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Dive into the research topics where Stephen J. Hattan is active.

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Featured researches published by Stephen J. Hattan.


Molecular & Cellular Proteomics | 2004

Multiplexed Protein Quantitation in Saccharomyces cerevisiae Using Amine-reactive Isobaric Tagging Reagents

Philip L. Ross; Yulin N. Huang; Jason Marchese; Brian L. Williamson; Kenneth C. Parker; Stephen J. Hattan; Nikita Khainovski; Sasi Pillai; Subhakar Dey; Scott Daniels; Subhasish Purkayastha; Peter Juhasz; Stephen A. Martin; Michael Bartlet-Jones; Feng He; Allan Jacobson; Darryl Pappin

We describe here a multiplexed protein quantitation strategy that provides relative and absolute measurements of proteins in complex mixtures. At the core of this methodology is a multiplexed set of isobaric reagents that yield amine-derivatized peptides. The derivatized peptides are indistinguishable in MS, but exhibit intense low-mass MS/MS signature ions that support quantitation. In this study, we have examined the global protein expression of a wild-type yeast strain and the isogenic upf1Δ and xrn1Δ mutant strains that are defective in the nonsense-mediated mRNA decay and the general 5′ to 3′ decay pathways, respectively. We also demonstrate the use of 4-fold multiplexing to enable relative protein measurements simultaneously with determination of absolute levels of a target protein using synthetic isobaric peptide standards. We find that inactivation of Upf1p and Xrn1p causes common as well as unique effects on protein expression.


Journal of Alzheimer's Disease | 2006

Detection of biomarkers with a multiplex quantitative proteomic platform in cerebrospinal fluid of patients with neurodegenerative disorders

Fadi Abdi; Joseph F. Quinn; Joseph Jankovic; Martin W. McIntosh; James B. Leverenz; Elaine R. Peskind; Randy Nixon; John G. Nutt; Katherine Chung; Cyrus P. Zabetian; Ali Samii; Melanie Lin; Stephen J. Hattan; Catherine Pan; Yan Wang; Jinghua Jin; David Zhu; G. Jane Li; Yan Liu; Dana Waichunas; Thomas J. Montine; Jing Zhang

Biomarkers are needed to assist in the diagnosis and medical management of various neurodegenerative disorders, including Alzheimers disease (AD), Parkinsons disease (PD), and dementia with Lewy body (DLB). We have employed a multiplex quantitative proteomics method, iTRAQ (isobaric Tagging for Relative and Absolute protein Quantification), in conjunction with multidimensional chromatography, followed by tandem mass spectrometry (MS/MS), to simultaneously measure relative changes in the proteome of cerebrospinal fluid (CSF) obtained from patients with AD, PD, and DLB compared to healthy controls. The diagnosis of AD and DLB was confirmed by autopsy, whereas the diagnosis of PD was based on clinical criteria. The proteomic findings showed quantitative changes in AD, PD, and DLB as compared to controls; among more than 1,500 identified CSF proteins, 136, 72, and 101 of the proteins displayed quantitative changes unique to AD, PD, and DLB, respectively. Eight unique proteins were confirmed by Western blot analysis, and the sensitivity at 95% specificity was calculated for each marker alone and in combination. Several panels of unique makers were capable of distinguishing AD, PD and DLB patients from each other as well as from controls with high sensitivity at 95% specificity. Although these preliminary findings must be validated in a larger and different population of patients, they suggest that a roster of proteins may be generated and developed into specific biomarkers that could eventually assist in clinical diagnosis and monitoring disease progression of AD, PD and DLB.


