Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 52: 1045-1053, 2006. First published March 30, 2006; 10.1373/clinchem.2005.065722
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow 065722.Supplemental data
Right arrow All Versions of this Article:
clinchem.2005.065722v1
clinchem.2005.065722v2
52/6/1045    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (21)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Song, J.
Right arrow Articles by Zhang, Z.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Song, J.
Right arrow Articles by Zhang, Z.
Related Collections
Right arrow Cancer Diagnostics (since 2002)
Right arrow Proteomics and Protein Markers
(Clinical Chemistry. 2006;52:1045-1053.)
© 2006 American Association for Clinical Chemistry, Inc.

Proteomics and Protein Markers

Quantification of Fragments of Human Serum Inter-{alpha}-Trypsin Inhibitor Heavy Chain 4 by a Surface-Enhanced Laser Desorption/Ionization-Based Immunoassay

Jin Song1, Manisha Patel1, C. Nicole Rosenzweig1, Yee Chan-Li1, Lori J. Sokoll1, Eric T. Fung2, Nam-Ho Choi-Miura3, Michael Goggins4, Daniel W. Chan1 and Zhen Zhang1,a

1 Center for Biomarker Discovery, Department of Pathology, and4 Department of Pathology, Johns Hopkins Medical Institutions, Baltimore, MD.
2 Ciphergen Biosystems, Fremont, CA.
3 Department of Physiological Chemistry, School of Pharmaceutical Sciences, Showa University, Shinagawa, Tokyo, Japan.

aAddress correspondence to this author at: Department of Pathology, Johns Hopkins Medical Institutions, 419 N. Caroline St., Baltimore, MD 21231. Fax 410-502-7882; e-mail zzhang7{at}jhmi.edu.

Background: Several proteolytically derived fragments from the proline-rich region (PRR) of human inter-{alpha}-trypsin inhibitor heavy chain 4 (ITIH4) have been identified by surface-enhanced or matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS or MALDI-TOF-MS) as potential disease markers.

Methods: Previously, we developed a SELDI-based immunoassay that can simultaneously distinguish and quantify multiple isoforms/variants of a protein/peptide of interest. In this study, we used this high-throughput approach to quantify and characterize the extensive fragmentation within the PRR of human serum ITIH4 and determined its association with different disease conditions. The ITIH4-related fragments were first immunocaptured by use of beads coupled with peptide-specific antibodies. The eluates were then studied by SELDI-TOF-MS. In addition, freshly collected and immediately processed serum and plasma samples were used to analyze the ex vivo stability of these ITIH4 fragments.

Results: Human serum ITIH4 was shown to be extensively proteolytically processed within the PRR, and its fragmentation patterns were closely associated with different disease conditions. Fragmentation patterns were generally consistent with cleavages by endoprotease followed by exoprotease actions. Observed fragments changed little under different assay conditions or blood collection and processing procedures.

Conclusions: The fragmentation patterns within the PRR of human serum ITIH4 are associated with different disease conditions and may hold important diagnostic information. These fragmentation patterns could be useful as potential biomarkers for detection and classification of cancer.




The following articles in journals at HighWire Press have cited this article:


Home page
 The Computer JournalHome page
A. Gammerman, V. Vovk, B. Burford, I. Nouretdinov, Z. Luo, A. Chervonenkis, M. Waterfield, R. Cramer, P. Tempst, J. Villanueva, et al.
Serum Proteomic Abnormality Predating Screen Detection of Ovarian Cancer
The Computer Journal, May 1, 2009; 52(3): 326 - 333.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
J. M. Koomen, E. B. Haura, G. Bepler, R. Sutphen, E. R. Remily-Wood, K. Benson, M. Hussein, L. A. Hazlehurst, T. J. Yeatman, L. T. Hildreth, et al.
Proteomic Contributions to Personalized Cancer Care
Mol. Cell. Proteomics, October 1, 2008; 7(10): 1780 - 1794.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y. Tang, K. Kitisin, W. Jogunoori, C. Li, C.-X. Deng, S. C. Mueller, H. W. Ressom, A. Rashid, A. R. He, J. S. Mendelson, et al.
Progenitor/stem cells give rise to liver cancer due to aberrant TGF-{beta} and IL-6 signaling
PNAS, February 19, 2008; 105(7): 2445 - 2450.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Chem.Home page
L. A. Liotta and E. F. Petricoin
Putting the "Bio" back into Biomarkers: Orienting Proteomic Discovery toward Biology and away from the Measurement Platform
Clin. Chem., January 1, 2008; 54(1): 3 - 5.
[Full Text] [PDF]

Home page
 Clin. Chem.Home page
M. J. Bennett
Untargeted Metabolomic Analysis Hits the Target
Clin. Chem., December 1, 2007; 53(12): 2037 - 2039.
[Full Text] [PDF]

Home page
 Clin. Chem.Home page
J. F. Timms, E. Arslan-Low, A. Gentry-Maharaj, Z. Luo, D. T'Jampens, V. N. Podust, J. Ford, E. T. Fung, A. Gammerman, I. Jacobs, et al.
Preanalytic Influence of Sample Handling on SELDI-TOF Serum Protein Profiles
Clin. Chem., April 1, 2007; 53(4): 645 - 656.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2006 by the American Association for Clinical Chemistry.