Proteases and their inhibitors in coagulation and inflammation
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Capítulo de livro |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRN |
Texto Completo: | https://repositorio.ufrn.br/handle/123456789/32802 |
Resumo: | Proteases or peptidases are molecules that promote cleavage through the hydrolysis of peptide bonds present in proteins and polypeptides, transforming them into smaller amino acid or polypeptide residues. The group of serine proteases is predominant in peptidases and is found in almost all living organisms, constituting the family of proteases best characterized and physiologically versatile. Within the serine proteases are protease inhibitors, proteins capable of blocking and / or inhibiting the catalytic activity of proteolytic enzymes, being found naturally in most living organisms. In serine protease inhibitors, two distinct categories have already been classified, entrapment inhibitors and high affinity inhibitors. The hemostatic system participates in maintaining balance in living organisms, maintaining adequate blood pressure and perfusion, controlling bleeding caused by damage to blood vessels, through processes known as coagulation, where most factors in the coagulation cascade are serine proteases or cofactors . Among the most important serine proteases that act in the coagulation cascade are some coagulation factors (II, VII, IX, X, XI, XII, for example), the vasodilating molecule kallikrein, which is also a serine protease that acts on various substrates releasing vasoactive peptides, exercising their natural functions. In disorders in this cascade, medicine uses inhibitors with anticoagulant action, managing to reverse or inhibit these diseases. In inflammatory reactions, which is an essential step for controlling microbial invasion or tissue damage, as well as for maintaining tissue homeostasis, neutrophils secrete serine proteases such as neutrophil elastase (NE1), proteinase 3 (PR3) and cathepsin G ( CG), which are components of one of the most important molecular arsenals for the defense of the organism. Therefore, these facts suggest that new studies in this area are of great relevance to the evolution of science and medicine |
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Santos, Jorge Anderson Nascimento dosMarques Neto, Antônio MoreiraFrança, Anderson Felipe Jácome deSantos, Yago Queiroz dosCarelli, Gabriella Silva CamposCruz, Joelton Igor Oliveira daRabêlo, Luciana Maria AraújoVeras, Bruno Oliveira deMoura, Geovanna Maria de Medeiros2021-07-05T12:19:55Z2021-07-05T12:19:55Z2020SANTOS, Jorge Anderson Nascimento dos et al. Proteases and their inhibitors in coagulation and inflammation. In: SILVA, Edson da (Org.). Tópicos Multidisciplinares em Ciências Biológicas 3. 1. ed. Ponta Grossa, PR: Atena Editora, 2020. p. 6-16978-65-5706-226-5https://repositorio.ufrn.br/handle/123456789/3280210.22533/at.ed.265202407Proteases or peptidases are molecules that promote cleavage through the hydrolysis of peptide bonds present in proteins and polypeptides, transforming them into smaller amino acid or polypeptide residues. The group of serine proteases is predominant in peptidases and is found in almost all living organisms, constituting the family of proteases best characterized and physiologically versatile. Within the serine proteases are protease inhibitors, proteins capable of blocking and / or inhibiting the catalytic activity of proteolytic enzymes, being found naturally in most living organisms. In serine protease inhibitors, two distinct categories have already been classified, entrapment inhibitors and high affinity inhibitors. The hemostatic system participates in maintaining balance in living organisms, maintaining adequate blood pressure and perfusion, controlling bleeding caused by damage to blood vessels, through processes known as coagulation, where most factors in the coagulation cascade are serine proteases or cofactors . Among the most important serine proteases that act in the coagulation cascade are some coagulation factors (II, VII, IX, X, XI, XII, for example), the vasodilating molecule kallikrein, which is also a serine protease that acts on various substrates releasing vasoactive peptides, exercising their natural functions. In disorders in this cascade, medicine uses inhibitors with anticoagulant action, managing to reverse or inhibit these diseases. In inflammatory reactions, which is an essential step for controlling microbial invasion or tissue damage, as well as for maintaining tissue homeostasis, neutrophils secrete serine proteases such as neutrophil elastase (NE1), proteinase 3 (PR3) and cathepsin G ( CG), which are components of