Marine Invertebrates
Proteolytic enzymes, also known as peptidases, are critical in all living organisms. Peptidases control the cleavage, activation, turnover, and synthesis of proteins and regulate many biochemical and physiological processes. They are also involved in several pathophysiological processes. Among pepti...
| Autores: | , , , , , , , , |
|---|---|
| Formato: | artículo |
| Fecha de publicación: | 2023 |
| País: | España |
| Recursos: | Universitat Autònoma de Barcelona |
| Repositorio: | Dipòsit Digital de Documents de la UAB |
| Idioma: | inglés |
| OAI Identifier: | oai:ddd.uab.cat:283088 |
| Acesso em linha: | https://ddd.uab.cat/record/283088 https://dx.doi.org/urn:doi:10.3390/md21050279 |
| Access Level: | acceso abierto |
| Palavra-chave: | Aminopeptidase Aminopeptidase N Aminopeptidase A TRH-degrading ectoenzyme Leucyl aminopeptidase Enzyme inhibitors Drug-oriented inhibitors Marine invertebrates |
| id |
ES_e625150fc17a9f1a94de70e9ba586de6 |
|---|---|
| oai_identifier_str |
oai:ddd.uab.cat:283088 |
| network_acronym_str |
ES |
| network_name_str |
España |
| repository_id_str |
|
| spelling |
Marine InvertebratesA Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 FamiliesPascual Alonso, IselAlmeida García, Fabiola|||0000-0001-9581-2586Valdés Tresanco, Mario ErnestoArrebola Sánchez, YariniOjeda del Sol, DanielSánchez Ramírez, BelindaFlorent, Isabelle|||0000-0002-7140-6417Schmitt, MarjorieAvilés, Francesc Xavier|||0000-0002-1399-6789AminopeptidaseAminopeptidase NAminopeptidase ATRH-degrading ectoenzymeLeucyl aminopeptidaseEnzyme inhibitorsDrug-oriented inhibitorsMarine invertebratesProteolytic enzymes, also known as peptidases, are critical in all living organisms. Peptidases control the cleavage, activation, turnover, and synthesis of proteins and regulate many biochemical and physiological processes. They are also involved in several pathophysiological processes. Among peptidases, aminopeptidases catalyze the cleavage of the N-terminal amino acids of proteins or peptide substrates. They are distributed in many phyla and play critical roles in physiology and pathophysiology. Many of them are metallopeptidases belonging to the M1 and M17 families, among others. Some, such as M1 aminopeptidases N and A, thyrotropin-releasing hormone-degrading ectoenzyme, and M17 leucyl aminopeptidase, are targets for the development of therapeutic agents for human diseases, including cancer, hypertension, central nervous system disorders, inflammation, immune system disorders, skin pathologies, and infectious diseases, such as malaria. The relevance of aminopeptidases has driven the search and identification of potent and selective inhibitors as major tools to control proteolysis with an impact in biochemistry, biotechnology, and biomedicine. The present contribution focuses on marine invertebrate biodiversity as an important and promising source of inhibitors of metalloaminopeptidases from M1 and M17 families, with foreseen biomedical applications in human diseases. The results reviewed in the present contribution support and encourage further studies with inhibitors isolated from marine invertebrates in different biomedical models associated with the activity of these families of exopeptidases.Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular 22023-01-0120232023-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/283088https://dx.doi.org/urn:doi:10.3390/md21050279reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:2830882026-06-06T12:50:31Z |
| dc.title.none.fl_str_mv |
Marine Invertebrates A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families |
| title |
Marine Invertebrates |
| spellingShingle |
Marine Invertebrates Pascual Alonso, Isel Aminopeptidase Aminopeptidase N Aminopeptidase A TRH-degrading ectoenzyme Leucyl aminopeptidase Enzyme inhibitors Drug-oriented inhibitors Marine invertebrates |
| title_short |
Marine Invertebrates |
| title_full |
Marine Invertebrates |
| title_fullStr |
Marine Invertebrates |
| title_full_unstemmed |
Marine Invertebrates |
| title_sort |
Marine Invertebrates |
| dc.creator.none.fl_str_mv |
