Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>

Autores
Laino, Aldana; Cunningham, Mónica Liliana; Suárez, Gustavo; García, Carlos Fernando
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipids due to its hydrophobic nature are transported in the hemolymph mainly by lipoproteic fractions. In the present work we studied the lipoproteic fractions present in the hemolymph of the spider Grammostola rosea. Through ultracentrifugation two lipoproteic fractions are isolated, one of high density named Gr-HDL (δ = 1.13 - 1.15 g/ml) and the other of very high density called Gr-VHDL (δ = 1.24 - 1.27 g/ml) Gr-VHDL in hemolymph is majority in relation to Gr-HDL. In this sense Gr-VHDL fraction has 98.6% of hemolymphatic proteins, and 89.3% of lipids presents in the hemolymph. Both lipoproteic fractions possess phospholipids such as majority lipids (phosphatidylcholine and phosphatidylethanolamine) and 18:1, 16:0, 18:2 and 18:0 as the major fatty acids. In order to confirm the role played by lipoproteic fractions in vitro assays with different 14C-lipid were performed. It was observed that Gr-VHDL takes up mainly free fatty acids and triacylglycerols unlike that observed for Gr-HDL in relation to phosphatidylcholine. Through electrophoresis it was observed that Gr-VHDL has three proteins: a predominant band of 68 kDa and two others of 99 and 121 kDa. Gr-HDL displayed a predominant band of 93 kDa, and other minority of 249 kDa. In conclusion, this study reports lipid characterization of the lipoproteic fractions present in the hemolymph of the tarantula, G. rosea. The role of each lipoproteic fraction in relation to lipid up- take is sustained by in vitro assays. Similarities and differences are found when it is compared to lipoproteins of only the three species of spiders studied.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Ciencias Exactas
Química
lipoproteins
hemocyanin
lipids
Arachnids
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/104770

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network_name_str SEDICI (UNLP)
spelling Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>Laino, AldanaCunningham, Mónica LilianaSuárez, GustavoGarcía, Carlos FernandoCiencias ExactasQuímicalipoproteinshemocyaninlipidsArachnidsLipids due to its hydrophobic nature are transported in the hemolymph mainly by lipoproteic fractions. In the present work we studied the lipoproteic fractions present in the hemolymph of the spider <i>Grammostola rosea</i>. Through ultracentrifugation two lipoproteic fractions are isolated, one of high density named Gr-HDL (δ = 1.13 - 1.15 g/ml) and the other of very high density called Gr-VHDL (δ = 1.24 - 1.27 g/ml) Gr-VHDL in hemolymph is majority in relation to Gr-HDL. In this sense Gr-VHDL fraction has 98.6% of hemolymphatic proteins, and 89.3% of lipids presents in the hemolymph. Both lipoproteic fractions possess phospholipids such as majority lipids (phosphatidylcholine and phosphatidylethanolamine) and 18:1, 16:0, 18:2 and 18:0 as the major fatty acids. In order to confirm the role played by lipoproteic fractions <i>in vitro</i> assays with different <sup>14</sup>C-lipid were performed. It was observed that Gr-VHDL takes up mainly free fatty acids and triacylglycerols unlike that observed for Gr-HDL in relation to phosphatidylcholine. Through electrophoresis it was observed that Gr-VHDL has three proteins: a predominant band of 68 kDa and two others of 99 and 121 kDa. Gr-HDL displayed a predominant band of 93 kDa, and other minority of 249 kDa. In conclusion, this study reports lipid characterization of the lipoproteic fractions present in the hemolymph of the tarantula, <i>G. rosea</i>. The role of each lipoproteic fraction in relation to lipid up- take is sustained by <i>in vitro</i> assays. Similarities and differences are found when it is compared to lipoproteins of only the three species of spiders studied.Instituto de Investigaciones Bioquímicas de La Plata2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf9-20http://sedici.unlp.edu.ar/handle/10915/104770enginfo:eu-repo/semantics/altIdentifier/url/http://hdl.handle.net/11336/49010info:eu-repo/semantics/altIdentifier/url/https://www.scirp.org/journal/paperinformation.aspx?paperid=52876info:eu-repo/semantics/altIdentifier/issn/2161-7597info:eu-repo/semantics/altIdentifier/doi/10.4236/ojas.2015.51002info:eu-repo/semantics/altIdentifier/hdl/11336/49010info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:03:35Zoai:sedici.unlp.edu.ar:10915/104770Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:03:36.111SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
title Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
spellingShingle Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
