TY - JOUR
T1 - Characterizing the normal proteome of human ciliary body
AU - Goel, Renu
AU - Murthy, Krishna R.
AU - Srikanth, Srinivas M.
AU - Pinto, Sneha M.
AU - Bhattacharjee, Mitali
AU - Kelkar, Dhanashree S.
AU - Madugundu, Anil K.
AU - Dey, Gourav
AU - Mohan, Sujatha S.
AU - Krishna, Venkatarangaiah
AU - Prasad, T. S.Keshava
AU - Chakravarti, Shukti
AU - Harsha, H. C.
AU - Pandey, Akhilesh
N1 - Funding Information:
We thank the Department of Biotechnology (DBT) of the Government of India for research support to the Institute of Bioinformatics. Srinivas M. Srikanth and Gourev Dey are recipients of Junior Research Fellowship from University Grants Commission (UGC), India. Sneha M. Pinto is a recipient of Senior Research Fellowship from Council of Scientific and Industrial Research (CSIR), Government of India. Anil K. Madugundu is the recipient of BINC-Junior Research Fellowship from Department of Biotechnology (DBT), India. Harsha Gowda is a Wellcome Trust/DBT India Alliance Early Career Fellow. Dr. T. S. Keshava Prasad is the recipient of a research grant on “Development of Infrastructure and a Computational Framework for Analysis of Proteomic Data” from DBT. Akhilesh Pandey was partially funded for this project by a grant from National Institutes of Health Roadmap initiative U54 RR020839.
PY - 2013
Y1 - 2013
N2 - Background: The ciliary body is the circumferential muscular tissue located just behind the iris in the anterior chamber of the eye. It plays a pivotal role in the production of aqueous humor, maintenance of the lens zonules and accommodation by changing the shape of the crystalline lens. The ciliary body is the major target of drugs against glaucoma as its inhibition leads to a drop in intraocular pressure. A molecular study of the ciliary body could provide a better understanding about the pathophysiological processes that occur in glaucoma. Thus far, no large-scale proteomic investigation has been reported for the human ciliary body. Results: In this study, we have carried out an in-depth LC-MS/MS-based proteomic analysis of normal human ciliary body and have identified 2,815 proteins. We identified a number of proteins that were previously not described in the ciliary body including importin 5 (IPO5), atlastin-2 (ATL2), B-cell receptor associated protein 29 (BCAP29), basigin (BSG), calpain-1 (CAPN1), copine 6 (CPNE6), fibulin 1 (FBLN1) and galectin 1 (LGALS1). We compared the plasma proteome with the ciliary body proteome and found that the large majority of proteins in the ciliary body were also detectable in the plasma while 896 proteins were unique to the ciliary body. We also classified proteins using pathway enrichment analysis and found most of proteins associated with ubiquitin pathway, EIF2 signaling, glycolysis and gluconeogenesis. Conclusions: More than 95% of the identified proteins have not been previously described in the ciliary body proteome. This is the largest catalogue of proteins reported thus far in the ciliary body that should provide new insights into our understanding of the factors involved in maintaining the secretion of aqueous humor. The identification of these proteins will aid in understanding various eye diseases of the anterior segment such as glaucoma and presbyopia.
AB - Background: The ciliary body is the circumferential muscular tissue located just behind the iris in the anterior chamber of the eye. It plays a pivotal role in the production of aqueous humor, maintenance of the lens zonules and accommodation by changing the shape of the crystalline lens. The ciliary body is the major target of drugs against glaucoma as its inhibition leads to a drop in intraocular pressure. A molecular study of the ciliary body could provide a better understanding about the pathophysiological processes that occur in glaucoma. Thus far, no large-scale proteomic investigation has been reported for the human ciliary body. Results: In this study, we have carried out an in-depth LC-MS/MS-based proteomic analysis of normal human ciliary body and have identified 2,815 proteins. We identified a number of proteins that were previously not described in the ciliary body including importin 5 (IPO5), atlastin-2 (ATL2), B-cell receptor associated protein 29 (BCAP29), basigin (BSG), calpain-1 (CAPN1), copine 6 (CPNE6), fibulin 1 (FBLN1) and galectin 1 (LGALS1). We compared the plasma proteome with the ciliary body proteome and found that the large majority of proteins in the ciliary body were also detectable in the plasma while 896 proteins were unique to the ciliary body. We also classified proteins using pathway enrichment analysis and found most of proteins associated with ubiquitin pathway, EIF2 signaling, glycolysis and gluconeogenesis. Conclusions: More than 95% of the identified proteins have not been previously described in the ciliary body proteome. This is the largest catalogue of proteins reported thus far in the ciliary body that should provide new insights into our understanding of the factors involved in maintaining the secretion of aqueous humor. The identification of these proteins will aid in understanding various eye diseases of the anterior segment such as glaucoma and presbyopia.
KW - Aqueous humor
KW - Ciliary processes
KW - Cyclitis and glaucoma
KW - Non-pigmented epithelial layer
KW - Pigmented epithelial layer
KW - Protein biomarkers
KW - Proteome discoverer
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U2 - 10.1186/1559-0275-10-9
DO - 10.1186/1559-0275-10-9
M3 - Article
AN - SCOPUS:84898428766
SN - 1542-6416
VL - 10
JO - Clinical Proteomics
JF - Clinical Proteomics
IS - 1
M1 - 9
ER -