Hyalectanase Activities by the ADAMTS Metalloproteases.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
15 Mar 2021
Historique:
received: 15 02 2021
revised: 07 03 2021
accepted: 11 03 2021
entrez: 3 4 2021
pubmed: 4 4 2021
medline: 24 4 2021
Statut: epublish

Résumé

The hyalectan family is composed of the proteoglycans aggrecan, versican, brevican and neurocan. Hyalectans, also known as lecticans, are components of the extracellular matrix of different tissues and play essential roles in key biological processes including skeletal development, and they are related to the correct maintenance of the vascular and central nervous system. For instance, hyalectans participate in the organization of structures such as perineural nets and in the regulation of neurite outgrowth or brain recovery following a traumatic injury. The ADAMTS (A Disintegrin and Metalloprotease domains, with thrombospondin motifs) family consists of 19 secreted metalloproteases. These enzymes also perform important roles in the structural organization and function of the extracellular matrix through interactions with other matrix components or as a consequence of their catalytic activity. In this regard, some of their preferred substrates are the hyalectans. In fact, ADAMTSs cleave hyalectans not only as a mechanism for clearance or turnover of proteoglycans but also to generate bioactive fragments which display specific functions. In this article we review some of the physiological and pathological effects derived from cleavages of hyalectans mediated by ADAMTSs.

Identifiants

pubmed: 33804223
pii: ijms22062988
doi: 10.3390/ijms22062988
pmc: PMC8000579
pii:
doi:

Substances chimiques

Hyalectins 0
Thrombospondins 0
Versicans 126968-45-4
ADAMTS Proteins EC 3.4.24.-

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Ministerio de Ciencia, Innovación y Universidades
ID : RTI2018-099756B-100

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Auteurs

Tania Fontanil (T)

Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, 33006 Oviedo, Spain.
Departamento de Investigación, Instituto Ordóñez, 33012 Oviedo, Spain.

Yamina Mohamedi (Y)

Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, 33006 Oviedo, Spain.

Jorge Espina-Casado (J)

Departamento de Química Física y Analítica, Universidad de Oviedo, 33006 Oviedo, Spain.

Álvaro J Obaya (ÁJ)

Departamento de Biología Funcional, Área de Fisiología, Universidad de Oviedo, 33006 Oviedo, Spain.
Instituto Universitario de Oncología, IUOPA, Universidad de Oviedo, 33006 Oviedo, Spain.

Teresa Cobo (T)

Departamento de Cirugía y Especialidades Médico-Quirúrgicas, Universidad de Oviedo, 33006 Oviedo, Spain.
Instituto Asturiano de Odontología, 33006 Oviedo, Spain.

Santiago Cal (S)

Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, 33006 Oviedo, Spain.
Instituto Universitario de Oncología, IUOPA, Universidad de Oviedo, 33006 Oviedo, Spain.

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Classifications MeSH