IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fitch, J. M.
Right arrow Articles by Linsenmayer, T. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fitch, J. M.
Right arrow Articles by Linsenmayer, T. F.

Investigative Ophthalmology & Visual Science, Vol 29, 1125-1136, Copyright © 1988 by Association for Research in Vision and Ophthalmology

ARTICLES AND REPORTS

Corneal collagen fibrils: dissection with specific collagenases and monoclonal antibodies

JM Fitch, DE Birk, A Mentzer, KA Hasty, C Mainardi and TF Linsenmayer
Department of Anatomy and Cellular Biology, Tufts University School of Medicine, Boston, Massachusetts 02111.

To investigate the relationship of collagen types I and V within corneal fibrils, and the collagenolytic mechanisms potentially involved in corneal development and remodeling, we have incubated cryostat sections of avian corneas with collagenases that specifically degrade collagen types I or V to digest selectively the collagen in situ. These preparations were then analyzed by immunofluorescence histochemistry and immunoelectron microscopy using anti-collagen type-specific monoclonal antibodies. Digestion of corneal sections with the type I- specific collagenase ("I'ase") exposed antigenically masked type V collagen, indicating that epitopes on type V collagen in heterotypic fibrils are inaccessible to the antibody due to their interaction with type I collagen. Sections digested with the type V collagen-degrading enzyme ("V'ase") showed no removal of type V collagen. However, after the fibrillar structure was disrupted by acetic acid treatment before enzyme digestion, the type V collagen was then degraded. Likewise, prior digestion of type I collagen by I'ase also rendered type V collagen susceptible to digestion by V'ase. These results suggest that the cleavage sites on type V collagen also are buried within heterotypic fibrils and therefore inaccessible to the enzyme. They also document, for the first time, V'ase activity against type V collagen in situ. Electron microscopic observations of sections partially digested with the I'ase revealed many short striated fibrillar segments from which smaller filaments protrude. Both the striated regions and some of the filaments were labeled by an antibody against type I collagen; anti- type V antibody reacted preferentially with the thin filaments. Thus avian corneal fibrils contain type I collagen, in which filaments of type V collagen are embedded. Complete removal of the fibrillar stromal matrix in the course of normal or pathological remodeling requires at least two different collagenases acting in concert.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. Koch, J. E. Foley, R. Hahn, P. Zhou, R. E. Burgeson, D. R. Gerecke, and M. K. Gordon
alpha 1(XX) Collagen, a New Member of the Collagen Subfamily, Fibril-associated Collagens with Interrupted Triple Helices
J. Biol. Chem., June 15, 2001; 276(25): 23120 - 23126.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1988 by the Association for Research in Vision and Ophthalmology