Proteomic analysis of human aqueous humor using multidimensional protein identification technology.

Matthew R. Richardson, Marianne O. Price, Francis W. Price, Jennifer C. Pardo, Juan C. Grandin, Jinsam You, Mu Wang, Mervin Yoder

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

Aqueous humor (AH) supports avascular tissues in the anterior segment of the eye, maintains intraocular pressure, and potentially influences the pathogenesis of ocular diseases. Nevertheless, the AH proteome is still poorly defined despite several previous efforts, which were hindered by interfering high abundance proteins, inadequate animal models, and limited proteomic technologies. To facilitate future investigations into AH function, the AH proteome was extensively characterized using an advanced proteomic approach. Samples from patients undergoing cataract surgery were pooled and depleted of interfering abundant proteins and thereby divided into two fractions: albumin-bound and albumin-depleted. Multidimensional Protein Identification Technology (MudPIT) was utilized for each fraction; this incorporates strong cation exchange chromatography to reduce sample complexity before reversed-phase liquid chromatography and tandem mass spectrometric analysis. Twelve proteins had multi-peptide, high confidence identifications in the albumin-bound fraction and 50 proteins had multi-peptide, high confidence identifications in the albumin-depleted fraction. Gene ontological analyses were performed to determine which cellular components and functions were enriched. Many proteins were previously identified in the AH and for several their potential role in the AH has been investigated; however, the majority of identified proteins were novel and only speculative roles can be suggested. The AH was abundant in anti-oxidant and immunoregulatory proteins as well as anti-angiogenic proteins, which may be involved in maintaining the avascular tissues. This is the first known report to extensively characterize and describe the human AH proteome and lays the foundation for future work regarding its function in homeostatic and pathologic states.

Original languageEnglish
Pages (from-to)2740-2750
Number of pages11
JournalMolecular Vision
Volume15
StatePublished - 2009

Fingerprint

Aqueous Humor
Proteomics
Technology
Albumins
Proteins
Proteome
Angiogenic Proteins
Anterior Eye Segment
Peptides
Eye Diseases
Reverse-Phase Chromatography
Intraocular Pressure
Oxidants
Cataract
Cations
Chromatography
Animal Models

ASJC Scopus subject areas

  • Ophthalmology

Cite this

Richardson, M. R., Price, M. O., Price, F. W., Pardo, J. C., Grandin, J. C., You, J., ... Yoder, M. (2009). Proteomic analysis of human aqueous humor using multidimensional protein identification technology. Molecular Vision, 15, 2740-2750.

Proteomic analysis of human aqueous humor using multidimensional protein identification technology. / Richardson, Matthew R.; Price, Marianne O.; Price, Francis W.; Pardo, Jennifer C.; Grandin, Juan C.; You, Jinsam; Wang, Mu; Yoder, Mervin.

In: Molecular Vision, Vol. 15, 2009, p. 2740-2750.

Research output: Contribution to journalArticle

Richardson, MR, Price, MO, Price, FW, Pardo, JC, Grandin, JC, You, J, Wang, M & Yoder, M 2009, 'Proteomic analysis of human aqueous humor using multidimensional protein identification technology.', Molecular Vision, vol. 15, pp. 2740-2750.
Richardson MR, Price MO, Price FW, Pardo JC, Grandin JC, You J et al. Proteomic analysis of human aqueous humor using multidimensional protein identification technology. Molecular Vision. 2009;15:2740-2750.
Richardson, Matthew R. ; Price, Marianne O. ; Price, Francis W. ; Pardo, Jennifer C. ; Grandin, Juan C. ; You, Jinsam ; Wang, Mu ; Yoder, Mervin. / Proteomic analysis of human aqueous humor using multidimensional protein identification technology. In: Molecular Vision. 2009 ; Vol. 15. pp. 2740-2750.
@article{188d7658307d4fe48d0534b3c7d8921b,
title = "Proteomic analysis of human aqueous humor using multidimensional protein identification technology.",
abstract = "Aqueous humor (AH) supports avascular tissues in the anterior segment of the eye, maintains intraocular pressure, and potentially influences the pathogenesis of ocular diseases. Nevertheless, the AH proteome is still poorly defined despite several previous efforts, which were hindered by interfering high abundance proteins, inadequate animal models, and limited proteomic technologies. To facilitate future investigations into AH function, the AH proteome was extensively characterized using an advanced proteomic approach. Samples from patients undergoing cataract surgery were pooled and depleted of interfering abundant proteins and thereby divided into two fractions: albumin-bound and albumin-depleted. Multidimensional Protein Identification Technology (MudPIT) was utilized for each fraction; this incorporates strong cation exchange chromatography to reduce sample complexity before reversed-phase liquid chromatography and tandem mass spectrometric analysis. Twelve proteins had multi-peptide, high confidence identifications in the albumin-bound fraction and 50 proteins had multi-peptide, high confidence identifications in the albumin-depleted fraction. Gene ontological analyses were performed to determine which cellular components and functions were enriched. Many proteins were previously identified in the AH and for several their potential role in the AH has been investigated; however, the majority of identified proteins were novel and only speculative roles can be suggested. The AH was abundant in anti-oxidant and immunoregulatory proteins as well as anti-angiogenic proteins, which may be involved in maintaining the avascular tissues. This is the first known report to extensively characterize and describe the human AH proteome and lays the foundation for future work regarding its function in homeostatic and pathologic states.",
author = "Richardson, {Matthew R.} and Price, {Marianne O.} and Price, {Francis W.} and Pardo, {Jennifer C.} and Grandin, {Juan C.} and Jinsam You and Mu Wang and Mervin Yoder",
year = "2009",
language = "English",
volume = "15",
pages = "2740--2750",
journal = "Molecular Vision",
issn = "1090-0535",

