The sequence of a cDNA encoding functional murine C1-inhibitor protein

Russell, Jacqueline A.; Whaley, K; Heaphy, Shaun

doi:10.1016/s0167-4781(97)00056-0

Cited by 12 publications

(6 citation statements)

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“…This cDNA sequence codes for an ORF of 504 amino acids, of which 22 represent the signal pepprobes full-length cDNA, a 5′ amplified fragment (from Ϫ84 to 592 in the genomic sequence), or a 3′ amplified fragment (from tide, as in the human sequence. It confirms a recently published mouse C1inh cDNA sequence [25], with the exception of nu-1301 to 1556 in the cDNA sequence).…”

supporting

confidence: 90%

“…Introns were PCR amplified from cleotide positions 921Ϫ923, where it carries a CGC codon for arginine, whereas the sequence published by Russell et al [25] BAC clones using exon-specific primers lying close to the intron-exon boundaries, based on the predicted conservation of has a TGC codon at this position, predicting a cysteine residue, which is not present in the human or the cattle protein [25]. Our the splice-junction positions between human and mouse.…”

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confidence: 99%

“…Total RNA codon, as in the published cDNA sequence [25]. In mouse C1inh only three of six asparagine residues known to be glycosylated was extracted from organs of BALB/c mice homogenized in guanidinium thiocyanate, according to standard protocols.…”

mentioning

confidence: 99%

“…This N-terminal domain (117 amino acids and 113 amino acids in the mouse and human proteins, respectively) is thought to be a rigid and elongated structure, and it contains DISCUSSION all the sites of O-glycosylation [28]. The predicted number of O-glycosylation sites is higher in human than in mouse C1inh Sequence analysis of naturally occurring dysfunctional mutant serpins allowed the identification of a large number of mis- [25], consistent with the observation of a slightly higher mobility of the mouse plasma protein in SDS/PAGE under reducing consense mutations that provided important knowledge about structure/function relationships among the serpins [27]. No patho-ditions (apparent molecular mass of 96 kDa for the mouse plasma protein against 104 kDa for the human protein; Fig.…”

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Molecular cloning, gene structure and expression profile of mouse C1 inhibitor

Lener

Vinci

Duponchel

et al. 1998

European Journal of Biochemistry

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The gene encoding C1 inhibitor, the major control element of activation of the classical pathway of complement and a major inhibitor of several plasma serine proteases, has been studied only in man, where deficiency of C1 inhibitor results in the dominantly transmitted disease hereditary angioedema. Full-length mouse C1 inhibitor cDNA and genomic clones were isolated and characterized as a first step towards the complete characterization of the pattern of C1 inhibitor expression and the production of an animal model of C1 inhibitor deficiency. Restriction-enzyme and sequence analyses of a full-length genomic clone demonstrated that the mouse gene has the same structure as the human homologue, but differs in size (9 kb versus 17 kb), mostly due to the presence of repetitive Alu elements in the human gene. Sequence comparisons in the promoter region indicate important similarities, i.e. the absence of a TATA box, the presence of an initiator sequence encompassing the transcription-start site and of a γ-interferonactivated sequence (GAS) element at position Ϫ124 of the human sequence. A stretch of about 100 nucleotides in intron 1 reveals an unusually high degree of conservation for non-coding sequences and contains non-canonical but conserved tandemly arranged GAS elements at positions 369 and 388 of the human sequence. This finding supports the conclusions of functional studies on the human C1INH gene indicating a role of this region in modulation of transcription by interferons. The profile of C1 inhibitor expression in mouse liver, lung, heart, kidney, spleen and brain was determined by quantitative northern blot analysis.Keywords : complement ; C1 inhibitor ; serpin ; mouse complement ; interferon response.The plasma protein C1 inhibitor (C1inh) belongs to the su-cells have been shown to be the major sites of C1inh synthesis [7, 8]. However, C1inh synthesis has been described in several perfamily of serine-protease inhibitors (serpins) [1, 2] and is the only physiological inhibitor of the activated proteases C1r and extrahepatic cells, such as monocytes, skin fibroblasts, umbelical-vein endothelial cells, platelets and several types of brain C1s of the complement system. Moreover, C1inh is the major inhibitor of plasma kallikrein and coagulation factor XIIa. Like cells [9Ϫ13]. In cell cultures C1inh synthesis is upregulated by a number of cytokines. While interferon γ has the strongest efother serpins, it inactivates target proteases by forming an SDSresistant heat-resistant protease · inhibitor complex through an fect in most of the cell types mentioned above [14Ϫ15], C1inh synthesis is also increased to different extents by interferon A, exposed peptide loop. The sequence of the reactive center contained in this loop determines the specificity toward proteases. interleukin 6 and tumor-necrosis factor A in different cell lines and primary cultures [16Ϫ17]. C1inh homologues have been In humans, genetic and acquired C1inh deficiencies lead to hereditary and acquired angioedema respectively, characterized by pu...

