The H4P Heavy Chain of Inter-α-inhibitor Family Largely Differs in the Structure and Synthesis of Its Prolin-Rich Region from Rat to Human

Soury, Emmanuelle; Olivier, Emmanuel; Daveau, Maryvonne; Hiron, Martine; Claeyssens, Sophie; Risler, Jean‐Loup; Salier, Jean‐Philippe

doi:10.1006/bbrc.1998.8128

Cited by 28 publications

(27 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Ordinate : relative mRNA levels expressed as a percentage of the level measured in healthy animals (100 %) after normalization with the 18 S RNA level. The results obtained with an hepatic mRNA whose level is up-regulated by a turpentine challenge, namely the IαIH4P mRNA [28,37], are shown as a control for a positive APP mRNA. Note that the absolute levels of fetuin-A versus fetuin-B mRNA cannot be compared in this figure.…”

Section: Figure 3 Inflammation-associated Changes In Hepatic Levels Omentioning

confidence: 97%

“…A full-length rat cDNA for the so-called IαIH4P precursor of the Inter-α-Inhibitor family of plasma proteins has been described previously [28] and was used in the present study as a probe for the mRNA of a positive APP. Mouse cDNA probes for 18 or 28 S RNAs were kindly provided by Dr Y. Rayssiguier (Institut National de la Recherche Agronomique, Clermont-Ferrand, France) or Dr J. Mallet (Centre National de la Recherche Scientifique, Paris, France), respectively.…”

Section: Cdna Probesmentioning

confidence: 99%

“…In all groups, total hepatic RNAs from five animals were pooled, separated by electrophoresis, blotted and successively hybridized with four rat cDNA probes, namely those for (i) fetuin-A, (ii) fetuin-B, (iii) IαIH4P used herein as a control for a positive APP mRNA [28,37] and (iv) GAPDH used as a control for an mRNA whose level does not vary in liver during APR [36,37]. A single blot was used throughout the study.…”

Section: Table 1 Hepatic Levels Of Fetuin-a and Fetuin-b Mrnas As A Fmentioning

confidence: 99%

See 2 more Smart Citations

Fetuin-B, a second member of the fetuin family in mammals

Olivier

Soury

Ruminy

et al. 2000

Biochemical Journal

112

View full text Add to dashboard Cite

A set of orthologous plasma proteins found in human, sheep, pig, cow and rodents, now collectively designated fetuin-A, constitutes the fetuin family. Fetuin-A has been identified as a major protein during fetal life and is also involved in important functions such as inhibition of the insulin receptor tyrosine kinase activity, protease inhibitory activities and development-associated regulation of calcium metabolism and osteogenesis. Furthermore, fetuin-A is a key partner in the recovery phase of an acute inflammatory response. We now describe a second protein of the fetuin family, called fetuin-B, which is found at least in human and rodents. On grounds of domain homology, overall conservation of cysteine residues and chromosomal assignments of the corresponding genes in these species, fetuin-B is unambiguously a paralogue of fetuin-A. Yet, fetuin-A and fetuin-B exhibit significant differences at the amino acid sequence level, notably including variations with respect to the archetypal fetuin-specific signature. Differences and similarities in terms of gene regulation were also observed. Indeed, studies performed during development in rat and mouse showed for the first time high expression of a member of the fetuin family in adulthood, as shown with the fetuin-B mRNA in rat. However, like its fetuin-A counterpart, the fetuin-B mRNA level is down-regulated during the acute phase of experimentally induced inflammation in rat.

show abstract

Section: Figure 3 Inflammation-associated Changes In Hepatic Levels Omentioning

confidence: 97%

Section: Cdna Probesmentioning

confidence: 99%

Section: Table 1 Hepatic Levels Of Fetuin-a and Fetuin-b Mrnas As A Fmentioning

confidence: 99%

See 1 more Smart Citation

Fetuin-B, a second member of the fetuin family in mammals

Olivier

Soury

Ruminy

et al. 2000

Biochemical Journal

112

View full text Add to dashboard Cite

show abstract

“…Inter-␣-trypsin inhibitor heavy chain 4 (ITIH4) 5 is a plasma glycoprotein with a relative molecular mass of 120 000 that is expressed mainly in liver and that acts as an acute-phase protein in several species (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11). Unlike other members of the inter-␣-trypsin inhibitor family (12,13 ), ITIH4 is present in plasma as a single-chain protein because its COOH terminus lacks the consensus sequence (DPHFII) for bikunin assembly through the glycosaminoglycan bridges (2,3,(12)(13)(14).…”

mentioning

confidence: 99%

“…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 ).…”

mentioning

confidence: 99%

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

View full text Add to dashboard Cite

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

show abstract