Ultrastructural and immunohistochemical analysis of proteoglycans in mouse pubic symphysis
Version of Record online: 2 JAN 2013
© The Author(s) Journal compilation © 2003 International Federation for Cell Biology
Cell Biology International
Volume 27, Issue 8, pages 647–655, August 2003
How to Cite
Pinheiro, M. C., Joazeiro, P. P., Mora, O. A. and Toledo, O. M.S. (2003), Ultrastructural and immunohistochemical analysis of proteoglycans in mouse pubic symphysis. Cell Biology International, 27: 647–655. doi: 10.1016/S1065-6995(03)00121-5
- Issue online: 2 JAN 2013
- Version of Record online: 2 JAN 2013
- Received 26 March 2002, revised 18 February 2003, accepted 22 April 2003
- Cuprolinic blue;
- Pubic symphysis;
Proteoglycans were accurately localized in mouse pubic symphyseal tissues using the cuprolinic blue method. Specific glycosaminoglycans degradative enzymes, together with chondroitin sulfate and decorin antibodies, allowed the identification of glycosaminoglycans.
Chondroitin sulfate proteoglycans were the main proteoglycans observed in hyaline cartilage, fibrocartilage, and dense connective tissue. Ultrastructurally, they were seen as electron-dense granules and filaments. The granules, rich in chondroitin sulfate chains, were exclusively found in hyaline cartilage, whereas filaments were present in cartilage, fibrocartilage, and dense connective tissue. The latter were classified by size and susceptibility to enzyme digestion into F1, F2 and F3 filaments: F1 filaments were small, thin, and collagen fibril-associated; F2 filaments were thick, heavily stained, and localized around individual collagen fibrils and between bundles of collagen fibrils; and F3 filaments were scattered throughout elastic fiber surfaces. Considering their localization, susceptibility to chondroitinase AC and immunohistochemical detection, the symphysial F1 filaments were found to be preferentially decorin substituted with chondroitin sulfate side chains. The F2 filaments were also susceptible to chondroitinase AC treatment, whereas F3 filaments could be digested by heparitinase.
The data thus obtained on the localization and identification of pubic symphyseal proteoglycans in virgin mice may be useful in the study of structural modifications that occur throughout pregnancy.