Pascual Alonso, Isel Almeida García, Fabiola|||0000-0001-9581-2586 Valdés Tresanco, Mario Ernesto Arrebola Sánchez, Yarini Ojeda del Sol, Daniel Sánchez Ramírez, Belinda Florent, Isabelle|||0000-0002-7140-6417 Schmitt, Marjorie Avilés, Francesc Xavier|||0000-0002-1399-6789 |
| author |
Pascual Alonso, Isel |
| author_facet |
Pascual Alonso, Isel Almeida García, Fabiola|||0000-0001-9581-2586 Valdés Tresanco, Mario Ernesto Arrebola Sánchez, Yarini Ojeda del Sol, Daniel Sánchez Ramírez, Belinda Florent, Isabelle|||0000-0002-7140-6417 Schmitt, Marjorie Avilés, Francesc Xavier|||0000-0002-1399-6789 |
| author_role |
author |
| author2 |
Almeida García, Fabiola|||0000-0001-9581-2586 Valdés Tresanco, Mario Ernesto Arrebola Sánchez, Yarini Ojeda del Sol, Daniel Sánchez Ramírez, Belinda Florent, Isabelle|||0000-0002-7140-6417 Schmitt, Marjorie Avilés, Francesc Xavier|||0000-0002-1399-6789 |
| author2_role |
author author author author author author author author |
| dc.contributor.none.fl_str_mv |
Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular |
| dc.subject.none.fl_str_mv |
Aminopeptidase Aminopeptidase N Aminopeptidase A TRH-degrading ectoenzyme Leucyl aminopeptidase Enzyme inhibitors Drug-oriented inhibitors Marine invertebrates |
| topic |
Aminopeptidase Aminopeptidase N Aminopeptidase A TRH-degrading ectoenzyme Leucyl aminopeptidase Enzyme inhibitors Drug-oriented inhibitors Marine invertebrates |
| description |
Proteolytic enzymes, also known as peptidases, are critical in all living organisms. Peptidases control the cleavage, activation, turnover, and synthesis of proteins and regulate many biochemical and physiological processes. They are also involved in several pathophysiological processes. Among peptidases, aminopeptidases catalyze the cleavage of the N-terminal amino acids of proteins or peptide substrates. They are distributed in many phyla and play critical roles in physiology and pathophysiology. Many of them are metallopeptidases belonging to the M1 and M17 families, among others. Some, such as M1 aminopeptidases N and A, thyrotropin-releasing hormone-degrading ectoenzyme, and M17 leucyl aminopeptidase, are targets for the development of therapeutic agents for human diseases, including cancer, hypertension, central nervous system disorders, inflammation, immune system disorders, skin pathologies, and infectious diseases, such as malaria. The relevance of aminopeptidases has driven the search and identification of potent and selective inhibitors as major tools to control proteolysis with an impact in biochemistry, biotechnology, and biomedicine. The present contribution focuses on marine invertebrate biodiversity as an important and promising source of inhibitors of metalloaminopeptidases from M1 and M17 families, with foreseen biomedical applications in human diseases. The results reviewed in the present contribution support and encourage further studies with inhibitors isolated from marine invertebrates in different biomedical models associated with the activity of these families of exopeptidases. |
| publishDate |
2023 |
| dc.date.none.fl_str_mv |
2 2023-01-01 2023 2023-01-01 |
| dc.type.none.fl_str_mv |
Article http://purl.org/coar/resource_type/c_6501 VoR http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| dc.type.openaire.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| dc.identifier.none.fl_str_mv |
https://ddd.uab.cat/record/283088 https://dx.doi.org/urn:doi:10.3390/md21050279 |
| url |
https://ddd.uab.cat/record/283088 https://dx.doi.org/urn:doi:10.3390/md21050279 |
| dc.language.none.fl_str_mv |
Inglés eng |
| language_invalid_str_mv |
Inglés |
| language |
eng |
| dc.rights.none.fl_str_mv |
open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
| dc.rights.openaire.fl_str_mv |
info:eu-repo/semantics/openAccess |
| rights_invalid_str_mv |
open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
application/pdf |
| dc.source.none.fl_str_mv |
reponame:Dipòsit Digital de Documents de la UAB instname:Universitat Autònoma de Barcelona |
| instname_str |
Universitat Autònoma de Barcelona |
| reponame_str |
Dipòsit Digital de Documents de la UAB |
| collection |
Dipòsit Digital de Documents de la UAB |
| repository.name.fl_str_mv |
|
| repository.mail.fl_str_mv |
|
| _version_ |
1869422741505966080 |
| score |
15,300719 |