Lectins as defence molecules in vertebrates and invertebrates
To access publisher full text version of this article. Please click on the hyperlink in Additional Links field The use of lectins for detecting structural variations in the glycocalyx of interacting cells is common to all forms of life, and forms the basis for their function in fertilisation, develo...
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Online Access: | http://hdl.handle.net/2336/112229 https://doi.org/10.1006/fsim.1996.0029 |
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ftlandspitaliuni:oai:www.hirsla.lsh.is:2336/112229 2023-05-15T15:32:29+02:00 Lectins as defence molecules in vertebrates and invertebrates Arason, G J 2010-10-01 http://hdl.handle.net/2336/112229 https://doi.org/10.1006/fsim.1996.0029 en eng Academic Press http://dx.doi.org/10.1006/fsim.1996.0029 Fish Shellfish Immunol. 1996, 6(4):277-89 10504648 doi:10.1006/fsim.1996.0029 http://hdl.handle.net/2336/112229 Fish & Shellfish Immunology Article 2010 ftlandspitaliuni https://doi.org/10.1006/fsim.1996.0029 2022-05-29T08:21:37Z To access publisher full text version of this article. Please click on the hyperlink in Additional Links field The use of lectins for detecting structural variations in the glycocalyx of interacting cells is common to all forms of life, and forms the basis for their function in fertilisation, development, leucocyte migration and self/non-self distinction. Six lectin families are recognised; legume lectins, cereal lectins, P-, S- and C-type lectins, and pentraxins. Of the latter four occurring in animals, only pentraxins and C-type lectins are implicated in defence. Pentraxins have been described from the horseshoe crab and tunicates, as well as trout and Xenopus. C-type lectins are known from at least four protostome and three deuterostome invertebrates. A role in defence is strongly implicated for at least some of these. The C-type molecules known from lower vertebrates have generally lost their lectin function and exist as antifreeze proteins in fish and as a component of snake venom. However, a factor with structural and functional resemblance to mammalian mannan-binding protein (MBP) has been described from the Atlantic salmon, Salmo salar. For a more complete understanding on the evolution of mammalian C-type lectins, attention should be paid not only to humoral but also membrane bound lectins and extracellular matrix components in invertebrates and lower vertebrates. Article in Journal/Newspaper Atlantic salmon Salmo salar Hirsla - Landspítali University Hospital research archive Fish & Shellfish Immunology 6 4 277 289 |
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Hirsla - Landspítali University Hospital research archive |
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ftlandspitaliuni |
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English |
description |
To access publisher full text version of this article. Please click on the hyperlink in Additional Links field The use of lectins for detecting structural variations in the glycocalyx of interacting cells is common to all forms of life, and forms the basis for their function in fertilisation, development, leucocyte migration and self/non-self distinction. Six lectin families are recognised; legume lectins, cereal lectins, P-, S- and C-type lectins, and pentraxins. Of the latter four occurring in animals, only pentraxins and C-type lectins are implicated in defence. Pentraxins have been described from the horseshoe crab and tunicates, as well as trout and Xenopus. C-type lectins are known from at least four protostome and three deuterostome invertebrates. A role in defence is strongly implicated for at least some of these. The C-type molecules known from lower vertebrates have generally lost their lectin function and exist as antifreeze proteins in fish and as a component of snake venom. However, a factor with structural and functional resemblance to mammalian mannan-binding protein (MBP) has been described from the Atlantic salmon, Salmo salar. For a more complete understanding on the evolution of mammalian C-type lectins, attention should be paid not only to humoral but also membrane bound lectins and extracellular matrix components in invertebrates and lower vertebrates. |
format |
Article in Journal/Newspaper |
author |
Arason, G J |
spellingShingle |
Arason, G J Lectins as defence molecules in vertebrates and invertebrates |
author_facet |
Arason, G J |
author_sort |
Arason, G J |
title |
Lectins as defence molecules in vertebrates and invertebrates |
title_short |
Lectins as defence molecules in vertebrates and invertebrates |
title_full |
Lectins as defence molecules in vertebrates and invertebrates |
title_fullStr |
Lectins as defence molecules in vertebrates and invertebrates |
title_full_unstemmed |
Lectins as defence molecules in vertebrates and invertebrates |
title_sort |
lectins as defence molecules in vertebrates and invertebrates |
publisher |
Academic Press |
publishDate |
2010 |
url |
http://hdl.handle.net/2336/112229 https://doi.org/10.1006/fsim.1996.0029 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_relation |
http://dx.doi.org/10.1006/fsim.1996.0029 Fish Shellfish Immunol. 1996, 6(4):277-89 10504648 doi:10.1006/fsim.1996.0029 http://hdl.handle.net/2336/112229 Fish & Shellfish Immunology |
op_doi |
https://doi.org/10.1006/fsim.1996.0029 |
container_title |
Fish & Shellfish Immunology |
container_volume |
6 |
container_issue |
4 |
container_start_page |
277 |
op_container_end_page |
289 |
_version_ |
1766362983903002624 |