Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Collagen fibril organization in the pregnant endometrium of decorin-deficient mice

Full text
Author(s):
Sanches, Juliane C. T. [1] ; Jones, Carolyn J. P. [2] ; Aplin, John D. [2] ; Iozzo, Renato V. [3] ; Zorn, Telma M. T. [1] ; Oliveira, Sergio F. [1]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Dept Cell & Dev Biol, Inst Biomed Sci, BR-05508900 Sao Paulo - Brazil
[2] Univ Manchester, St Marys Hosp, Maternal & Fetal Hlth Res Grp, Manchester M13 0JH, Lancs - England
[3] Thomas Jefferson Univ, Dept Pathol Anat & Cell Biol, Philadelphia, PA 19107 - USA
Total Affiliations: 3
Document type: Journal article
Source: Journal of Anatomy; v. 216, n. 1, p. 144-155, JAN 2010.
Web of Science Citations: 18
Abstract

In the pregnant mouse endometrium, collagen fibrillogenesis is characterized by the presence of very thick collagen fibrils which are topographically located exclusively within the decidualized stroma. This dynamic biological process is in part regulated by the small leucine-rich proteoglycans decorin and biglycan. In the present study we utilized wild-type (Dcn+/+) and decorin-deficient (Dcn-/-) time-pregnant mice to investigate the evolution of non-decidualized and decidualized collagen matrix in the uterine wall of these animals. Ultrastructural and morphometric analyses revealed that the organization of collagen fibrils in the pregnant endometrium of both non-decidualized and decidualized stroma showed a great variability of shape and size, regardless of the genotype. However, the decidualized endometrium from Dcn-/- mice contained fibrils with larger diameter and more irregular contours as compared to the wild-type littermates. In the Dcn-/- animals, the proportion of thin (10-50 nm) fibrils was also higher as compared to Dcn+/+ animals. On day 7 of pregnancy, biglycan was similarly localized in the decidualized endometrium in both genotypes. Lumican immunostaining was intense both in decidualized and non-decidualized stroma from Dcn-/- animals. The present results support previous findings suggesting that decorin participates in uterine collagen fibrillogenesis. In addition, we suggest that the absence of decorin disturbs the process of lateral assembly of thin fibrils, resulting in very thick collagen fibrils with irregular profiles. Our data further suggest that decorin, biglycan and lumican might play an interactive role in collagen fibrillogenesis in the mouse endometrium, a process modulated according to the stage of pregnancy. (AU)