HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ueda, J. Articles by Yue, B. Y. J. T. Search for Related Content PubMed PubMed Citation Articles by Ueda, J. Articles by Yue, B. Y. J. T.

Distribution of Myocilin and Extracellular Matrix Components in the Corneoscleral Meshwork of Human Eyes

From the Department of Ophthalmology and Visual Sciences, University of Illinois at Chicago College of Medicine, Chicago, Illinois.

PURPOSE. To examine ultrastructurally the composition of major extracellular matrix (ECM) components and the distribution of myocilin in the trabecular lamellae of corneoscleral (CS) meshwork in normal human eyes. The codistribution of myocilin with ECM components was also investigated.

METHODS. Postembedding immunoelectron microscopic studies were performed with antibodies against myocilin and other ECM components, including fibronectin, laminin, vitronectin, tenascin, elastin, fibrillin-1, microfibril-associated glycoprotein (MAGP)-1, decorin, versican, hyaluronic acid, and five types of collagen (I, III, IV, V, and VI). Double labeling of myocilin with other ECM components was performed with different sized gold particles.

RESULTS. In the trabecular beams of CS meshwork, fibronectin, laminin, and collagen type IV were associated with basement membranes, whereas elastin was specifically localized to the core of elastic-like fibers. Several types of collagens, glycoproteins, proteoglycans, and hyaluronic acid were detected both in the collagen fibers and ground substances. Myocilin predominantly localized in the long-spacing collagens and sheath materials surrounding elastic-like fibers, codistributed with fibronectin, fibrillin-1, MAGP-1, decorin, and type VI collagen.

CONCLUSIONS. This study illustrated the composition of ECM materials in the trabecular lamellae of CS meshwork. Myocilin was specifically localized to long-spacing collagens and the surrounding sheath of elastic-like fibers interacting with microfibril-associated elements where changes have been documented to occur in glaucomatous and aging eyes.

This article has been cited by other articles:

				A. Ohno-Jinno, Z. Isogai, M. Yoneda, K. Kasai, O. Miyaishi, Y. Inoue, T. Kataoka, J.-S. Zhao, H. Li, M. Takeyama, et al. Versican and Fibrillin-1 Form a Major Hyaluronan-Binding Complex in the Ciliary Body Invest. Ophthalmol. Vis. Sci., July 1, 2008; 49(7): 2870 - 2877. [Abstract] [Full Text] [PDF]

				K. Sanka, R. Maddala, D. L. Epstein, and P. V. Rao Influence of Actin Cytoskeletal Integrity on Matrix Metalloproteinase-2 Activation in Cultured Human Trabecular Meshwork Cells Invest. Ophthalmol. Vis. Sci., May 1, 2007; 48(5): 2105 - 2114. [Abstract] [Full Text] [PDF]

				D. B. Gould, M. Reedy, L. A. Wilson, R. S. Smith, R. L. Johnson, and S. W. M. John Mutant Myocilin Nonsecretion In Vivo Is Not Sufficient To Cause Glaucoma Mol. Cell. Biol., November 15, 2006; 26(22): 8427 - 8436. [Abstract] [Full Text] [PDF]