AH from 120 to 500 ng/?L. The proteins

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Last updated: August 23, 2019

AH is a complex mixture of electrolytes,organic solutes, growth factors, cytokines, and proteins that provide themetabolic requirements to the avascular tissues of the anterior segment. (i,ii,iii)The protein component of AH is minimal ranging from120 to 500 ng/?L. The proteins in AH arise from plasma as the result offiltration through fenestrated capillaries of the ciliary body stroma via theiris root. Although AH is a diffusate of plasma, but it has qualitative andquantitative differences in protein content in compared plasma. Identifying theprotein component of tissues or fluids is vital to understanding the role theseproteins have in normal physiology. AH proteins that are secreted from theanterior segment tissues may have a significant role in the pathogenesis ofvarious eye diseases.

(iv,v,vi,vii,viii)Characterization of the hAH proteome willprovide new insights into the factors involved in maintaining anterior segmenthomeostasis and will also establish a foundation for biomarker discovery invarious eye diseases of the anterior segment, such as glaucoma and cornealdystrophies. The Human Proteome Organization (HUPO) plasma proteome projectdatabase provided in the public domain by the University of Michigan MedicalSchool contains more than 3000 proteins and protein isoforms. (ix)However, literature searches identified less than 150 proteins in hAH. Many ofthese proteins were identified as individual proteins based on targetedmolecules of interest by Western blot analysis or enzyme-linked immunosorbentassay (ELISA). These were identified using proteomic approaches such asdifferential protein expression, Multidimensional Protein IdentificationTechnology (MudPIT) (x).Other studies using one- and two-dimensional gel electrophoresis coupled withmass spectrometry have relied mostly on comparative studies & differentialprotein expression (xi,xii,xiii).However, these studies have confirmed only a few proteins across studies.

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Therefore, it is reasonable to suggest that little is known about the proteincomposition of hAH.Matrix-assistedlaser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS)is apowerful analytical tool to study peptides, proteins, and most otherbiomolecules (oligonucleotides, carbohydrates, natural products, and lipids) atfemtomole levels and identify relevant biomarkers. (xiv,xv,xvi)Sample preparation strategies are aimed atreducing sample complexity and improving quality of the measurements. A commonmethod is solid-phase extraction (SPE) including affinity enrichment strategiesto obtained peptide and protein fractions that can be mass analyzed by directinfusion into an electrospray ionization (ESI) source or by means ofmatrix-assisted laser desorption ionization (MALDI) without further need oftime-consuming liquid chromatography (LC) separations.

Functionalized magneticbeads are SPEs that due to their small size, offer the advantage of a higherconcentration rate and therefore sensitivity due to their large binding surfacearea (xvii,xviii).Also the use of magnetic beads can be automated, providing a highly consistenthigh-throughput methodxix.In this work, we aimed to search for differentially expressed proteins aspotential biomarkers in primary congenital glaucoma patients using  MALDI-TOF MS and SPE .i- To CH, Kong CW, Chan CY,Shahidullah M, Do CW. The mechanism of aqueous humour formation. Clin Exp Optom.2002;85:335–349  ii-Freddo TF. The Glenn A.

Fry AwardLecture 1992: aqueous humor proteins: a key for unlocking glaucoma? Optom VisSci. 1993;70:263–270  iii-McLaren JW, ZiaiN, Brubaker RF. A simple three-compartment model of anterior segment kinetics.Exp Eye Res. 1993;56:355–366 iv-Tripathi RC, Millard CB, TripathiBJ. Protein composition of human aqueous humor: SDS-PAGE analysis of surgicaland post-mortem samples.

Exp Eye Res. 1989;48:117–130  v-Kinsey VE. The chemical compositionand the osmotic pressure of the aqueous humor and plasma of the rabbit. J GenPhysiol. 1951;34:389–402  vi-Fleenor DL, Shepard AR, HellbergPE, Jacobson N, Pang IH, Clark AF. TGFbeta2-induced changes in human trabecularmeshwork: implications for intraocular pressure. Invest Ophthalmol Vis Sci.

