Skip to Content
Merck
  • Collagen, glycosaminoglycans and matrix metalloproteinase-2 and metalloproteinase-9 in the cervix of the ewe during prepubertal development.

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

Anatomia, histologia, embryologia (2019-03-25)
Marcelo Rodríguez-Piñón, Daniela Casuriaga, Patricia Genovese, Gonzalo García-Barcelo, Fernanda Alcaide, Alejandro Bielli
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Matrix Metalloproteinase-9 human, recombinant, >90% (SDS-PAGE), buffered aqueous solution
Sigma-Aldrich
Matrix Metalloproteinase-2 from mouse, recombinant, expressed in NSO cells, >95% (SDS-PAGE), buffered aqueous glycerol solution
Sigma-Aldrich
Gelatin from bovine skin, Type B, powder, BioReagent, suitable for cell culture