Latent TGFβ binding protein-1 and fibrillin-1 in human capsular opacification and in cultured lens epithelial cells
- aDepartment of Ophthalmology, Wakayama Medical University School of Medicine, Wakayama, Japan, bDepartment of Pathology
- Shizuya Saika, MD, Department of Ophthalmology, Wakayama Medical University School of Medicine, 811-1 Kimiidera, Wakayama, 641-8509, Japanshizuya{at}wakayama-med.ac.jp
- Accepted 10 May 2001
Abstract
BACKGROUND/AIM It was previously reported that collagenous extracellular matrix (ECM) in human capsular opacification contained isoforms of transforming growth factor β (TGFβ). In the present study, the authors performed immunohistochemistry to examine whether ECM in human capsular opacification and in cultures of bovine lens epithelial cells (LECs) contained latent TGFβ binding protein-1 (LTBP-1), TGFβ1 latency associated peptide (β1-LAP), and fibrillin-1, a suspected ligand of LTBP-1 as well as a component of the extracellular microfibrillar apparatus. The aim of the study was to further clarify the mechanism of TGFβ1 deposition in ECM of capsular opacification.
METHODS Human capsular opacification specimens and uninjured lens capsules, as well as cultured bovine LECs, were processed for immunohistochemistry using antibodies against LTBP-1, β1-LAP, fibrillin-1, and collagen type I.
RESULTS LTBP-1, β1-LAP, and fibrillin-1 all were localised to the ECM in human capsular opacification. Uninjured lens epithelium stained for β1-LAP, but not for LTBP-1 and fibrillin-1. ECM deposited in confluent LEC cultures stained for LTBP-1, β1-LAP, and fibrillin-1, while cultures with only sparse cellularity were unstained for LTBP-1 or fibrillin-1.
CONCLUSIONS LECs upregulate LTBP-1 and fibrillin-1 during postoperative healing. LTBP-1, β1-LAP, and fibrillin-1 colocalised to the ECM in capsular opacification and in confluent LEC cultures. TGFβ1 is considered to deposit in ECM in the large latent form. ECM secreted by LEC may function as a scavenger or repository of TGFβ.