}

TY - JOUR

T1 - Proteomic analysis of human aqueous humor using multidimensional protein identification technology.

AU - Richardson, Matthew R.

AU - Price, Marianne O.

AU - Price, Francis W.

AU - Pardo, Jennifer C.

AU - Grandin, Juan C.

AU - You, Jinsam

AU - Wang, Mu

AU - Yoder, Mervin

PY - 2009

Y1 - 2009

N2 - Aqueous humor (AH) supports avascular tissues in the anterior segment of the eye, maintains intraocular pressure, and potentially influences the pathogenesis of ocular diseases. Nevertheless, the AH proteome is still poorly defined despite several previous efforts, which were hindered by interfering high abundance proteins, inadequate animal models, and limited proteomic technologies. To facilitate future investigations into AH function, the AH proteome was extensively characterized using an advanced proteomic approach. Samples from patients undergoing cataract surgery were pooled and depleted of interfering abundant proteins and thereby divided into two fractions: albumin-bound and albumin-depleted. Multidimensional Protein Identification Technology (MudPIT) was utilized for each fraction; this incorporates strong cation exchange chromatography to reduce sample complexity before reversed-phase liquid chromatography and tandem mass spectrometric analysis. Twelve proteins had multi-peptide, high confidence identifications in the albumin-bound fraction and 50 proteins had multi-peptide, high confidence identifications in the albumin-depleted fraction. Gene ontological analyses were performed to determine which cellular components and functions were enriched. Many proteins were previously identified in the AH and for several their potential role in the AH has been investigated; however, the majority of identified proteins were novel and only speculative roles can be suggested. The AH was abundant in anti-oxidant and immunoregulatory proteins as well as anti-angiogenic proteins, which may be involved in maintaining the avascular tissues. This is the first known report to extensively characterize and describe the human AH proteome and lays the foundation for future work regarding its function in homeostatic and pathologic states.

AB - Aqueous humor (AH) supports avascular tissues in the anterior segment of the eye, maintains intraocular pressure, and potentially influences the pathogenesis of ocular diseases. Nevertheless, the AH proteome is still poorly defined despite several previous efforts, which were hindered by interfering high abundance proteins, inadequate animal models, and limited proteomic technologies. To facilitate future investigations into AH function, the AH proteome was extensively characterized using an advanced proteomic approach. Samples from patients undergoing cataract surgery were pooled and depleted of interfering abundant proteins and thereby divided into two fractions: albumin-bound and albumin-depleted. Multidimensional Protein Identification Technology (MudPIT) was utilized for each fraction; this incorporates strong cation exchange chromatography to reduce sample complexity before reversed-phase liquid chromatography and tandem mass spectrometric analysis. Twelve proteins had multi-peptide, high confidence identifications in the albumin-bound fraction and 50 proteins had multi-peptide, high confidence identifications in the albumin-depleted fraction. Gene ontological analyses were performed to determine which cellular components and functions were enriched. Many proteins were previously identified in the AH and for several their potential role in the AH has been investigated; however, the majority of identified proteins were novel and only speculative roles can be suggested. The AH was abundant in anti-oxidant and immunoregulatory proteins as well as anti-angiogenic proteins, which may be involved in maintaining the avascular tissues. This is the first known report to extensively characterize and describe the human AH proteome and lays the foundation for future work regarding its function in homeostatic and pathologic states.

UR - http://www.scopus.com/inward/record.url?scp=77649242514&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77649242514&partnerID=8YFLogxK

M3 - Article

C2 - 20019884

AN - SCOPUS:77649242514

VL - 15

SP - 2740

EP - 2750

JO - Molecular Vision

JF - Molecular Vision

SN - 1090-0535

ER -