | journal = Cancer Research | volume = 40 | issue = 6 | pages = 2006–2009 | date = June 1980 | pmid = 7371036 }}</ref><ref>{{cite journal | vauthors = Becker FF, Shurgin A | title = Concanavalin A agglutination of cells from primary hepatocellular carcinomas and hepatic nodules induced by N-2-fluorenylacetamide | journal = Cancer Research | volume = 35 | issue = 10 | pages = 2879–2883 | date = October 1975 | pmid = 168971 }}</ref> It was demonstrated that transformed cells and [[trypsin]]-treated normal cells do not agglutinate at 4&nbsp;°C, thereby suggesting that there is a temperature-sensitive step involved in ConA-mediated agglutination.<ref>{{cite journal | vauthors = Inbar M, Ben-Bassat H, Sachs L | title = A specific metabolic activity on the surface membrane in malignant cell-transformation | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 68 | issue = 11 | pages = 2748–2751 | date = November 1971 | pmid = 4330939 | pmc = 389516 | doi = 10.1073/pnas.68.11.2748 | doi-access = free | bibcode = 1971PNAS...68.2748I | jstor = 61219 }}</ref><ref>{{cite journal | vauthors = Sela BA, Lis H, Sharon N, Sachs L | title = Quantitation of N-acetyl-D-galactosamine-like sites on the surface membrane of normal and transformed mammalian cells | journal = Biochimica et Biophysica Acta (BBA) - Biomembranes | volume = 249 | issue = 2 | pages = 564–568 | date = December 1971 | pmid = 4332414 | doi = 10.1016/0005-2736(71)90132-5 }}</ref>