2006;47:226–234  vii-Maatta M, Tervahartiala T, Harju M,Airaksinen J, Autio-Harmainen H, Sorsa T. Matrix metalloproteinases and theirtissue inhibitors in aqueous humor of patients with primary open-angleglaucoma, exfoliation syndrome, and exfoliation glaucoma. J Glaucoma.2005;14:64–69  viii-Ozcan AA, OzdemirN, Canataroglu A. The aqueous levels of TGF-beta2 in patients with glaucoma.Int Ophthalmol. 2004;25:19–22 ix- OmennGS, States DJ, Adamski MR, et al.

Overview of the HUGO Plasma Proteome Project:results from the pilot phase with 35 collaborating laboritories and multipleanalytical groups, generating a core dataset of 3020 proteins and apublicly-available database. Proteomics. 2005;5:3226–3245x- Richardson MR, Price MO, Price FW,et al. Proteomic analysis of human aqueous humor using multidimensional proteinidentification technology. Mol Vis.

2009;15:2740–2750xi-Rohde E, Tomlinson AJ, Johnson DH, Naylor S. Comparison of protein mixtures inaqueous humor by membrane preconcentration-capillary electrophoresis-massspectrometry. Electrophoresis.

1998;19:2361–2370xii-Duan X, Lu Q, Xue P, et al. Proteomic analysis of aqueous humor from patientswith myopia. Mol Vis. 2008;14:370–377xiii-Funding M, Vorum H, Honore B, Nexo E, Ehlers N. Proteomic analysis of aqueoushumour from patients with acute corneal rejection.

Acta Ophthalmol Scand.2005;83:31–39xiv -Matrix-assistedLaser Desorption/Ionization Mass Spectrometry in Peptide and Protein Analysis J. Kathleen Lewis, Jing Wei, and Gary Siuzdak in Encyclopedia ofAnalytical Chemistry R.A. Meyers (Ed.) pp. 5880–5894 . John Wiley & SonsLtd, Chichester, 2000 xv-Int J Med Sci.

2011; 8(1): 39–47.MALDI-TOF MS Combined With Magnetic Beads for Detecting Serum ProteinBiomarkers and Establishment of Boosting Decision Tree Model for Diagnosis ofColorectal CancerChibo Liu, Chunqin Pan, Jianmin Shen, Haibao Wang, and Liang Yongxvi-Lin Wang, ChuanhaoTang, Bin Xu, Lin Yang, Lili Qu, LiangliangLi, Xiaoyan Li, Weixia Wang, Haifeng Qin, Hongjun Gao. Massspectrometry-based serum peptidome profiling accurately and reliably predictsoutcomes of pemetrexed plus platinum chemotherapy in patients with advancedlung adenocarcinomaPLOS,Published: June 8, 2017xvii-F. Magni, Y.

E. M. van der Burgt, C. Chinello et al., “Biomarkers discovery bypeptide and protein profiling in biological fluids based on functionalizedmagnetic beads purification and mass spectrometry,” Blood Transfusion, vol. 8,no. 3, pp. s92–s97, 2010.

xviii-J. F. Peter and A. M. Otto, “Magnetic particles as powerful purification toolfor high sensitive mass spectrometric screening procedures,” Proteomics, vol.10, no. 4, pp.

628–633, 2010.xix-Marco R. Bladergroen and Yuri E. M. van der Burgt, “Solid-Phase ExtractionStrategies to Surmount Body Fluid Sample Complexity in High-Throughput MassSpectrometry-Based Proteomics,” Journal of Analytical Methods in Chemistry,vol.

2015, Article ID 250131, 8 pages, 2015. doi:10.1155/2015/250131AH is a complex mixture of electrolytes,organic solutes, growth factors, cytokines, and proteins that provide themetabolic requirements to the avascular tissues of the anterior segment. (i,ii,iii)

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