Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | The Journal of venomous animals and toxins including tropical diseases (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100214 |
Resumo: | AbstractHyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus martensii, Polybia paulista and Tityus serrulatus venoms. These enzymes are employed as adjuvants to increase the absorption and dispersion of other drugs and have been used in various off-label clinical conditions to reduce tissue edema. Moreover, a PEGylated form of a recombinant human hyaluronidase is currently under clinical trials for the treatment of metastatic pancreatic cancer. This review focuses on the arthropod venom hyaluronidases and provides an overview of their biochemical properties, role in the envenoming, structure/activity relationship, and potential medical and biotechnological applications. |
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Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnologyHyaluronidaseScorpionSpiderCaterpillarHymenopteraInsectsCloningHeterologous expressionPEGylationBiotechnological applicationsAbstractHyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus martensii, Polybia paulista and Tityus serrulatus venoms. These enzymes are employed as adjuvants to increase the absorption and dispersion of other drugs and have been used in various off-label clinical conditions to reduce tissue edema. Moreover, a PEGylated form of a recombinant human hyaluronidase is currently under clinical trials for the treatment of metastatic pancreatic cancer. This review focuses on the arthropod venom hyaluronidases and provides an overview of their biochemical properties, role in the envenoming, structure/activity relationship, and potential medical and biotechnological applications.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2015-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100214Journal of Venomous Animals and Toxins including Tropical Diseases v.21 2015reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1186/s40409-015-0042info:eu-repo/semantics/openAccessBordon,Karla C FWiezel,Gisele A.Amorim,Fernanda G.Arantes,Eliane C.eng2015-11-13T00:00:00Zoai:scielo:S1678-91992015000100214Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2015-11-13T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology |
title |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology |
spellingShingle |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology Bordon,Karla C F Hyaluronidase Scorpion Spider Caterpillar Hymenoptera Insects Cloning Heterologous expression PEGylation Biotechnological applications |
title_short |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology |
title_full |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology |
title_fullStr |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology |
title_full_unstemmed |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology |
title_sort |
Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology |
author |
Bordon,Karla C F |
author_facet |
Bordon,Karla C F Wiezel,Gisele A. Amorim,Fernanda G. Arantes,Eliane C. |
author_role |
author |
author2 |
Wiezel,Gisele A. Amorim,Fernanda G. Arantes,Eliane C. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Bordon,Karla C F Wiezel,Gisele A. Amorim,Fernanda G. Arantes,Eliane C. |
dc.subject.por.fl_str_mv |
Hyaluronidase Scorpion Spider Caterpillar Hymenoptera Insects Cloning Heterologous expression PEGylation Biotechnological applications |
topic |
Hyaluronidase Scorpion Spider Caterpillar Hymenoptera Insects Cloning Heterologous expression PEGylation Biotechnological applications |
description |
AbstractHyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus martensii, Polybia paulista and Tityus serrulatus venoms. These enzymes are employed as adjuvants to increase the absorption and dispersion of other drugs and have been used in various off-label clinical conditions to reduce tissue edema. Moreover, a PEGylated form of a recombinant human hyaluronidase is currently under clinical trials for the treatment of metastatic pancreatic cancer. This review focuses on the arthropod venom hyaluronidases and provides an overview of their biochemical properties, role in the envenoming, structure/activity relationship, and potential medical and biotechnological applications. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100214 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100214 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1186/s40409-015-0042 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP) |
publisher.none.fl_str_mv |
Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP) |
dc.source.none.fl_str_mv |
Journal of Venomous Animals and Toxins including Tropical Diseases v.21 2015 reponame:The Journal of venomous animals and toxins including tropical diseases (Online) instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
The Journal of venomous animals and toxins including tropical diseases (Online) |
collection |
The Journal of venomous animals and toxins including tropical diseases (Online) |
repository.name.fl_str_mv |
The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
||editorial@jvat.org.br |
_version_ |
1748958539675598848 |