ConA-mediated agglutination of other cell types has been reported, including [[myocytes|muscle cell]]s ,<ref>{{cite journal | vauthors = Gartner TK, Podleski TR | title = Evidence that a membrane bound lectin mediates fusion of L6 myoblasts | journal = Biochemical and Biophysical Research Communications | volume = 67 | issue = 3 | pages = 972–8 | date = December 1975 | pmid = 1201086 | doi = 10.1016/0006-291X(75)90770-6 }}</ref> B-[[lymphocyte]]s (through surface [[Immunoglobulin]]s),<ref>{{cite journal | vauthors = de Petris S | title = Concanavalin A receptors, immunoglobulins, and theta antigen of the lymphocyte surface. Interactions with concanavalin A and with Cytoplasmic structures | journal = The Journal of Cell Biology | volume = 65 | issue = 1 | pages = 123–46 | date = April 1975 | pmid = 1092699 | pmc = 2111157 | doi = 10.1083/jcb.65.1.123 }}</ref> [[fibroblast]]s,<ref>{{cite journal | vauthors = Noonan KD, Burger MM | title = The relationship of concanavalin A binding to lectin-initiated cell agglutination | journal = The Journal of Cell Biology | volume = 59 | issue = 1 | pages = 134–42 | date = October 1973 | pmid = 4201706 | pmc = 2110924 | doi = 10.1083/jcb.59.1.134 }}</ref> rat [[thymocyte]]s,<ref>{{cite journal | vauthors = Capo C, Garrouste F, Benoliel AM, Bongrand P, Ryter A, Bell GI | title = Concanavalin-A-mediated thymocyte agglutination: a model for a quantitative study of cell adhesion | journal = Journal of Cell Science | volume = 56 | pages = 21–48 | date = August 1982 | doi = 10.1242/jcs.56.1.21 | pmid = 7166565 | url = http://jcs.biologists.org/cgi/pmidlookup?view=long&pmid=7166565 }}</ref> human fetal (but not adult) [[intestinal epithelial cells]],<ref>{{cite journal | vauthors = Weiser MM | title = Concanavalin A agglutination of intestinal cells from the human fetus | journal = Science | volume = 177 | issue = 4048 | pages = 525–6 | date = August 1972 | pmid = 5050484 | doi = 10.1126/science.177.4048.525 | bibcode = 1972Sci...177..525W | s2cid = 23661797 }}</ref> and [[adipocyte]]s.<ref>{{cite journal | vauthors = Cuatrecasas P | title = Interaction of wheat germ agglutinin and concanavalin A with isolated fat cells | journal = Biochemistry | volume = 12 | issue = 7 | pages = 1312–23 | date = March 1973 | pmid = 4696755 | doi = 10.1021/bi00731a011 }}</ref>
ConA-mediated agglutination of other cell types has been reported, including [[myocytes|muscle cell]]s,<ref>{{cite journal | vauthors = Gartner TK, Podleski TR | title = Evidence that a membrane bound lectin mediates fusion of L6 myoblasts | journal = Biochemical and Biophysical Research Communications | volume = 67 | issue = 3 | pages = 972–978 | date = December 1975 | pmid = 1201086 | doi = 10.1016/0006-291X(75)90770-6 }}</ref> B-[[lymphocyte]]s (through surface [[immunoglobulin]]s),<ref>{{cite journal | vauthors = de Petris S | title = Concanavalin A receptors, immunoglobulins, and theta antigen of the lymphocyte surface. Interactions with concanavalin A and with Cytoplasmic structures | journal = The Journal of Cell Biology | volume = 65 | issue = 1 | pages = 123–146 | date = April 1975 | pmid = 1092699 | pmc = 2111157 | doi = 10.1083/jcb.65.1.123 }}</ref> [[fibroblast]]s,<ref>{{cite journal | vauthors = Noonan KD, Burger MM | title = The relationship of concanavalin A binding to lectin-initiated cell agglutination | journal = The Journal of Cell Biology | volume = 59 | issue = 1 | pages = 134–142 | date = October 1973 | pmid = 4201706 | pmc = 2110924 | doi = 10.1083/jcb.59.1.134 }}</ref> rat [[thymocyte]]s,<ref>{{cite journal | vauthors = Capo C, Garrouste F, Benoliel AM, Bongrand P, Ryter A, Bell GI | title = Concanavalin-A-mediated thymocyte agglutination: a model for a quantitative study of cell adhesion | journal = Journal of Cell Science | volume = 56 | pages = 21–48 | date = August 1982 | pmid = 7166565 | doi = 10.1242/jcs.56.1.21 }}</ref> human fetal (but not adult) [[intestinal epithelial cells]],<ref>{{cite journal | vauthors = Weiser MM | title = Concanavalin A agglutination of intestinal cells from the human fetus | journal = Science | volume = 177 | issue = 4048 | pages = 525–526 | date = August 1972 | pmid = 5050484 | doi = 10.1126/science.177.4048.525 | s2cid = 23661797 | bibcode = 1972Sci...177..525W }}</ref> and [[adipocyte]]s.<ref>{{cite journal | vauthors = Cuatrecasas P | title = Interaction of wheat germ agglutinin and concanavalin A with isolated fat cells | journal = Biochemistry | volume = 12 | issue = 7 | pages = 1312–1323 | date = March 1973 | pmid = 4696755 | doi = 10.1021/bi00731a011 }}</ref>


ConA is a [[lymphocyte]] [[mitogen]]. Similar to [[phytohemagglutinin]] (PHA), it is a selective T cell mitogen relative to its effects on B cells. PHA and ConA bind and cross-link components of the [[T cell receptor]], and their ability to activate T cells is dependent on expression of the T cell receptor.<ref>{{cite journal | vauthors = Weiss A, Shields R, Newton M, Manger B, Imboden J | title = Ligand-receptor interactions required for commitment to the activation of the interleukin 2 gene | journal = Journal of Immunology | volume = 138 | issue = 7 | pages = 2169–76 | date = April 1987 | pmid = 3104454 | url = http://www.jimmunol.org/cgi/pmidlookup?view=long&pmid=3104454 }}</ref><ref>{{cite journal | vauthors = Kanellopoulos JM, De Petris S, Leca G, Crumpton MJ | title = The mitogenic lectin from Phaseolus vulgaris does not recognize the T3 antigen of human T lymphocytes | journal = European Journal of Immunology | volume = 15 | issue = 5 | pages = 479–86 | date = May 1985 | pmid = 3873340 | doi = 10.1002/eji.1830150512 | s2cid = 21414006 }}</ref>
ConA is a [[lymphocyte]] [[mitogen]]. Similar to [[phytohemagglutinin]] (PHA), it is a selective T cell mitogen relative to its effects on B cells. PHA and ConA bind and cross-link components of the [[T cell receptor]], and their ability to activate T cells is dependent on expression of the T cell receptor.<ref>{{cite journal | vauthors = Weiss A, Shields R, Newton M, Manger B, Imboden J | title = Ligand-receptor interactions required for commitment to the activation of the interleukin 2 gene | journal = Journal of Immunology | volume = 138 | issue = 7 | pages = 2169–2176 | date = April 1987 | doi = 10.4049/jimmunol.138.7.2169 | pmid = 3104454 | s2cid = 35173412 | url = http://www.jimmunol.org/cgi/pmidlookup?view=long&pmid=3104454 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Kanellopoulos JM, De Petris S, Leca G, Crumpton MJ | title = The mitogenic lectin from Phaseolus vulgaris does not recognize the T3 antigen of human T lymphocytes | journal = European Journal of Immunology | volume = 15 | issue = 5 | pages = 479–486 | date = May 1985 | pmid = 3873340 | doi = 10.1002/eji.1830150512 | s2cid = 21414006 }}</ref>


