Human inter-α-trypsin inhibitor: Full-length cDNA sequence of the heavy chain H1

Diarra‐Mehrpour, Maryam; Bourguignon, Jeannette; Bost, Fréd́eric; Sesboüé, Richard; Muschio, Florence; Sarafan, Nasrin; Martín, J. P.

doi:10.1016/0167-4781(92)90065-8

Cited by 30 publications

(22 citation statements)

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“…The peptide sequence of the light chain, deduced from that of the cDNA [5,6], corresponds to the precursor of two tandemly arranged proteins, ~l-microglobulin and bikunin (responsible for the protease inhibitory activity), which separate at the time of ITI maturation [7,8]. Three mRNAs coding for distinct heavy-chain peptides, called H1, H2 and H3, were then described [9][10][11]; they showed highly similar amino acid sequences. Further, the ITI-related proteins are synthesized in the liver by four genes located on three different chromosomes [12].…”

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confidence: 99%

Involvement of the three inter‐α‐trypsin inhibitor (ITI) heavy chains in each member of the serum ITI family

et al. 1995

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Partial cDNAs coding for each of the three human inter-a-trypsin inhibitor (ITI) heavy chains were expressed in a bacterial plasmid system and rabbits were immunised with the fusion peptides obtained. Despite the strong sequence homology of these chains, the antisera turned out to be highly specific in the analysis of corresponding mRNA translation products or partially digested serum ITI. Besides classical serum ITI members, their use in Western blotting made it possible to evidence an H3-related ITI form and a low-amount HI-related HC/bikunin component. The relative levels of ITI family members was further studied in baboon and foetal calf sera.

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confidence: 99%

Involvement of the three inter‐α‐trypsin inhibitor (ITI) heavy chains in each member of the serum ITI family

et al. 1995

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“…The genetic polymorphism of plasma ITI has been described by isoelectric focusing (IEF) and immunostaining techniques (Vogt and Cleve, 1990;Vogt et al, 1991a;Yuasa et al, 1991;Harada et al, 1994) and has been revealed to arise from the variation for the ITIH1 chain by Southern hybridization analysis (Vogt et al, 1994) and by an immunological assay with three monoclonal antibodies for each chain (Harada et al, 1995). The ITIHI chain is composed of 877 amino acid residues with a molecular mass of 92 kDa (Diarra-Mehrpour et al, 1992). The ITIHI gene spans about 14 kb and includes 22 exons with 15-281 bp in size (Bost et al, 1993).…”

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ITIH1*Q0 iwate, a null allele of inter-alpha-trypsin inhibitor H1 caused by deletion/frameshift mutation

et al. 1997

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SummaryThe molecular characterization of the first example of null allele in the inter-alpha-trypsin inhibitor H1 (ITIH1) system, ITIHI* QOiwate, encountered as apparent inverse homozygosity of ITIH 1 phenotypes between mother and child in a paternity case, is described. Single-strand conformation polymorphism analysis and subsequent sequencing showed that deletion of a single nucleotide in the codon for Lys 8r results irfa frameshift causing a terminator codon downstream of the deletion. This leads to premature termination of ITIH1 protein translation at amino acid 128, resulting in a truncated protein. Key Wordsinter-alpha-trypsin inhibitor HI, null allele, frameshift mutation, PCR, SSCP, sequencing Inter-alpha-trypsin inhibitor (ITI) is a plasma serine protease inhibitor consisting of two heavy chains, ITIH1 and ITIH2, and one light chain, ITIL (Enghild et al., 1989), for which the structural genes are located on chromosome 3p211-p212, 10p13 and 9q32-33, respectively (Diarra-Mehrpour et al., 1989). The function of the heavy chains is not clear, but is likely to play a role of carrier protein as a regulator for hyaluronan (Huang et al., 1993). The genetic polymorphism of plasma ITI has been described by isoelectric focusing (IEF) and immunostaining techniques (Vogt and Cleve, 1990;Vogt et al., 1991a;Yuasa et al., 1991;

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“…The mature proteins HC1, HC3 and HC2 contain five, two and four Cys residues, respectively. Given the fact that two Asn residues were found to be glycosylated among four putative sites (NXTIS) in HC2 ll.51 and two in HC1 [14], it is highly probable that the two such sites in HC3 are also derivatized (Figs 2 and 3).…”

