Human anaphylatoxin (C3a) from the third component of complement. Primary structure.

Hugli, T E

doi:10.1016/s0021-9258(19)40758-8

Cited by 147 publications

(6 citation statements)

References 26 publications

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“…Although Bokisch et al (1969) reported that a 13:1 molar ratio of C3 to trypsin would effect a complete conversion of C3 to C3a and C3b within several minutes, we have found that a 130:1 molar ratio of C3 to trypsin would effect a stoichiometric conversion within 1-2 min. The C3a fragment produced at the higher trypsin concentrations was a mixture of residues 1-77 and 1-69 (numbering of Hugli, 1975). While the C3a formed at the lower trypsin concentrations still contained the 1-69 species, the lower level was preferred here in order to reduce the possibility of secondary cleavages in C3b.…”

Section: Resultsmentioning

confidence: 99%

Third component of human complement: structural analysis of the polypeptide chains of C3 and C3b

Tack¹,

Morris²,

Prahl³

1979

Biochemistry

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Section: Resultsmentioning

confidence: 99%

Third component of human complement: structural analysis of the polypeptide chains of C3 and C3b

Tack¹,

Morris²,

Prahl³

1979

Biochemistry

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“…Determination of the complete primary structure of rat anaphylatoxin permits a comparison of this molecule with the previously determined amino acid sequences of human and porcine C3a (Hugli, 1975;Corbin and Hugh, 1976) as shown in Figure 9. It appears that anaphylatoxins from these selected species share a close genetic relatedness, as evidenced by an approximate 70% sequence identify that exists between the three polypeptides.…”

Section: Discussionmentioning

confidence: 99%

Purification, characterization, and amino acid sequence of rat anaphylatoxin (C3a)

Jacobs¹,

Rubin²,

Hugli³

et al. 1978

Biochemistry

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C3a anaphylatoxin derived from the third component of complement has been isolated from rat serum and its complete amino acid seuqence determined. A three-step purification procedure was employed that consisted of gel filtration on Sephadex G-100, followed by chromatography of the anaphylatoxin-containing pool on carboxymethylcellulose. A subsequent separation on DEAE-Sephadex resolved C3a from minor contaminating peptides. Biological studies have shown that purified rat anaphylatoxin is approximately twice as active as human or porcine C3a when tested for smooth-muscle contraction. In addition to the active form of rat anaphylatoxin, a serum carboxypeptidase B inactivated form of C3a (C3ades-Arg) was purified from rat serum and utilized in subsequent structural studies. Sequence analysis of rat C3a was facilitated by a long automated Edman degradation which established the first 55 residues of the anaphylatoxin. Overlapping peptides were generated by cyanogen bromide and trypsin, and the resultant fragments were sequenced by either automated or manual Edman procedures. The primary structure of rat C3a is 70% identical to the previously determined structures of human and porcine anaphylatoxin. Antisera raised to the purified rat peptide do not cross-react immunologically by Ouchterlony analysis with either human or porcine C3a.

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“…One can further deduce from the cDNA sequence that mouse C3a is a 78 amino acid residue peptide of the same length as rat C3a. In contrast, human and porcine C3a are 77 residues long [25,47,49]. The sequence shows that mouse C3a shares 72/78 residues (92~o homology) with rat C3a, and 52/77 and 50/77 residues with human and porcine C3a, respectively [25,47,49].…”

Section: Structure Of the C3 Genementioning

confidence: 99%

“…In contrast, human and porcine C3a are 77 residues long [25,47,49]. The sequence shows that mouse C3a shares 72/78 residues (92~o homology) with rat C3a, and 52/77 and 50/77 residues with human and porcine C3a, respectively [25,47,49]. Furthermore, the cDNA sequence indicates that the cleavage of C3 by the C3 convertases occurs by hydrolysis of a single peptide bond.…”

Section: Structure Of the C3 Genementioning

confidence: 99%

Structure and expression of the C3 gene

Fey

Domdey

Wiebauer

et al. 1983

Springer Semin Immunopathol

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To map the multiple interactive sites on the C3 polypeptide, it is advantageous to combine the approaches of protein chemistry, nucleic acid technology, and molecular biology. This review summarizes the currently known molecular properties of mouse liver C3 mRNA, cloned C3 cDNA, and genomic DNA. Original data communicated have specified the amino acid sequence of the 215 amino-terminal residues of mature mouse C3 beta. Southern blot analysis of liver DNA indicated that the mouse genome contains only one type of C3 gene, that murine and human C3 sequences strongly cross-hybridize, and that the human C3 gene is not somatically rearranged. Included are descriptions of the first human C3 genomic DNA clones, their preparation, and their use to map the human C3 gene to chromosome 19 in linkage with the myotonic dystrophy (DM) locus. After a brief survey of reports describing inherited human C3 deficiencies, we discuss a Dutch family and their three members with total homozygous C3 deficiency who were the subjects of a recent publication. The restricted synthesis of C3 in major and minor producer tissues is discussed and it is proposed that the C3 gene provides a good model system for studying the molecular basis of tissue-specific gene expression. Data are presented documenting the production of C3 in two established mouse macrophage-like cell lines and two rat hepatoma cell lines in tissue cultures. A short account covers the extensive literature on regulation of C3 serum concentrations in acute and chronic inflammation and the very incomplete picture that presently depicts hormonal regulation of C3 synthesis. The final experiment reported demonstrates that nucleic acid hybridization with cloned cDNA probes is a sensitive assay for quantitative determinations of C3 mRNA. With the help of cloned cDNA and genomic DNA, researchers can address questions concerning the functional topography of the C3 polypeptide, the gene's structure, and the molecular nature of inherited C3 deficiencies in humans.

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Human anaphylatoxin (C3a) from the third component of complement. Primary structure.

Cited by 147 publications

References 26 publications

Third component of human complement: structural analysis of the polypeptide chains of C3 and C3b

Third component of human complement: structural analysis of the polypeptide chains of C3 and C3b

Purification, characterization, and amino acid sequence of rat anaphylatoxin (C3a)

Structure and expression of the C3 gene

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