The Anaphylatoxic Peptide C3a of Guinea Pig Complement

Meuer, Stefan; Becker, Stefan; Hadding, U.; Bitter‐Suermann, D.

doi:10.1016/s0340-904x(78)80028-1

Cited by 13 publications

(3 citation statements)

References 18 publications

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“…Guinea pig C3 was purified from pooled guinea plasma as described [20] and was radiolabeled using the lactoperoxidasecontaining radioiodination system NEZ 151 (New England Nuclear, Dreieich, FRG) according to the manufacturers directions. The specific radioactivity of the '"I-labeled C3 (12%-C3) was in the range of 1 X lo6 cpmlpg protein.…”

Section: Measurement Of C3 Catabolism Using '251-laheled C3mentioning

confidence: 99%

An inherited deficiency of the third component of complement, C3, in guinea pigs

et al. 1986

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Hereditary deficiency of the third component of complement, C3, is found very seldom in the human. C3 deficiency is associated with severe bacterial infections revealing the central role of C3 in complement activation via the classical or alternative pathway. We describe a new hereditary C3 deficiency in strain 2 guinea pigs. Serum from these animals had a markedly reduced lytic activity in a standard assay for complement-dependent, antibody-mediated cytotoxicity. In functional assays of individual components, the hemolytic activity of the components C4, C2, C5 and of factors B, D and H was in the normal range. The functional C3 titer, and similarly C3 antigenic activity in the serum of these C3-deficient animals (C3D) was on average only 5.7% of normal activity. Typing the animals with alloantisera or monoclonal antibodies to guinea pig Ia-antigens revealed that the C3D animals had the major histocompatibility complex-haplotype of inbred strain 2 guinea pigs (B.1, Ia.2,4). The C3 defect is not linked to the major histocompatibility complex and, in addition, is not linked to a C3a receptor deficiency. Macrophages and hepatocytes of the C3D animals have an unimpaired capacity for synthesis and secretion of C3 as measured by enzyme-linked immunosorbent assay. There was no indication for hypercatabolism of normal C3 by the animals as shown by plasma clearance of 125I-radiolabeled C3. Thrombocytes of the C3D animals responded normally to stimulation with purified C3a in an ATP-release assay without an indication for a desensitization in vivo. Possibly the fault resides in an enhanced susceptibility of their own C3 to proteolysis. However, C3 partially purified from the plasma of the C3D animals or secreted by hepatocytes exhibited no obvious structural differences to purified normal C3 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis or in immunoblotting. The C3D serum had a reduced bactericidal activity compared to normal or to C4-deficient serum. Nevertheless, the animals are apparently healthy without an indication for increased frequency of bacterial infections. These guinea pigs provide an unique model for analysis of the biological functions of C3 in vivo and in vitro without the need for artificial C3-depletion procedures with all their known and unknown side-effects.

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Section: Measurement Of C3 Catabolism Using '251-laheled C3mentioning

confidence: 99%

An inherited deficiency of the third component of complement, C3, in guinea pigs

et al. 1986

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“…gp C3 was purified from pooled gp plasma as described [5]. C3b was generated from highly purified C3 by cleavage with a preformed cobra venom factor (VF)-dependent enzyme…”

Section: Preparation Of C3bmentioning

confidence: 99%

Inhibition of interleukin 3 function by a fragment of the third component of complement

et al. 1987

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A C3d-like (C3d-1) fragment of 33 kDa was isolated and its biological activity studied. The fragment was generated from guinea pig C3b by porcine pancreas kallikrein and purified by fast protein liquid chromatography. The C3d-like fragment inhibited interleukin (IL) 2-dependent T lymphocyte proliferation. The suppressive activity of the described C3d-1 fragment was not restricted to lymphocytes as targets but inhibited in addition the proliferation of a nonlymphocyte mast cell line which was strictly IL3-dependent in its proliferative capacity. Kinetic studies implied early stages of cellular proliferation to be influenced. Furthermore, the C3d-1 fragment was not only an inhibitor of cellular proliferation but was also a potent inducer of leukocytosis.

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“…Shin & Mayer (1968) were the first to obtain guinea pig C3 in a biochemically pure state, although the protein had been previously prepared in a functionally pure form (Nelson et al, 1966). Further procedures for the isolation of guinea pig C3 have been published; however, yields based on quantitative functional and antigenic analyses were not reported (Bitter-Suermann et al, 1970;Kawachi-Takahashi et al, 1973;Okuda, 1973;Meuer et al, 1978). In this paper we (1) describe a significantly improved method for the isolation of guinea pig C3, (2) present the amino-terminal structures of several subdomain structures of the protein, (3) identify the presence of a thiol ester site in the native protein, and (4) position this site within the amino-terminal region of C3d.…”

mentioning

confidence: 99%

Identification and alignment of a thiol ester site in the third component of guinea pig complement

Thomas¹,

Tack²

1983

Biochemistry

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The Anaphylatoxic Peptide C3a of Guinea Pig Complement

Cited by 13 publications

References 18 publications

An inherited deficiency of the third component of complement, C3, in guinea pigs

An inherited deficiency of the third component of complement, C3, in guinea pigs

Inhibition of interleukin 3 function by a fragment of the third component of complement

Identification and alignment of a thiol ester site in the third component of guinea pig complement

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