ConA interacts with the surface [[mannose]] residues of many microbes, including the bacteria ''[[Escherichia coli|E. coli]]'',<ref>{{cite journal | vauthors = Ofek I, Mirelman D, Sharon N | title = Adherence of Escherichia coli to human mucosal cells mediated by mannose receptors | journal = Nature | volume = 265 | issue = 5595 | pages = 623–5 | date = February 1977 | pmid = 323718 | doi = 10.1038/265623a0 | bibcode = 1977Natur.265..623O | s2cid = 4223466 }}</ref> and ''[[Bacillus subtilis]]''<ref>{{cite journal | vauthors = Doyle RJ, Birdsell DC | title = Interaction of concanavalin A with the cell wall of Bacillus subtilis | journal = Journal of Bacteriology | volume = 109 | issue = 2 | pages = 652–8 | date = February 1972 | doi = 10.1128/JB.109.2.652-658.1972 | pmid = 4621684 | pmc = 285189 }}</ref> and the protist ''[[Dictyostelium discoideum]]''.<ref>{{cite journal | vauthors = West CM, McMahon D | title = Identification of concanavalin A receptors and galactose-binding proteins in purified plasma membranes of Dictyostelium discoideum | journal = The Journal of Cell Biology | volume = 74 | issue = 1 | pages = 264–73 | date = July 1977 | pmid = 559679 | pmc = 2109878 | doi = 10.1083/jcb.74.1.264 }}</ref>
ConA interacts with the surface [[mannose]] residues of many microbes, including the bacteria ''[[Escherichia coli|E. coli]]'',<ref>{{cite journal | vauthors = Ofek I, Mirelman D, Sharon N | title = Adherence of Escherichia coli to human mucosal cells mediated by mannose receptors | journal = Nature | volume = 265 | issue = 5595 | pages = 623–625 | date = February 1977 | pmid = 323718 | doi = 10.1038/265623a0 | s2cid = 4223466 | bibcode = 1977Natur.265..623O }}</ref> and ''[[Bacillus subtilis]]''<ref>{{cite journal | vauthors = Doyle RJ, Birdsell DC | title = Interaction of concanavalin A with the cell wall of Bacillus subtilis | journal = Journal of Bacteriology | volume = 109 | issue = 2 | pages = 652–658 | date = February 1972 | pmid = 4621684 | pmc = 285189 | doi = 10.1128/JB.109.2.652-658.1972 }}</ref> and the protist ''[[Dictyostelium discoideum]]''.<ref>{{cite journal | vauthors = West CM, McMahon D | title = Identification of concanavalin A receptors and galactose-binding proteins in purified plasma membranes of Dictyostelium discoideum | journal = The Journal of Cell Biology | volume = 74 | issue = 1 | pages = 264–273 | date = July 1977 | pmid = 559679 | pmc = 2109878 | doi = 10.1083/jcb.74.1.264 }}</ref>


