Proteomic characterization of inter-alpha inhibitor proteins from human plasma

Inter‐alpha inhibitor proteins (IaIp) are a family of structurally related serine protease inhibitors found in relatively high concentrations in human plasma. Recent studies have implicated a role for IaIp in sepsis, and have demonstrated their potential as biomarkers in sepsis and cancer. For chara...

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Veröffentlicht in:Proteomics (Weinheim) 2006-05, Vol.6 (9), p.2874-2885
Hauptverfasser: Josic, Djuro, Brown, Mari Kino, Huang, Feilei, Lim, Yow-Pin, Rucevic, Marijana, Clifton, James G., Hixson, Douglas C.
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container_issue 9
container_start_page 2874
container_title Proteomics (Weinheim)
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creator Josic, Djuro
Brown, Mari Kino
Huang, Feilei
Lim, Yow-Pin
Rucevic, Marijana
Clifton, James G.
Hixson, Douglas C.
description Inter‐alpha inhibitor proteins (IaIp) are a family of structurally related serine protease inhibitors found in relatively high concentrations in human plasma. Recent studies have implicated a role for IaIp in sepsis, and have demonstrated their potential as biomarkers in sepsis and cancer. For characterization of isolated IaI proteins and contaminating proteins during the last steps of the purification process, SELDI‐TOF MS and HPLC–ESI‐MS/MS were used. After separation by SDS‐PAGE or 2‐DE, polypeptide bands of 80, 125 and 250 kDa were excised from gels and digested by trypsin. The tryptic peptides were analyzed by both MS methods. The main contamination during the purification process, a band of 80 kDa, contains mainly IaIp heavy chain (HC) H3. HC H1 and H2 were also found in this band. In addition, some vitamin K‐dependent clotting factors and inhibitors and other plasma proteins were identified. The 125‐kDa band, representing the pre‐alpha inhibitor, was found to contain both bikunin and HC H3. The presence of other HC H1, H2 and the recently described HC H4 was also detected by SELDI‐TOF MS. The presence of HC H1, H2, and H3 in the 125‐kDa band was confirmed by ESI‐MS/MS, but not the presence of the H4. Three polypeptides, H1 and H2 together with bikunin, were identified in the 250‐kDa band, representing the ITI, by both MS techniques. Once again, the presence of H4 was detected in this band only by SELDI‐TOF MS, but the number of corresponding peptides was still not sufficient for final identification of this polypeptide. The importance of the application of proteomic methods for the proper evaluation of therapeutic drugs based on human plasma is discussed.
doi_str_mv 10.1002/pmic.200500563
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subjects Alpha-Globulins - analysis
Alpha-Globulins - isolation & purification
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Biomarkers
Diagnostic and therapeutic agents
Fundamental and applied biological sciences. Psychology
Gas Chromatography-Mass Spectrometry
Humans
Inter-alpha inhibitor proteins
Membrane Glycoproteins - blood
Membrane Glycoproteins - isolation & purification
Miscellaneous
Molecular Sequence Data
Plasma - chemistry
Proteins
Proteomic characterization
Proteomics
Serine Proteinase Inhibitors - blood
Serine Proteinase Inhibitors - isolation & purification
Spectrometry, Mass, Electrospray Ionization
Trypsin Inhibitor, Kunitz Soybean - blood
Trypsin Inhibitor, Kunitz Soybean - isolation & purification
title Proteomic characterization of inter-alpha inhibitor proteins from human plasma
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