Clinical Chemistry | 2016

Applications of MALDI Mass Spectrometry in Clinical Chemistry

Mark W. Duncan; Dobrin Nedelkov; Ryan Walsh; Stephen J. Hattan

BACKGROUND MALDI-TOF mass spectrometry (MS) is set to make inroads into clinical chemistry because it offers advantages over other analytical platforms. These advantages include low acquisition and operating costs, ease of use, ruggedness, and high throughput. When coupled with innovative front-end strategies and applied to important clinical problems, it can deliver rapid, sensitive, and cost-effective assays. CONTENT This review describes the general principles of MALDI-TOF MS, highlights the unique features of the platform, and discusses some practical methods based upon it. There is substantial potential for MALDI-TOF MS to make further inroads into clinical chemistry because of the selectivity of mass detection and its ability to independently quantify proteoforms. SUMMARY MALDI-TOF MS has already transformed the practice of clinical microbiology and this review illustrates how and why it is now set to play an increasingly important role in in vitro diagnostics in particular, and clinical chemistry in general.


Journal of the American Society for Mass Spectrometry | 2016

Analysis and Quantitation of Glycated Hemoglobin by Matrix Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry

Stephen J. Hattan; Kenneth C. Parker; Marvin L. Vestal; Jane Y. Yang; David A. Herold; Mark W. Duncan

AbstractMeasurement of glycated hemoglobin is widely used for the diagnosis and monitoring of diabetes mellitus. Matrix assisted laser desorption/ionization (MALDI) time of flight (TOF) mass spectrometry (MS) analysis of patient samples is used to demonstrate a method for quantitation of total glycation on the β-subunit of hemoglobin. The approach is accurate and calibrated with commercially available reference materials. Measurements were linear (R2 > 0.99) across the clinically relevant range of 4% to 20% glycation with coefficients of variation of ≤ 2.5%. Additional and independent measurements of glycation of the α-subunit of hemoglobin are used to validate β-subunit glycation measurements and distinguish hemoglobin variants. Results obtained by MALDI-TOF MS were compared with those obtained in a clinical laboratory using validated HPLC methodology. MALDI-TOF MS sample preparation was minimal and analysis times were rapid making the method an attractive alternative to methodologies currently in practice. Graphical Abstractᅟ


Analytical Chemistry | 2015

Bifunctional glass membrane designed to interface SDS-PAGE separations of proteins with the detection of peptides by mass spectrometry.

Stephen J. Hattan; Jie Du; Kenneth C. Parker

We describe the construction and characterization of a novel membrane designed to allow proteins separated by gel electrophoresis (SDS-PAGE) to be detected as peptides by mass spectrometry in an efficient and comprehensive manner. The key attribute of the membrane is a bifunctional design that allows for the digestion of protein(s) and retention of the resulting peptides with minimal lateral diffusion. Silane chemistries are used to differentially treat the opposing surfaces of a glass filter paper to enable this unique capability.


Journal of Proteome Research | 2005

Comparative study of [Three] LC-MALDI workflows for the analysis of complex proteomic samples.

Stephen J. Hattan; Jason Marchese; Nikita Khainovski; S. Martin; Peter Juhasz


Analytical Chemistry | 2006

Methodology Utilizing MS Signal Intensity and LC Retention Time for Quantitative Analysis and Precursor Ion Selection in Proteomic LC-MALDI Analyses

Stephen J. Hattan; Kenneth C. Parker


Analytical Chemistry | 2008

Novel Three-Dimensional MALDI Plate for Interfacing High-Capacity LC Separations with MALDI-TOF

Stephen J. Hattan; Marvin L. Vestal


Journal of Chromatography A | 2004

Effect of solvent composition on signal intensity in liquid chromatography–matrix-assisted laser desorption ionization experiments

Stephen J. Hattan; Jason Marchese; Michael Albertinetti; Srinivasan C. Krishnan; Nikita Khainovski; Peter Juhasz


Archive | 2006

Systems for interfacing separations with MALDI mass spectrometry

Marvin L. Vestal; Stephen J. Hattan

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Mark W. Duncan

University of Colorado Denver

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Ali Samii

University of Washington

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Catherine Pan

University of Washington

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