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Clinical Chemistry 52: 1045-1053, 2006. First published March 30, 2006; 10.1373/clinchem.2005.065722
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(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.




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