ADAMTS-12: Functions and Challenges for a Complex Metalloprotease
Nineteen members of the ADAMTS family of secreted zinc metalloproteinases are present in the human degradome. A wide range of different functions are being attributed to these enzymes and the number of their known substrates is considerably increasing in recent years. ADAMTSs can participate in proc...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2021-04-01
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| Series: | Frontiers in Molecular Biosciences |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2021.686763/full |
| _version_ | 1818728303839674368 |
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| author | Yamina Mohamedi Tania Fontanil Tania Fontanil Santiago Cal Santiago Cal Teresa Cobo Teresa Cobo Álvaro J. Obaya Álvaro J. Obaya |
| author_facet | Yamina Mohamedi Tania Fontanil Tania Fontanil Santiago Cal Santiago Cal Teresa Cobo Teresa Cobo Álvaro J. Obaya Álvaro J. Obaya |
| author_sort | Yamina Mohamedi |
| collection | DOAJ |
| description | Nineteen members of the ADAMTS family of secreted zinc metalloproteinases are present in the human degradome. A wide range of different functions are being attributed to these enzymes and the number of their known substrates is considerably increasing in recent years. ADAMTSs can participate in processes such as fertility, inflammation, arthritis, neuronal and behavioral disorders, as well as cancer. Since its first annotation in 2001, ADAMTS-12 has been described to participate in different processes displayed by members of this family of proteinases. In this sense, ADAMTS-12 performs essential roles in modulation and recovery from inflammatory processes such as colitis, endotoxic sepsis and pancreatitis. ADAMTS-12 has also been involved in cancer development acting either as a tumor suppressor or as a pro-tumoral agent. Furthermore, participation of ADAMTS-12 in arthritis or in neuronal disorders has also been suggested through degradation of components of the extracellular matrix. In addition, ADAMTS-12 proteinase activity can also be modified by interaction with other proteins and thus, can be an alternative way of modulating ADAMTS-12 functions. In this review we revised the most relevant findings about ADAMTS-12 function on the 20th anniversary of its identification. |
| first_indexed | 2024-12-17T22:27:51Z |
| format | Article |
| id | doaj.art-99f9462c2a1047a0a832c4df60b24c2f |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-17T22:27:51Z |
| publishDate | 2021-04-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-99f9462c2a1047a0a832c4df60b24c2f2022-12-21T21:30:19ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2021-04-01810.3389/fmolb.2021.686763686763ADAMTS-12: Functions and Challenges for a Complex MetalloproteaseYamina Mohamedi0Tania Fontanil1Tania Fontanil2Santiago Cal3Santiago Cal4Teresa Cobo5Teresa Cobo6Álvaro J. Obaya7Álvaro J. Obaya8Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Oviedo, SpainDepartamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Oviedo, SpainDepartamento de Investigación, Instituto Ordóñez, Oviedo, SpainDepartamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Oviedo, SpainInstituto Universitario de Oncología, IUOPA, Universidad de Oviedo, Oviedo, SpainDepartamento de Cirugía y Especialidades Médico-Quirúrgicas, Universidad de Oviedo, Oviedo, SpainInstituto Asturiano de Odontología, Oviedo, SpainInstituto Universitario de Oncología, IUOPA, Universidad de Oviedo, Oviedo, SpainDepartamento de Biología Funcional, Área de Fisiología, Universidad de Oviedo, Oviedo, SpainNineteen members of the ADAMTS family of secreted zinc metalloproteinases are present in the human degradome. A wide range of different functions are being attributed to these enzymes and the number of their known substrates is considerably increasing in recent years. ADAMTSs can participate in processes such as fertility, inflammation, arthritis, neuronal and behavioral disorders, as well as cancer. Since its first annotation in 2001, ADAMTS-12 has been described to participate in different processes displayed by members of this family of proteinases. In this sense, ADAMTS-12 performs essential roles in modulation and recovery from inflammatory processes such as colitis, endotoxic sepsis and pancreatitis. ADAMTS-12 has also been involved in cancer development acting either as a tumor suppressor or as a pro-tumoral agent. Furthermore, participation of ADAMTS-12 in arthritis or in neuronal disorders has also been suggested through degradation of components of the extracellular matrix. In addition, ADAMTS-12 proteinase activity can also be modified by interaction with other proteins and thus, can be an alternative way of modulating ADAMTS-12 functions. In this review we revised the most relevant findings about ADAMTS-12 function on the 20th anniversary of its identification.https://www.frontiersin.org/articles/10.3389/fmolb.2021.686763/fullADAMTS-12matrix metalloproteaseinflammationarthritisschizophreniacancer |
| spellingShingle | Yamina Mohamedi Tania Fontanil Tania Fontanil Santiago Cal Santiago Cal Teresa Cobo Teresa Cobo Álvaro J. Obaya Álvaro J. Obaya ADAMTS-12: Functions and Challenges for a Complex Metalloprotease Frontiers in Molecular Biosciences ADAMTS-12 matrix metalloprotease inflammation arthritis schizophrenia cancer |
| title | ADAMTS-12: Functions and Challenges for a Complex Metalloprotease |
| title_full | ADAMTS-12: Functions and Challenges for a Complex Metalloprotease |
| title_fullStr | ADAMTS-12: Functions and Challenges for a Complex Metalloprotease |
| title_full_unstemmed | ADAMTS-12: Functions and Challenges for a Complex Metalloprotease |
| title_short | ADAMTS-12: Functions and Challenges for a Complex Metalloprotease |
| title_sort | adamts 12 functions and challenges for a complex metalloprotease |
| topic | ADAMTS-12 matrix metalloprotease inflammation arthritis schizophrenia cancer |
| url | https://www.frontiersin.org/articles/10.3389/fmolb.2021.686763/full |
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