one of the most important molecular arsenals for the defense of the organism. Therefore, these facts suggest that new studies in this area are of great relevance to the evolution of science and medicineProteases ou peptidases são moléculas que promovem a clivagem através da hidrólise de ligações peptídicas presentes em proteínas e polipeptídeos, transformando os em resíduos de aminoácidos ou polipeptídeos menores. O grupo das serina-proteases é predominante nas peptidases e é encontrado em quase todos os organismos vivos, constituindo a família de proteases melhor caracterizadas e fisiologicamente versáteis. Dentro das serino-proteases estão os inibidores de protease, proteínas capazes de bloquear e/ou inibir a atividade catalítica das enzimas proteolíticas, sendo encontradas naturalmente na maioria dos organismos vivos. Nos inibidores de proteases de serina, já foram classificadas duas categorias distintas, os inibidores de aprisionamento e inibidores de alta afinidade. O sistema hemostático participa da manutenção do equilíbrio nos organismos vivos, mantendo pressão e perfusão sanguínea adequadas, controlando o sangramento causado por danos aos vasos sanguíneos, através de processos conhecidos como coagulação, onde a maioria dos fatores na cascata de coagulação são serina proteases ou cofatores. Entre as serina proteases mais importantes que atuam na cascata de coagulação estão alguns fatores de coagulação (II, VII, IX, X, XI, XII, por exemplo), a molécula vasodilatadora calicreína, que também é uma serina protease que atua em vários substratos liberando vasoativo peptídeos, exercendo suas funções naturais. Em distúrbios nessa cascata, a medicina utiliza de inibidores com ação anticoagulante, conseguindo reverter ou inibir essas doenças. Nas reações Inflamatórias, que é uma etapa essencial para o controle da invasão microbiana ou lesão tecidual, bem como para a manutenção da homeostase tecidual, os neutrófilos secretam serina proteases como elastase de neutrófilos (NE1), proteinase 3 (PR3) e catepsina G (CG), que são componentes de um dos arsenais moleculares mais importantes para a defesa do organismo. Sendo assim, esses fatos sugerem que novos estudos nessa área são de grande relevância para a evolução da ciência e medicinaAtena EditoraAttribution 3.0 Brazilhttp://creativecommons.org/licenses/by/3.0/br/info:eu-repo/semantics/openAccessProteasesInibidores de proteasesCoagulaçãoProteasesProtease inhibitorsCoagulationProteases and their inhibitors in coagulation and inflammationProteases e seus inibidores nos processos de coagulação e inflamaçãoinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookPartengreponame:Repositório Institucional da UFRNinstname:Universidade Federal do Rio Grande do Norte (UFRN)instacron:UFRNORIGINALProteasesInhibitorsCoagulation_Franca_2020.pdfProteasesInhibitorsCoagulation_Franca_2020.pdfapplication/pdf602485https://repositorio.ufrn.br/bitstream/123456789/32802/1/ProteasesInhibitorsCoagulation_Franca_2020.pdf7b39dd5516b22875ec769db11211ba71MD51CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8914https://repositorio.ufrn.br/bitstream/123456789/32802/2/license_rdf4d2950bda3d176f570a9f8b328dfbbefMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81484https://repositorio.ufrn.br/bitstream/123456789/32802/3/license.txte9597aa2854d128fd968be5edc8a28d9MD53123456789/328022022-04-12 14:31:37.345oai:https://repositorio.ufrn.br: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Repositório de PublicaçõesPUBhttp://repositorio.ufrn.br/oai/opendoar:2022-04-12T17:31:37Repositório Institucional da UFRN - Universidade Federal do Rio Grande do Norte (UFRN)false |
dc.title.pt_BR.fl_str_mv |
Proteases and their inhibitors in coagulation and inflammation |
dc.title.alternative.pt_BR.fl_str_mv |
Proteases e seus inibidores nos processos de coagulação e inflamação |
title |
Proteases and their inhibitors in coagulation and inflammation |
spellingShingle |
Proteases and their inhibitors in coagulation and inflammation Santos, Jorge Anderson Nascimento dos Proteases Inibidores de proteases Coagulação Proteases Protease inhibitors Coagulation |
title_short |
Proteases and their inhibitors in coagulation and inflammation |
title_full |
Proteases and their inhibitors in coagulation and inflammation |
title_fullStr |
Proteases and their inhibitors in coagulation and inflammation |
title_full_unstemmed |
Proteases and their inhibitors in coagulation and inflammation |
title_sort |
Proteases and their inhibitors in coagulation and inflammation |
author |
Santos, Jorge Anderson Nascimento dos |
author_facet |