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confidence: 90%

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confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Molecular cloning, gene structure and expression profile of mouse C1 inhibitor

Lener

Vinci

Duponchel

et al. 1998

European Journal of Biochemistry

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“…One error up in the insoluble fraction. However, the soluble frac-was found in our DNA sequence (codon 165 was changed tion of rC1-Inh produced in an E. coli strain enabling from CAG to GAG), but this error was not corrected the formation of disulfide bonds appeared to be active, since amino acid 165 is not conserved among various suggesting that other than disulfide bonds, no post-C1-Inh proteins (16). Plasmid pTL0020 (Fig.…”

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Expression of Active Human C1 Inhibitor Serpin Domain in Escherichia coli

Lamark

Ingebrigtsen

Bjørnstad

et al. 2001

Protein Expression and Purification

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Complete sequencing and expression of three complement components, C1r, C4 and C1 inhibitor, of the classical activation pathway of the complement system in rainbow trout Oncorhynchus mykiss

2003

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Three complement components, C1r, C4 and C1 inhibitor, of the classical activation pathway have been fully sequenced and their expression investigated in rainbow trout (Oncorhynchus mykiss). Trout C1r cDNA encodes a 707-amino-acid (aa) protein with a theoretical M(r) of 77,200. The trout translation shows highest homology with carp C1r/s, and lower, equal homologies to mammalian C1r and C1s, and MASPs from other vertebrate species. However, phylogenetic analysis and structural features suggest that the trout sequence, together with the two carp sequences, are the orthologues of mammalian C1r. The trout C4 cDNA encodes a 1,724-aa protein with a theoretical M(r) of 192,600. The trout translation shows higher homologies to the carp C4B and medaka C4, but lower homologies to C4 from other species and the carp C4A. It has a predicted signal peptide of 22 aa, a alpha-chain of 773 aa, a beta-chain of 635 aa and a lambda-chain of 288 aa. Trout C1 inhibitor cDNA encodes a 611-aa protein with a theoretical M(r) of 68,700. The trout translation has a C-terminal serpin domain with high homologies with mammalian counterparts (~37% identities), and a longer N-terminus, with no significant homology to other serpins, which contains two Ig-like domains. A molecule containing two Ig-like domains followed by a serpin domain, has also been found in an EST clone from another bony fish, the Japanese flounder. This suggests a unique structural feature of C1 inhibitor in fish. The functional significance of the Ig domains is discussed. The liver is the major site of expression of the three trout complement components, C1r, C4 and C1 inhibitor, although their expression is also detectable in other tissues. The extra-hepatic expression of complement genes may be important for local protection and inflammatory responses. Low-level constitutive expression of the three components was also detectable in a trout monocyte/macrophage cell line RTS-11, but only the expression of C4 could be upregulated by LPS.

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The sequence of a cDNA encoding functional murine C1-inhibitor protein

Cited by 12 publications

References 10 publications

Molecular cloning, gene structure and expression profile of mouse C1 inhibitor

Molecular cloning, gene structure and expression profile of mouse C1 inhibitor

Expression of Active Human C1 Inhibitor Serpin Domain in Escherichia coli

Complete sequencing and expression of three complement components, C1r, C4 and C1 inhibitor, of the classical activation pathway of the complement system in rainbow trout Oncorhynchus mykiss

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