Integrins, cancer and snake toxins (mini-review)

Detalhes bibliográficos
Autor(a) principal: Rádis-Baptista,G.
Data de Publicação: 2005
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=S1678-91992005000300002
Resumo: Integrins encompass a family of transmembrane heterodimeric proteins of adhesion that maintain cells attached to other cells and to the extracellular matrix (ECM). Integrins work as bi-directional mechanotransducers, conveying mechanical signal from outside to inside the cell through a cascade of phosphorylation signals. On the other hand, the signal from inside to outside controls the strength and affinity of integrin adhesion. As proteins of focal contact, integrins are involved in diverse cell functions, such as cell activation, migration, growth, and survival. In the development of neoplastic disease and metastatic tumor, integrins can influence cancer invasiveness and progression, as well as mediate the formation of new blood vessels (angiogenesis). Diverse snake venom toxins have the ability to interact with multiple integrins, what results in inhibition of cell attachment, inhibition of angiogenesis, and induction of apoptotic death of tumor and vascular endothelial cells. The aim of this review is to present data about snake venom toxins that bind to integrins and evoke antiangiogenesis and antitumoral effects.
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spelling Integrins, cancer and snake toxins (mini-review)integrinangiogenesiscancerapoptosissnake toxinsnake venom C-type lectinmetalloproteasedisintegrinIntegrins encompass a family of transmembrane heterodimeric proteins of adhesion that maintain cells attached to other cells and to the extracellular matrix (ECM). Integrins work as bi-directional mechanotransducers, conveying mechanical signal from outside to inside the cell through a cascade of phosphorylation signals. On the other hand, the signal from inside to outside controls the strength and affinity of integrin adhesion. As proteins of focal contact, integrins are involved in diverse cell functions, such as cell activation, migration, growth, and survival. In the development of neoplastic disease and metastatic tumor, integrins can influence cancer invasiveness and progression, as well as mediate the formation of new blood vessels (angiogenesis). Diverse snake venom toxins have the ability to interact with multiple integrins, what results in inhibition of cell attachment, inhibition of angiogenesis, and induction of apoptotic death of tumor and vascular endothelial cells. The aim of this review is to present data about snake venom toxins that bind to integrins and evoke antiangiogenesis and antitumoral effects.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2005-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992005000300002Journal of Venomous Animals and Toxins including Tropical Diseases v.11 n.3 2005reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1590/S1678-91992005000300002info:eu-repo/semantics/openAccessRádis-Baptista,G.eng2005-08-16T00:00:00Zoai:scielo:S1678-91992005000300002Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2005-08-16T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Integrins, cancer and snake toxins (mini-review)
title Integrins, cancer and snake toxins (mini-review)
spellingShingle Integrins, cancer and snake toxins (mini-review)
Rádis-Baptista,G.
integrin
angiogenesis
cancer
apoptosis
snake toxin
snake venom C-type lectin
metalloprotease
disintegrin
title_short Integrins, cancer and snake toxins (mini-review)
title_full Integrins, cancer and snake toxins (mini-review)
title_fullStr Integrins, cancer and snake toxins (mini-review)
title_full_unstemmed Integrins, cancer and snake toxins (mini-review)
title_sort Integrins, cancer and snake toxins (mini-review)
author Rádis-Baptista,G.
author_facet Rádis-Baptista,G.
author_role author
dc.contributor.author.fl_str_mv Rádis-Baptista,G.
dc.subject.por.fl_str_mv integrin
angiogenesis
cancer
apoptosis
snake toxin
snake venom C-type lectin
metalloprotease
disintegrin
topic integrin
angiogenesis
cancer
apoptosis
snake toxin
snake venom C-type lectin
metalloprotease
disintegrin
description Integrins encompass a family of transmembrane heterodimeric proteins of adhesion that maintain cells attached to other cells and to the extracellular matrix (ECM). Integrins work as bi-directional mechanotransducers, conveying mechanical signal from outside to inside the cell through a cascade of phosphorylation signals. On the other hand, the signal from inside to outside controls the strength and affinity of integrin adhesion. As proteins of focal contact, integrins are involved in diverse cell functions, such as cell activation, migration, growth, and survival. In the development of neoplastic disease and metastatic tumor, integrins can influence cancer invasiveness and progression, as well as mediate the formation of new blood vessels (angiogenesis). Diverse snake venom toxins have the ability to interact with multiple integrins, what results in inhibition of cell attachment, inhibition of angiogenesis, and induction of apoptotic death of tumor and vascular endothelial cells. The aim of this review is to present data about snake venom toxins that bind to integrins and evoke antiangiogenesis and antitumoral effects.
publishDate 2005
dc.date.none.fl_str_mv 2005-09-01
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=S1678-91992005000300002
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992005000300002
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1678-91992005000300002
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.11 n.3 2005
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
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