Affordable Access

In situ ultrastructural characterization of chondroitin sulfate proteoglycans in normal rabbit aorta.

Authors
  • Galis, Z S
  • Alavi, M Z
  • Moore, S
Type
Published Article
Journal
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
Publication Date
Feb 01, 1992
Volume
40
Issue
2
Pages
251–263
Identifiers
PMID: 1552168
Source
Medline
License
Unknown

Abstract

We used a monoclonal antibody recognizing chondroitin sulfate (CS) to investigate by immunocytochemistry the characteristics displayed in situ by aortic proteoglycans (PG) containing CS side chains. The antibody specifically precipitated metabolically labeled PG from aortic extracts. Anti-CS specificity was also tested directly on tissue sections and was confirmed by the virtual abolition of immunolabeling on those previously digested with CS-specific enzymes. The overall CS-PG distribution assessed by light microscopy after embedding in Lowicryl KM4 by silver-enhanced immunogold recapitulated that obtained on frozen sections with immunoperoxidase. Extracellular concentrations of CS-PG were very high in the innermost regions of aorta and decreased in the media. The reaction was weak and diffuse in the adventitia. By electron microscopy, the detailed labeling of CS-PG discriminated patterns of organization at both the regional and the molecular level and enabled morphometric estimations. In relation to other components of the extracellular matrix, we found that CS-PG and elastin mutually excluded each other, while two types of CS-PG were differently associated with collagen within media or adventitia. The use of high-resolution immunodetection for the in situ characterization of aortic CS-PG could add specific information relevant to many biological processes in which these molecules have been implicated.

Report this publication

Statistics

Seen <100 times