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Kaili Wu, Qian Yang, Xiuping Liu, Liping Lin, Feng Zou; High level of carbonic anhydrase 1 in pterygium. Invest. Ophthalmol. Vis. Sci. 2015;56(7 ):3035.
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© ARVO (1962-2015); The Authors (2016-present)
Carbonic anhydrase 1 (CA1)catalyze the reversible hydration of carbon dioxide and participate in a variety of biological processes.The aim of this study was to determine the level of CA1 in pterygial tissue, using normal human conjunctival samples as a control.
Water soluable proteins of pterygium and normal human conjunctiva were extracted and underwent SDS-polyacrimide gel electrophoresis (SDS-PAGE). Intensive bands of pterygial proteins were identified by MALDI-TOF-MS/MS. CA1, one of identied proteins, was examined by Westernblot and immunohistochemical staining, using normal human conjunctival samples as the control.
On SDS-PAGE gel, several bands of pterygial extracts were more intensive than that of normal conjunctiva. One band was identified as CA1 by MALDI-TOF-MS/MS. Western blot analysis reveraled that CA1 level increased in pterygial tissue when compared with normal conjuctiva. Immunohistochemical staining revealed that CA1 was more intensively stained in pterygial tissue than that observed in normal conjunctival tissue. In pterygial tissue that was characterized with neovascularization and congestion, intensive staining appeared in red blood cells, vascular wall cells and fibroblast cells as well as in some epithelial cells. While none neovascularization and epithelial staining was found in normal conjunctiva.
A high level of CA1 existed in pterygial tissue, which was mainly resulted from the neovascularization and congestion of pterygium.
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