It has also been shown as a stimulator of several [[matrix metalloproteinases]] (MMPs).<ref name="pmid7614461">{{cite journal | vauthors = Yu M, Sato H, Seiki M, Thompson EW | title = Complex regulation of membrane-type matrix metalloproteinase expression and matrix metalloproteinase-2 activation by concanavalin A in MDA-MB-231 human breast cancer cells | journal = Cancer Research | volume = 55 | issue = 15 | pages = 3272–7 | date = August 1995 | pmid = 7614461 }}</ref>
It has also been shown as a stimulator of several [[matrix metalloproteinases]] (MMPs).<ref name="pmid7614461">{{cite journal | vauthors = Yu M, Sato H, Seiki M, Thompson EW | title = Complex regulation of membrane-type matrix metalloproteinase expression and matrix metalloproteinase-2 activation by concanavalin A in MDA-MB-231 human breast cancer cells | journal = Cancer Research | volume = 55 | issue = 15 | pages = 3272–3277 | date = August 1995 | pmid = 7614461 }}</ref>


ConA has proven useful in applications requiring solid-phase immobilization of glycoenzymes, especially those that have proved difficult to immobilize by traditional covalent coupling. Using ConA-couple matrices, such enzymes may be immobilized in high quantities without a concurrent loss of activity and/or stability. Such noncovalent ConA-glycoenzyme couplings may be relatively easily reversed by competition with sugars or at acidic pH. If necessary for certain applications, these couplings can be converted to covalent bindings by chemical manipulation.<ref>{{cite journal | vauthors = Saleemuddin M, Husain Q | title = Concanavalin A: a useful ligand for glycoenzyme immobilization--a review | journal = Enzyme and Microbial Technology | volume = 13 | issue = 4 | pages = 290–5 | date = April 1991 | pmid = 1367163 | doi = 10.1016/0141-0229(91)90146-2 }}</ref>
ConA has proven useful in applications requiring solid-phase immobilization of glycoenzymes, especially those that have proved difficult to immobilize by traditional covalent coupling. Using ConA-couple matrices, such enzymes may be immobilized in high quantities without a concurrent loss of activity or stability. Such noncovalent ConA-glycoenzyme couplings may be relatively easily reversed by competition with sugars or at acidic pH. If necessary for certain applications, these couplings can be converted to covalent bindings by chemical manipulation.<ref>{{cite journal | vauthors = Saleemuddin M, Husain Q | title = Concanavalin A: a useful ligand for glycoenzyme immobilization--a review | journal = Enzyme and Microbial Technology | volume = 13 | issue = 4 | pages = 290–295 | date = April 1991 | pmid = 1367163 | doi = 10.1016/0141-0229(91)90146-2 }}</ref>


A report from Taiwan (2009) demonstrated potent therapeutic effect of ConA against experimental hepatoma (liver cancer); in the study by Lei and Chang,<ref name="pmid19272170">{{cite journal | vauthors = Lei HY, Chang CP | title = Lectin of Concanavalin A as an anti-hepatoma therapeutic agent | journal = Journal of Biomedical Science | volume = 16 | pages = 10 | date = January 2009 | pmid = 19272170 | pmc = 2644972 | doi = 10.1186/1423-0127-16-10 }}</ref> ConA was found to be sequestered more by hepatic tumor cells, in preference to surrounding normal hepatocytes. Internalization of ConA occurs preferentially to the mitochondria after binding to cell membrane glycoproteins, which triggers an autophagic cell death. ConA was found to partially inhibit tumor nodule growth independent of its lymphocyte activation; the eradication of the tumor in the murine ''in-situ'' hepatoma model in this study was additionally attributed to the mitogenic/lymphoproliferative action of ConA that may have activated a CD8+ T-cell-mediated, as well as NK- and NK-T cell-mediated, immune response in the liver.<ref name="pmid19272170" />
A report from Taiwan (2009) demonstrated potent therapeutic effect of ConA against experimental hepatoma (liver cancer); in the study by Lei and Chang,<ref name="pmid19272170">{{cite journal | vauthors = Lei HY, Chang CP | title = Lectin of Concanavalin A as an anti-hepatoma therapeutic agent | journal = Journal of Biomedical Science | volume = 16 | pages = 10 | date = January 2009 | issue = 1 | pmid = 19272170 | pmc = 2644972 | doi = 10.1186/1423-0127-16-10 | doi-access = free }}</ref> ConA was found to be sequestered more by hepatic tumor cells, in preference to surrounding normal hepatocytes. Internalization of ConA occurs preferentially to the mitochondria after binding to cell membrane glycoproteins, which triggers an autophagic cell death. ConA was found to partially inhibit tumor nodule growth independent of its lymphocyte activation; the eradication of the tumor in the murine ''in-situ'' hepatoma model in this study was additionally attributed to the mitogenic/lymphoproliferative action of ConA that may have activated a CD8+ T-cell-mediated, as well as NK- and NK-T cell-mediated, immune response in the liver.<ref name="pmid19272170" />


