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Characterizing the normal proteome of human ciliary body.

Goel R, Murthy KR, Srikanth SM, Pinto SM, Bhattacharjee M, Kelkar DS, Madugundu AK, Dey G, Mohan SS, Krishna V, Prasad TsK, Chakravarti S, Harsha H, Pandey A - Clin Proteomics (2013)

Bottom Line: 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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Johns Hopkins University School of Medicine, Baltimore 21205, MD, USA. pandey@jhmi.edu.

ABSTRACT

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.

No MeSH data available.


Related in: MedlinePlus

MS/MS spectra of novel proteins identified. A. shows the MS/MS spectra of peptide, EEAENNLAAFR, from Desmin B. The peptide, GAEILEVLHSLPAVR, derived from 26S proteasome non-ATPase regulatory subunit 6 C. NVDILKDPETVK Peptide from exportin-1 D. SEDPDQQYLILNTAR Peptide from vacuolar sorting-associated protein 35.
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Figure 3: MS/MS spectra of novel proteins identified. A. shows the MS/MS spectra of peptide, EEAENNLAAFR, from Desmin B. The peptide, GAEILEVLHSLPAVR, derived from 26S proteasome non-ATPase regulatory subunit 6 C. NVDILKDPETVK Peptide from exportin-1 D. SEDPDQQYLILNTAR Peptide from vacuolar sorting-associated protein 35.

Mentions: The majority of identified proteins were not previously reported in the ciliary body proteome. A partial list of these proteins is provided in Table 2. Representative MS/MS spectra of four proteins identified in this study - desmin, 26S proteasome non-ATPase regulatory subunit 6, exportin 1 and vacuolar protein sorting-associated protein 35 are shown in Figure 3 and described in the subsequent sections.


Characterizing the normal proteome of human ciliary body.

Goel R, Murthy KR, Srikanth SM, Pinto SM, Bhattacharjee M, Kelkar DS, Madugundu AK, Dey G, Mohan SS, Krishna V, Prasad TsK, Chakravarti S, Harsha H, Pandey A - Clin Proteomics (2013)

MS/MS spectra of novel proteins identified. A. shows the MS/MS spectra of peptide, EEAENNLAAFR, from Desmin B. The peptide, GAEILEVLHSLPAVR, derived from 26S proteasome non-ATPase regulatory subunit 6 C. NVDILKDPETVK Peptide from exportin-1 D. SEDPDQQYLILNTAR Peptide from vacuolar sorting-associated protein 35.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3750387&req=5

Figure 3: MS/MS spectra of novel proteins identified. A. shows the MS/MS spectra of peptide, EEAENNLAAFR, from Desmin B. The peptide, GAEILEVLHSLPAVR, derived from 26S proteasome non-ATPase regulatory subunit 6 C. NVDILKDPETVK Peptide from exportin-1 D. SEDPDQQYLILNTAR Peptide from vacuolar sorting-associated protein 35.
Mentions: The majority of identified proteins were not previously reported in the ciliary body proteome. A partial list of these proteins is provided in Table 2. Representative MS/MS spectra of four proteins identified in this study - desmin, 26S proteasome non-ATPase regulatory subunit 6, exportin 1 and vacuolar protein sorting-associated protein 35 are shown in Figure 3 and described in the subsequent sections.

Bottom Line: 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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Johns Hopkins University School of Medicine, Baltimore 21205, MD, USA. pandey@jhmi.edu.

ABSTRACT

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.

No MeSH data available.


Related in: MedlinePlus