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Diversified Carbohydrate-Binding Lectins from Marine Resources

Marine bioresources produce a great variety of specific and potent bioactive molecules including natural organic compounds such as fatty acids, polysaccharides, polyether, peptides, proteins, and enzymes. Lectins are also one of the promising candidates for useful therapeutic agents because they can...

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Detalles Bibliográficos
Autores principales: Ogawa, Tomohisa, Watanabe, Mizuki, Naganuma, Takako, Muramoto, Koji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE-Hindawi Access to Research 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3269628/
https://www.ncbi.nlm.nih.gov/pubmed/22312473
http://dx.doi.org/10.4061/2011/838914
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author Ogawa, Tomohisa
Watanabe, Mizuki
Naganuma, Takako
Muramoto, Koji
author_facet Ogawa, Tomohisa
Watanabe, Mizuki
Naganuma, Takako
Muramoto, Koji
author_sort Ogawa, Tomohisa
collection PubMed
description Marine bioresources produce a great variety of specific and potent bioactive molecules including natural organic compounds such as fatty acids, polysaccharides, polyether, peptides, proteins, and enzymes. Lectins are also one of the promising candidates for useful therapeutic agents because they can recognize the specific carbohydrate structures such as proteoglycans, glycoproteins, and glycolipids, resulting in the regulation of various cells via glycoconjugates and their physiological and pathological phenomenon through the host-pathogen interactions and cell-cell communications. Here, we review the multiple lectins from marine resources including fishes and sea invertebrate in terms of their structure-activity relationships and molecular evolution. Especially, we focus on the unique structural properties and molecular evolution of C-type lectins, galectin, F-type lectin, and rhamnose-binding lectin families.
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spelling pubmed-32696282012-02-06 Diversified Carbohydrate-Binding Lectins from Marine Resources Ogawa, Tomohisa Watanabe, Mizuki Naganuma, Takako Muramoto, Koji J Amino Acids Review Article Marine bioresources produce a great variety of specific and potent bioactive molecules including natural organic compounds such as fatty acids, polysaccharides, polyether, peptides, proteins, and enzymes. Lectins are also one of the promising candidates for useful therapeutic agents because they can recognize the specific carbohydrate structures such as proteoglycans, glycoproteins, and glycolipids, resulting in the regulation of various cells via glycoconjugates and their physiological and pathological phenomenon through the host-pathogen interactions and cell-cell communications. Here, we review the multiple lectins from marine resources including fishes and sea invertebrate in terms of their structure-activity relationships and molecular evolution. Especially, we focus on the unique structural properties and molecular evolution of C-type lectins, galectin, F-type lectin, and rhamnose-binding lectin families. SAGE-Hindawi Access to Research 2011 2011-11-15 /pmc/articles/PMC3269628/ /pubmed/22312473 http://dx.doi.org/10.4061/2011/838914 Text en Copyright © 2011 Tomohisa Ogawa et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Ogawa, Tomohisa
Watanabe, Mizuki
Naganuma, Takako
Muramoto, Koji
Diversified Carbohydrate-Binding Lectins from Marine Resources
title Diversified Carbohydrate-Binding Lectins from Marine Resources
title_full Diversified Carbohydrate-Binding Lectins from Marine Resources
title_fullStr Diversified Carbohydrate-Binding Lectins from Marine Resources
title_full_unstemmed Diversified Carbohydrate-Binding Lectins from Marine Resources
title_short Diversified Carbohydrate-Binding Lectins from Marine Resources
title_sort diversified carbohydrate-binding lectins from marine resources
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3269628/
https://www.ncbi.nlm.nih.gov/pubmed/22312473
http://dx.doi.org/10.4061/2011/838914
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