ConA intravitreal injection can be used in the modeling of [[proliferative vitreoretinopathy]] in rats.<ref>{{cite journal | vauthors = Erdiakov AK, Tikhonovich MV, Rzhavina EM, Gavrilova SA | title = [The characteristics of retina at the development of proliferative vitreoretinopathy in rats after intraocular injection of concanavalin a and dispase] | journal = Rossiĭskii Fiziologicheskiĭ Zhurnal Imeni I.M. Sechenova | volume = 101 | issue = 5 | pages = 572–85 | date = May 2015 | pmid = 26263683 }}</ref><ref>{{cite journal | vauthors = Tikhonovich MV, Erdiakov AK, Gavrilova SA | title = Nonsteroid anti-inflammatory therapy suppresses the development of proliferative vitreoretinopathy more effectively than a steroid one | journal = International Ophthalmology | volume = 38 | issue = 4 | pages = 1365–1378 | date = August 2018 | pmid = 28639085 | doi = 10.1007/s10792-017-0594-3 | s2cid = 4017540 }}</ref>
ConA intravitreal injection can be used in the modeling of [[proliferative vitreoretinopathy]] in rats.<ref>{{cite journal | vauthors = Erdiakov AK, Tikhonovich MV, Rzhavina EM, Gavrilova SA | title = [The characteristics of retina at the development of proliferative vitreoretinopathy in rats after intraocular injection of concanavalin a and dispase] | journal = Rossiĭskii Fiziologicheskiĭ Zhurnal Imeni I.M. Sechenova | volume = 101 | issue = 5 | pages = 572–585 | date = May 2015 | pmid = 26263683 }}</ref><ref>{{cite journal | vauthors = Tikhonovich MV, Erdiakov AK, Gavrilova SA | title = Nonsteroid anti-inflammatory therapy suppresses the development of proliferative vitreoretinopathy more effectively than a steroid one | journal = International Ophthalmology | volume = 38 | issue = 4 | pages = 1365–1378 | date = August 2018 | pmid = 28639085 | doi = 10.1007/s10792-017-0594-3 | s2cid = 4017540 }}</ref>


== References ==
== References ==
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* {{MeshName|Concanavalin+A}}
* {{MeshName|Concanavalin+A}}
* {{MeshName|Concanavalin+A+Receptors}}
* {{MeshName|Concanavalin+A+Receptors}}
* [http://www.life.uiuc.edu/crofts/bioph354/bergman/1cvn/e1cvnm.htm Concanavalin A structure]
* [http://www.life.uiuc.edu/crofts/bioph354/bergman/1cvn/e1cvnm.htm Concanavalin A structure] {{Webarchive|url=https://web.archive.org/web/20080820103956/http://www.life.uiuc.edu/crofts/bioph354/bergman/1cvn/e1cvnm.htm |date=2008-08-20 }}
* [https://web.archive.org/web/20080905174252/http://plab.ku.dk/tcbh/lectin-links.htm World of Lectin, Gateway to lectins]
* [https://web.archive.org/web/20080905174252/http://plab.ku.dk/tcbh/lectin-links.htm World of Lectin, Gateway to lectins]
*{{Proteopedia|1bxh}} con A in complex with methyl alpha1-2 mannobioside
*{{Proteopedia|1bxh}} con A in complex with methyl alpha1-2 mannobioside

Latest revision as of 17:28, 18 April 2024

"ConA" redirects here. For other uses, see Cona.
Concanavalin A
Crystallographic structure of a tetramer of jack bean concanavalin A (the monomers are colored cyan, green, red, and magenta respectively). Calcium (gold) and manganese cations (grey) are depicted as spheres.[1]
Identifiers
OrganismCanavalia ensiformis (jackbean)
SymbolConA
PDB3CNA
UniProtP81461
Search for
StructuresSwiss-model
DomainsInterPro

