Primary Structure of the Pig Homologue of Human IHRP: Inter- -Trypsin Inhibitor Family Heavy Chain-Related Protein

Hashimoto, Ken; Tobe, Takashi; Sumiya, Jun-ichi; Sano, Yuichi; Choi-Miura, Nam-Ho; Ozawa, Akihito; Yasue, Hiroshi; Tomita, Motowo

doi:10.1093/oxfordjournals.jbchem.a021281

Cited by 25 publications

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“…2C). A search of the FASTA protein database showed high homology with the deduced amino acid sequence of human PK-120 (human IHRP) (33,35) and pig MAP (pig IHRP) (19). Figure 2C also shows the moderate homology found with the heavy chain H3 of the human ITI family (6).…”

Section: Resultsmentioning

confidence: 86%

“…This protein, which is also called porcine inter-alpha-trypsin inhibitor human-related protein (pig IHRP) (19), is the porcine counterpart of human plasma kallikrein-sensitive protein (PK-120; also called human IHRP) (33,35). The amino acid sequences obtained from the pig, human, and rat proteins show significant homology for over two-thirds of the amino-terminal sequences with the heavy chains (H1, H2, and H3) of the inter-alpha-trypsin inhibitor (ITI) protein family (19,33,35,36,39). Pig MAP or pig IHRP, PK-120 or human IHRP, and the homologous rat protein have been designated ITIH4, a new member of the heavy-chain ITI family (36).…”

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confidence: 99%

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ITIH4 (Inter-Alpha-Trypsin Inhibitor Heavy Chain 4) Is a New Acute-Phase Protein Isolated from Cattle during Experimental Infection

et al. 2004

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We have isolated from calf serum a protein with an apparent M r of 120,000. The protein was detected by using antibodies against major acute-phase protein in pigs with acute inflammation. The amino acid sequence of an internal fragment revealed that this protein is the bovine counterpart of ITIH4, the heavy chain 4 of the inter-alpha-trypsin inhibitor family. The response of this protein in the sera was determined for animals during experimental bacterial and viral infections. In the bacterial model, animals were inoculated with a mixture of Actinomyces pyogenes, Fusobacterium necrophorum, and Peptostreptococcus indolicus to induce an acute-phase reaction. All animals developed moderate to severe clinical mastitis and exhibited remarkable increases in ITIH4 concentration in serum (from 3 to 12 times the initial values, peaking at 48 to 72 h after infection) that correlated with the severity of the disease. Animals with experimental infections with bovine respiratory syncytial virus (BRSV) also showed increases in ITIH4 concentration (from two-to fivefold), which peaked at around 7 to 8 days after inoculation. Generally, no response was seen after a second infection of the same animals with the virus. Because of the significant induction of the protein in the animals in the mastitis and BRSV infection models, we can conclude that ITIH4 is a new positive acute-phase protein in cattle.The acute-phase response occurs in animals as a consequence of infection, inflammation, or trauma. It is a nonspecific response mediated by inflammation-related cytokines (mainly by interleukin-6 [IL-6], IL-1, and tumor necrosis factor alpha) and is characterized by several systemic reactions, including fever, catabolism of muscle protein, alterations in sleep and appetite patterns, and changes in the concentrations of a group of serum proteins called acute-phase proteins (APP) (3,22,27,40).APP have been studied extensively in humans and in many animal species, mostly rats (38), though the panel of these proteins is probably not complete. The APP response differs among species. For domestic animals, the studies on APP are relatively recent (reviewed in reference 18). For cattle, several APP, including serum amyloid A, haptoglobin, alpha-1-acid glycoprotein, and alpha-1-proteinase inhibitor (alpha-1-antitrypsin), have been shown to increase in different inflammatory processes, in both in vivo (9,14,18,20,23,25,32) and in vitro models (2, 31). The course of infection in human patients is monitored by the determination of APP in blood samples (43), and a similar clinical use has been proposed for veterinary medicine (15,18,26) as well as for monitoring the health status of animals during farm production and at slaughter (42).In previous works from our laboratory, a new 120-kDa plasma glycoprotein, designated major acute-phase protein or pig MAP, was described as an APP occurring in pigs with turpentine-induced inflammation (16,29). This protein, which is also called porcine inter-alpha-trypsin inhibitor human-related protein (pig IHRP) (...

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Section: Resultsmentioning

confidence: 86%

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confidence: 99%

ITIH4 (Inter-Alpha-Trypsin Inhibitor Heavy Chain 4) Is a New Acute-Phase Protein Isolated from Cattle during Experimental Infection

et al. 2004

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“…Day 1 serum was serially diluted, × 2, × 4, × 10 and × 20, and compared to Day 0. rat and mouse revealed high homology throughout their entire amino acid sequences, with the exception of approximately one hundred residues from Val 605 to Pro 716 in human IHRP. 14) In this region IHRP has a kallikrein cleavage site and mouse IHRP contains the putative kallikrein cleavage site (Phe 626-Arg 627). This region is coded by small exons (exons 14, 15, 16, 17, 18 and 19) in the human IHRP gene.…”

Section: Fig 4 the Effect Of Lps On The Expression Of Ihrp Mrnamentioning

confidence: 99%

Mouse Inter-Alpha-Trypsin Inhibitor Family Heavy Chain-Related Protein is an Acute Phase Protein Induced by Inflammation

Sano

Tobe

Saguchi

et al. 2006

JOURNAL OF HEALTH SCIENCE

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The mouse counterpart of the human inter-alpha-trypsin inhibitor family heavy chain-related protein (IHRP), inter-alpha-trypsin inhibitor family heavy chain-related protein, was partially purified from mouse serum through Western blot analysis using anti-human IHRP antibody. The amino-terminal amino acid sequence was then determined, and the cDNA clone encoding mouse IHRP was isolated and characterized. The mouse IHRP amino-terminal amino acid sequence matched the predicted sequence from the cDNA, and has high homology compared with human and pig IHRP. Furthermore, the whole mouse IHRP amino acid sequence predicted from the cDNA nucleotide sequence showed reasonable homology to that of both human and pig IHRP. Mouse IHRP expression was induced by treatment with typical inflammation-inducing compounds, such as turpentine and lipopolysaccharide.

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“…The COOH terminus of human ITIH4 contains a proline-rich region (PRR; Gly 611 -Gln 730 ; GenBank accession no. Q14624) that is ϳ120 residues in length and harbors species-and tissue-specific domains (2,4,15 ). ITIH4 is highly sensitive to plasma kallikrein and has been proposed to be a potential precursor for plasma kallikrein-induced bioactive peptides (1,2 ).…”

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

et al. 2006

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Background: Several proteolytically derived fragments from the proline-rich region (PRR) of human inter-␣-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 peptidespecific 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

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Primary Structure of the Pig Homologue of Human IHRP: Inter- -Trypsin Inhibitor Family Heavy Chain-Related Protein

Cited by 25 publications

References 0 publications

ITIH4 (Inter-Alpha-Trypsin Inhibitor Heavy Chain 4) Is a New Acute-Phase Protein Isolated from Cattle during Experimental Infection

ITIH4 (Inter-Alpha-Trypsin Inhibitor Heavy Chain 4) Is a New Acute-Phase Protein Isolated from Cattle during Experimental Infection

Mouse Inter-Alpha-Trypsin Inhibitor Family Heavy Chain-Related Protein is an Acute Phase Protein Induced by Inflammation

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

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