Collagen, glycosaminoglycans and matrix metalloproteinase-2 and metalloproteinase-9 in the cervix of the ewe during prepubertal development.


Journal

Anatomia, histologia, embryologia
ISSN: 1439-0264
Titre abrégé: Anat Histol Embryol
Pays: Germany
ID NLM: 7704218

Informations de publication

Date de publication:
Jul 2019
Historique:
received: 11 06 2018
revised: 06 12 2018
accepted: 02 03 2019
pubmed: 25 3 2019
medline: 18 12 2019
entrez: 26 3 2019
Statut: ppublish

Résumé

The tortuous nature of the ovine cervix restricts the transcervical passage of the cannula, and many studies have aimed to understand the endocrine mechanism of the remodelling of cervical tissue in adult ewe. However, little is known about the remodelling of the cervical tissue during the prepubertal development of the lambs. To obtain histochemical and biochemical evidence about the nature of the prepubertal development of the cervix of the ewe, cervices of Corriedale lambs obtained at 0, 1, 2, 4, 6 and 8 months of age (n = 5 to 6 in each) were processed. Neutral and acidic glycosaminoglycans (by PAS-Alcian stain) were weakly in the cervical stroma and not shown change during the development, whereas the percentage volume of fibrillar collagen (by van Gieson stain) increases throughout the experimental period in the superficial fold stroma and deep wall stroma (p < 0.05). The relative cervical weight (g/kg of body weight) and the collagen concentration (by spectrophotometry, mg/mg wet tissue) showed an early decreasing phase from months 0 to 4 and a later increasing phase from months 4 to 8 (p < 0.05). The latent form of matrix metalloproteinase-2 (MMP-2) detected by gelatin zymography (ng/mg protein) decreased from months 0 to 2 and increased from months 4 to 8, whereas the activated form decreased from months 0 to 2, remained low until month 6 and then recovered on month 8 (p < 0.0001). Data suggest that the relative cervical weight biphasic pattern during the development is related to MMP-2-dependent changes in the collagen content.

Identifiants

pubmed: 30907032
doi: 10.1111/ahe.12441
doi:

Substances chimiques

Glycosaminoglycans 0
Collagen 9007-34-5
Matrix Metalloproteinase 2 EC 3.4.24.24
Matrix Metalloproteinase 9 EC 3.4.24.35

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

306-314

Subventions

Organisme : Comisión Sectorial de Investigación Científica
Organisme : Universidad de la República
Organisme : Agencia Nacional de Investigación e Innovación

Informations de copyright

© 2019 Blackwell Verlag GmbH.

Auteurs

Marcelo Rodríguez-Piñón (M)

Biochemistry, Department of Molecular and Cellular Biology, Universidad de la República, Montevideo, Uruguay.

Daniela Casuriaga (D)

Biochemistry, Department of Molecular and Cellular Biology, Universidad de la República, Montevideo, Uruguay.

Patricia Genovese (P)

Histology and Embryology, Department of Morphology and Development, Veterinary Faculty, Universidad de la República, Montevideo, Uruguay.

Gonzalo García-Barcelo (G)

Biochemistry, Department of Molecular and Cellular Biology, Universidad de la República, Montevideo, Uruguay.

Fernanda Alcaide (F)

Histology and Embryology, Department of Morphology and Development, Veterinary Faculty, Universidad de la República, Montevideo, Uruguay.

Alejandro Bielli (A)

Histology and Embryology, Department of Morphology and Development, Veterinary Faculty, Universidad de la República, Montevideo, Uruguay.

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Classifications MeSH