Concanavalin A (ConA) is a lectin (carbohydrate-binding protein) originally extracted from the jack-bean (Canavalia ensiformis). It is a member of the legume lectin family. It binds specifically to certain structures found in various sugars, glycoproteins, and glycolipids, mainly internal and nonreducing terminal α-D-mannosyl and α-D-glucosyl groups.[2][3] Its physiological function in plants, however, is still unknown. ConA is a plant mitogen, and is known for its ability to stimulate mouse T-cell subsets giving rise to four functionally distinct T cell populations, including precursors to regulatory T cells;[4] a subset of human suppressor T-cells is also sensitive to ConA.[4] ConA was the first lectin to be available on a commercial basis, and is widely used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities on the surface of various cells.[5] It is also used to purify glycosylated macromolecules in lectin affinity chromatography,[6] as well as to study immune regulation by various immune cells.[4]

Structure and properties

[edit]

Like most lectins, ConA is a homotetramer: each sub-unit (26.5kDa, 235 amino-acids, heavily glycated) binds a metallic atom (usually Mn2+ and a Ca2+). It has the D2 symmetry.[1] Its tertiary structure has been elucidated,[7] as have the molecular basis of its interactions with metals as well as its affinity for the sugars mannose and glucose[8] are well known.

ConA binds specifically α-D-mannosyl and α-D-glucosyl residues (two hexoses differing only in the alcohol on carbon 2) in terminal position of ramified structures from B-Glycans (rich in α-mannose, or hybrid and bi-antennary glycan complexes). It has 4 binding sites, corresponding to the 4 sub-units.[3] The molecular weight is 104–112 kDa and the isoelectric point (pI) is in the range of 4.5–5.5.

ConA can also initiate cell division (mitogenesis), primarily acting on T-lymphocytes, by stimulating their energy metabolism within seconds of exposure.[9]

For biotechnological uses, see Fluorescent glucose biosensors.

Maturation process

[edit]

ConA and its variants (found in closely related plants) are the only proteins known to undergo a post-translational sequence arrangement known as Circular permutation in proteins whereby the N-terminal half of the conA precursor is swapped to become the C-terminal half in the mature form; all other known circular permutations occur at the genetic level.[10][11] ConA circular permutation is carried out by jack bean asparaginyl endopeptidase,[12] a versatile enzyme capable of cleaving and ligating peptide substrates at a single active site.[13] To convert conA to the mature form, jack bean asparaginyl endopeptidase cleaves the precursor of conA in the middle and ligates the two original termini.

Biological activity

[edit]

Concanavalin A interacts with diverse receptors containing mannose carbohydrates, notably rhodopsin, blood group markers, insulin receptors,[14] the immunoglobulins and the carcino-embryonary antigen (CEA). It also interacts with lipoproteins.[15]

ConA strongly agglutinates erythrocytes irrespective of blood-group, and various cancerous cells.[16][17][18] It was demonstrated that transformed cells and trypsin-treated normal cells do not agglutinate at 4 °C, thereby suggesting that there is a temperature-sensitive step involved in ConA-mediated agglutination.[19][20]

ConA-mediated agglutination of other cell types has been reported, including muscle cells,[21] B-lymphocytes (through surface immunoglobulins),[22] fibroblasts,[23] rat thymocytes,[24] human fetal (but not adult) intestinal epithelial cells,[25] and adipocytes.[26]

ConA is a lymphocyte mitogen. Similar to phytohemagglutinin (PHA), it is a selective T cell mitogen relative to its effects on B cells. PHA and ConA bind and cross-link components of the T cell receptor, and their ability to activate T cells is dependent on expression of the T cell receptor.[27][28]

ConA interacts with the surface mannose residues of many microbes, including the bacteria E. coli,[29] and Bacillus subtilis[30] and the protist Dictyostelium discoideum.[31]

It has also been shown as a stimulator of several matrix metalloproteinases (MMPs).[32]

ConA has proven useful in applications requiring solid-phase immobilization of glycoenzymes, especially those that have proved difficult to immobilize by traditional covalent coupling. Using ConA-couple matrices, such enzymes may be immobilized in high quantities without a concurrent loss of activity or stability. Such noncovalent ConA-glycoenzyme couplings may be relatively easily reversed by competition with sugars or at acidic pH. If necessary for certain applications, these couplings can be converted to covalent bindings by chemical manipulation.[33]

