Phosphorylation of alphaB-crystallin in epiretinal membrane of human proliferative diabetic retinopathy

• 作者: Atsuhiro Kanda Erdal Tan Ishizuka Junichi Fukuhara Kousuke Noda Miyuki Murata Ryo Ando Saori Inafuku Satoru Kase Satoshi Kinoshita Susumu Ishida Wataru Saito Yoko Dong Yoshiaki Tagawa Zhenyu Dong
• 来源期刊: 国际眼科杂志：英文版
• 学科: 医学
• 关键词: phosphorylated alpha B-CRYSTALLIN vascular endothelial growth factor NEOVASCULARIZATION PROLIFERATIVE diabetic RETINOPATHY
• 年，卷（期）: 2016,（8）
• 页码范围: 1100-1105
• 页数: 0页
• 分类号: R587.2

摘要

AIM: To examine phosphorylation of alpha B-crystallin(p-αBC), a vascular endothelial growth factor(VEGF)chaperone, and immunohistochemically investigate relationship between p-αBC, VEGF and phosphorylated p38-mitogen-activated protein kinase(p-p38 MAPK) in the epiretinal membrane of human proliferative diabetic retinopathy(PDR).METHODS: Eleven epiretinal membranes of PDR surgically excised were included in this study. Two normal retinas were also collected from enucleation tissues due to choroidal melanoma. Paraformaldehyde-fixed, paraffin-embedded tissue sections were processed for immunohistochemistry with anti-p-αBC, VEGF, CD31,and p-p38 MAPK antibodies.RESULTS: Immunoreactivity for p-αBC was observed in all of the epiretinal membranes examined, where phosphorylation on serine(Ser) 59 showed strongest immunoreactivity in over 70% of the membranes. The immunolocalization of p-αBC was detected in the CD31-positive endothelial cells, and co-localized with VEGF and p-p38 MAPK in PDR membranes. Immunoreactivity for p-αBC, however, was undetectable in endothelial cells of the normal retinas, where p-p38 MAPK immunoreactivity was less marked than PDR membranes.CONCLUSION: Phosphorylation of αBC, in particular,phosphorylation on Ser59 by p-p38 MAPK may play a potential role as a molecular chaperon for VEGF in the pathogenesis of epiretinal membranes in PDR.