Laino, Aldana
Ciencias Exactas
Química
lipoproteins
hemocyanin
lipids
Arachnids
title_short Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
title_full Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
title_fullStr Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
title_full_unstemmed Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
title_sort Identification and Characterization of the Lipid Transport System in the Tarantula <i>Grammostola rosea</i>
dc.creator.none.fl_str_mv Laino, Aldana
Cunningham, Mónica Liliana
Suárez, Gustavo
García, Carlos Fernando
author Laino, Aldana
author_facet Laino, Aldana
Cunningham, Mónica Liliana
Suárez, Gustavo
García, Carlos Fernando
author_role author
author2 Cunningham, Mónica Liliana
Suárez, Gustavo
García, Carlos Fernando
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Química
lipoproteins
hemocyanin
lipids
Arachnids
topic Ciencias Exactas
Química
lipoproteins
hemocyanin
lipids
Arachnids
dc.description.none.fl_txt_mv Lipids due to its hydrophobic nature are transported in the hemolymph mainly by lipoproteic fractions. In the present work we studied the lipoproteic fractions present in the hemolymph of the spider <i>Grammostola rosea</i>. Through ultracentrifugation two lipoproteic fractions are isolated, one of high density named Gr-HDL (δ = 1.13 - 1.15 g/ml) and the other of very high density called Gr-VHDL (δ = 1.24 - 1.27 g/ml) Gr-VHDL in hemolymph is majority in relation to Gr-HDL. In this sense Gr-VHDL fraction has 98.6% of hemolymphatic proteins, and 89.3% of lipids presents in the hemolymph. Both lipoproteic fractions possess phospholipids such as majority lipids (phosphatidylcholine and phosphatidylethanolamine) and 18:1, 16:0, 18:2 and 18:0 as the major fatty acids. In order to confirm the role played by lipoproteic fractions <i>in vitro</i> assays with different <sup>14</sup>C-lipid were performed. It was observed that Gr-VHDL takes up mainly free fatty acids and triacylglycerols unlike that observed for Gr-HDL in relation to phosphatidylcholine. Through electrophoresis it was observed that Gr-VHDL has three proteins: a predominant band of 68 kDa and two others of 99 and 121 kDa. Gr-HDL displayed a predominant band of 93 kDa, and other minority of 249 kDa. In conclusion, this study reports lipid characterization of the lipoproteic fractions present in the hemolymph of the tarantula, <i>G. rosea</i>. The role of each lipoproteic fraction in relation to lipid up- take is sustained by <i>in vitro</i> assays. Similarities and differences are found when it is compared to lipoproteins of only the three species of spiders studied.
Instituto de Investigaciones Bioquímicas de La Plata
description Lipids due to its hydrophobic nature are transported in the hemolymph mainly by lipoproteic fractions. In the present work we studied the lipoproteic fractions present in the hemolymph of the spider <i>Grammostola rosea</i>. Through ultracentrifugation two lipoproteic fractions are isolated, one of high density named Gr-HDL (δ = 1.13 - 1.15 g/ml) and the other of very high density called Gr-VHDL (δ = 1.24 - 1.27 g/ml) Gr-VHDL in hemolymph is majority in relation to Gr-HDL. In this sense Gr-VHDL fraction has 98.6% of hemolymphatic proteins, and 89.3% of lipids presents in the hemolymph. Both lipoproteic fractions possess phospholipids such as majority lipids (phosphatidylcholine and phosphatidylethanolamine) and 18:1, 16:0, 18:2 and 18:0 as the major fatty acids. In order to confirm the role played by lipoproteic fractions <i>in vitro</i> assays with different <sup>14</sup>C-lipid were performed. It was observed that Gr-VHDL takes up mainly free fatty acids and triacylglycerols unlike that observed for Gr-HDL in relation to phosphatidylcholine. Through electrophoresis it was observed that Gr-VHDL has three proteins: a predominant band of 68 kDa and two others of 99 and 121 kDa. Gr-HDL displayed a predominant band of 93 kDa, and other minority of 249 kDa. In conclusion, this study reports lipid characterization of the lipoproteic fractions present in the hemolymph of the tarantula, <i>G. rosea</i>. The role of each lipoproteic fraction in relation to lipid up- take is sustained by <i>in vitro</i> assays. Similarities and differences are found when it is compared to lipoproteins of only the three species of spiders studied.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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info:eu-repo/semantics/altIdentifier/issn/2161-7597
info:eu-repo/semantics/altIdentifier/doi/10.4236/ojas.2015.51002
info:eu-repo/semantics/altIdentifier/hdl/11336/49010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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