A report from Taiwan (2009) demonstrated potent therapeutic effect of ConA against experimental hepatoma (liver cancer); in the study by Lei and Chang,[34] ConA was found to be sequestered more by hepatic tumor cells, in preference to surrounding normal hepatocytes. Internalization of ConA occurs preferentially to the mitochondria after binding to cell membrane glycoproteins, which triggers an autophagic cell death. ConA was found to partially inhibit tumor nodule growth independent of its lymphocyte activation; the eradication of the tumor in the murine in-situ hepatoma model in this study was additionally attributed to the mitogenic/lymphoproliferative action of ConA that may have activated a CD8+ T-cell-mediated, as well as NK- and NK-T cell-mediated, immune response in the liver.[34]

ConA intravitreal injection can be used in the modeling of proliferative vitreoretinopathy in rats.[35][36]

References

[edit]
  1. ^ a b PDB: 3CNA​; Hardman KD, Ainsworth CF (December 1972). "Structure of concanavalin A at 2.4-A resolution". Biochemistry. 11 (26): 4910–4919. doi:10.1021/bi00776a006. PMID 4638345.
  2. ^ Goldstein, Irwin J.; Poretz, Ronald D. (2012). "Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins". In Liener, Irvin E.; Sharon, Nathan; Goldstein, Irwin J. (eds.). The Lectins Properties, Functions and Applications in Biology and Medicine. Elsevier. pp. 33–247. ISBN 978-0-323-14444-5.
  3. ^ a b Sumner JB, Gralën N, Eriksson-Quensel IB (April 1938). "The Molecular Weights of Urease, Canavalin, Concanavalin a and Concanavalin B". Science. 87 (2261): 395–396. Bibcode:1938Sci....87..395S. doi:10.1126/science.87.2261.395. PMID 17746464.
  4. ^ a b c Dwyer JM, Johnson C (November 1981). "The use of concanavalin A to study the immunoregulation of human T cells". Clinical and Experimental Immunology. 46 (2): 237–249. PMC 1536405. PMID 6461456.
  5. ^ Schiefer HG, Krauss H, Brunner H, Gerhardt U (December 1975). "Ultrastructural visualization of surface carbohydrate structures on mycoplasma membranes by concanavalin A". Journal of Bacteriology. 124 (3): 1598–1600. doi:10.1128/JB.124.3.1598-1600.1975. PMC 236075. PMID 1104592.
  6. ^ GE Healthcare Life Sciences, Immobilized lectin Archived 2012-03-03 at the Wayback Machine[full citation needed]
  7. ^ Min W, Dunn AJ, Jones DH (April 1992). "Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage". The EMBO Journal. 11 (4): 1303–1307. doi:10.1002/j.1460-2075.1992.tb05174.x. PMC 556578. PMID 1563347.
  8. ^ Loris R, Hamelryck T, Bouckaert J, Wyns L (March 1998). "Legume lectin structure". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1383 (1): 9–36. doi:10.1016/S0167-4838(97)00182-9. PMID 9546043.
  9. ^ Krauss S, Buttgereit F, Brand MD (June 1999). "Effects of the mitogen concanavalin A on pathways of thymocyte energy metabolism". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1412 (2): 129–138. doi:10.1016/S0005-2728(99)00058-4. PMID 10393256.
  10. ^ Carrington DM, Auffret A, Hanke DE (1985). "Polypeptide ligation occurs during post-translational modification of concanavalin A". Nature. 313 (5997): 64–67. Bibcode:1985Natur.313...64C. doi:10.1038/313064a0. PMID 3965973. S2CID 4359482.
  11. ^ Hendrix RW (April 1991). "Protein carpentry". Current Biology. 1 (2): 71–73. doi:10.1016/0960-9822(91)90280-a. PMID 15336168. S2CID 45963307.
  12. ^ Nonis SG, Haywood J, Schmidberger JW, Mackie ER, Soares da Costa TP, Bond CS, Mylne JS (August 2021). "Structural and biochemical analyses of concanavalin A circular permutation by jack bean asparaginyl endopeptidase". The Plant Cell. 33 (8): 2794–2811. doi:10.1093/plcell/koab130. PMC 8408470. PMID 34235541.
  13. ^ Nonis SG, Haywood J, Mylne JS (April 2021). "Plant asparaginyl endopeptidases and their structural determinants of function". Biochemical Society Transactions. 49 (2): 965–976. doi:10.1042/BST20200908. PMC 8106488. PMID 33666219.
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