Santos, Jorge Anderson Nascimento dos Marques Neto, Antônio Moreira França, Anderson Felipe Jácome de Santos, Yago Queiroz dos Carelli, Gabriella Silva Campos Cruz, Joelton Igor Oliveira da Rabêlo, Luciana Maria Araújo Veras, Bruno Oliveira de Moura, Geovanna Maria de Medeiros |
author_role |
author |
author2 |
Marques Neto, Antônio Moreira França, Anderson Felipe Jácome de Santos, Yago Queiroz dos Carelli, Gabriella Silva Campos Cruz, Joelton Igor Oliveira da Rabêlo, Luciana Maria Araújo Veras, Bruno Oliveira de Moura, Geovanna Maria de Medeiros |
author2_role |
author author author author author author author author |
dc.contributor.author.fl_str_mv |
Santos, Jorge Anderson Nascimento dos Marques Neto, Antônio Moreira França, Anderson Felipe Jácome de Santos, Yago Queiroz dos Carelli, Gabriella Silva Campos Cruz, Joelton Igor Oliveira da Rabêlo, Luciana Maria Araújo Veras, Bruno Oliveira de Moura, Geovanna Maria de Medeiros |
dc.subject.por.fl_str_mv |
Proteases Inibidores de proteases Coagulação Proteases Protease inhibitors Coagulation |
topic |
Proteases Inibidores de proteases Coagulação Proteases Protease inhibitors Coagulation |
description |
Proteases or peptidases are molecules that promote cleavage through the hydrolysis of peptide bonds present in proteins and polypeptides, transforming them into smaller amino acid or polypeptide residues. The group of serine proteases is predominant in peptidases and is found in almost all living organisms, constituting the family of proteases best characterized and physiologically versatile. Within the serine proteases are protease inhibitors, proteins capable of blocking and / or inhibiting the catalytic activity of proteolytic enzymes, being found naturally in most living organisms. In serine protease inhibitors, two distinct categories have already been classified, entrapment inhibitors and high affinity inhibitors. The hemostatic system participates in maintaining balance in living organisms, maintaining adequate blood pressure and perfusion, controlling bleeding caused by damage to blood vessels, through processes known as coagulation, where most factors in the coagulation cascade are serine proteases or cofactors . Among the most important serine proteases that act in the coagulation cascade are some coagulation factors (II, VII, IX, X, XI, XII, for example), the vasodilating molecule kallikrein, which is also a serine protease that acts on various substrates releasing vasoactive peptides, exercising their natural functions. In disorders in this cascade, medicine uses inhibitors with anticoagulant action, managing to reverse or inhibit these diseases. In inflammatory reactions, which is an essential step for controlling microbial invasion or tissue damage, as well as for maintaining tissue homeostasis, neutrophils secrete serine proteases such as neutrophil elastase (NE1), proteinase 3 (PR3) and cathepsin G ( CG), which are components of one of the most important molecular arsenals for the defense of the organism. Therefore, these facts suggest that new studies in this area are of great relevance to the evolution of science and medicine |
publishDate |
2020 |
dc.date.issued.fl_str_mv |
2020 |
dc.date.accessioned.fl_str_mv |
2021-07-05T12:19:55Z |
dc.date.available.fl_str_mv |
2021-07-05T12:19:55Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/bookPart |
format |
bookPart |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
SANTOS, Jorge Anderson Nascimento dos et al. Proteases and their inhibitors in coagulation and inflammation. In: SILVA, Edson da (Org.). Tópicos Multidisciplinares em Ciências Biológicas 3. 1. ed. Ponta Grossa, PR: Atena Editora, 2020. p. 6-16 |
dc.identifier.uri.fl_str_mv |
https://repositorio.ufrn.br/handle/123456789/32802 |
dc.identifier.isbn.none.fl_str_mv |
978-65-5706-226-5 |
dc.identifier.doi.none.fl_str_mv |
10.22533/at.ed.265202407 |
identifier_str_mv |
SANTOS, Jorge Anderson Nascimento dos et al. Proteases and their inhibitors in coagulation and inflammation. In: SILVA, Edson da (Org.). Tópicos Multidisciplinares em Ciências Biológicas 3. 1. ed. Ponta Grossa, PR: Atena Editora, 2020. p. 6-16 978-65-5706-226-5 10.22533/at.ed.265202407 |
url |
https://repositorio.ufrn.br/handle/123456789/32802 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
Attribution 3.0 Brazil http://creativecommons.org/licenses/by/3.0/br/ info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Attribution 3.0 Brazil http://creativecommons.org/licenses/by/3.0/br/ |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
Atena Editora |
publisher.none.fl_str_mv |
Atena Editora |
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reponame:Repositório Institucional da UFRN instname:Universidade Federal do Rio Grande do Norte (UFRN) instacron:UFRN |
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