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“…The comparison between H1 [14], H3 and H2 [15] precursors shows that they all undergo a proteolytic processing behind an Arg residue in their N-terminal (Fig. 3).…”

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Human pre‐α‐trypsin inhibitor‐precursor heavy chain cDNA and deduced amino‐acid sequence

Bourguignon

Diarra‐Mehrpour

Thiberville

et al. 1993

European Journal of Biochemistry

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Pre-a-trypsin inhibitor (Pal) is a serine-proteinase inhibitor of M, 130000 found in human serum. This protein belongs to the family of proteins called inter-a-trypsin inhibitor (ITI). Pa1 is composed of a heavy chain (HC3) and of a light chain (bikunin), synthesized by two separate mRNA. Bikunin is identical to the IT1 light chain, the structure of which has already been established. The HC3 is obtained from a precursor called H3. The bikunin is covalently linked to HC3 by a chondroitin-4-sulfate glycosaminoglycan. We report here the H3 full-length cDNA sequence and the deduced amino-acid sequence of the heavy-chain H3 precursor. The high degree of similarity between the nucleotide and amino-acid sequences of IT1 heavy-chain families H1, H2, H3 is examined with respect to their probable structure and assembly with bikunin in the final proteins, Pal and ITI.Pre-a-trypsin inhibitor (PaI) is a recently described glycoprotein of M, 130000 [l], structurally related to the intera-trypsin-inhibitor (ITI) family of serine-proteinase inhibitors. Pal is composed of one heavy-chain of M, 90000, called HC3, and one light chain of M , 30000 named bikunin because it is composed of two pancreatic-trypsin-inhibitor(Kunitz)-type domains [2]. The isolation and sequence of ITI-light-chain cDNA [3, 41 and gene [5] showed that they code for two tandemly arranged proteins : a-1-microglobulin and bikunin. Pal chains are covalently linked to each other by an unusual structure among plasma proteins: the interchain linkage is mediated through esterification of the a-carbon of the C-terminal Asp of HC3 with the C6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain 0-linked to SerlO of the bikunin [6]. The sequence analysis of peptides derived from the proteolysis of Pal indicates that the heavy-chain precursor (heavy-chain precursors are called H, whereas mature heavy chains are denominated HC, according to [l]) of this protein is coded by the IT1 H3 heavy-chain cDNA which we previously described [7]. We have also shown that the H3 gene is located in the p211-p212 region of chromosome 3 [7]. Abbreviations. PaI, pre-a-trypsin inhibitor; ITI, inter-a-trypsin inhibitor; H1, H2 and H3, heavy chain precursor of inter-a-trypsin inhibitor family; HC1, HC2 and HC3, mature heavy chain of inter-atrypsin-inhibitor family; RACE, rapid amplification of cDNA ends.Enzymes. Reverse transcriptase (EC 2.7.7.49) ; DNA polymerase I, Tuq DNA polymerase (EC 2.7.7.7).Note. The novel nucleotide sequence data reported here have been deposited in the EMBL/GenBank library under accession number X 67055.In the present study, we report the complete cDNA sequence of H3 heavy chain, and therefore the complete amino-acid sequence of Pa1 precursor HC3 heavy chain. The amino-acid-sequence similarity between ITI-heavy-chain families H1, H2 and H3 was also studied. MATERIALS AND METHODS ReagentsRestriction endonucleases, reverse transcriptase, M13 mp18, M13 mp19 and pUC 18 vectors were from Bethesda Research Laboratories. Nitrocellulose filters (BA 85) we...

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Human inter-α-trypsin inhibitor: Full-length cDNA sequence of the heavy chain H1

Cited by 30 publications

References 16 publications

Involvement of the three inter‐α‐trypsin inhibitor (ITI) heavy chains in each member of the serum ITI family

Involvement of the three inter‐α‐trypsin inhibitor (ITI) heavy chains in each member of the serum ITI family

ITIH1*Q0 iwate, a null allele of inter-alpha-trypsin inhibitor H1 caused by deletion/frameshift mutation

Human pre‐α‐trypsin inhibitor‐precursor heavy chain cDNA and deduced amino‐acid sequence

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