Hemolytic reactions in the hemolymph of bivalve Sinonovacula constricta show complement-like activity.

08:00 EDT 30th April 2018 | BioPortfolio

Summary of "Hemolytic reactions in the hemolymph of bivalve Sinonovacula constricta show complement-like activity."

The complement-like hemolysis method was used to determine the total complement-like activity of the plasma of Sinonovacula constricta. In this study, the effects of both physical and chemical conditions on complement hemolysis of S. constricta were measured. Physical conditions included proportion (S. constricta plasma: 2% rabbit red blood cells), temperature, time, and incubation, while the chemical factors consisted of Lipopolysaccharide (LPS), Flagellin (FLA), Zymosan, Peptidoglycan (PGN), Phenylmethanesulfonyl fluoride (PMSF), Methylamine, and Poly (
C). The results showed that LPS, flagellin, Zymosan and PGN could activate complement-like activity of S. constricta plasma and cause hemolysis. PMSF and methylamine inhibited complement-like activity, resulting in the disappearance of hemolysis. Poly (
C) had no effect on plasma complement-like activity. When the reaction temperature was less than 50 °C, hemolytic activity would increase following an increase in temperature. The ratio of plasma to rabbit blood cells had a great impact on the rate of hemolysis. Additionally, incubation with low speed oscillation could improve the hemolysis rate. It is indicated that the hemolytic reactions in the hemolymph of bivalve S. constricta show complement-like activity. The results contribute to further research on immune function of complement in bivalve.


Journal Details

This article was published in the following journal.

Name: Fish & shellfish immunology
ISSN: 1095-9947


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Medical and Biotech [MESH] Definitions

A screening assay for circulating COMPLEMENT PROTEINS. Diluted SERUM samples are added to antibody-coated ERYTHROCYTES and the percentage of cell lysis is measured. The values are expressed by the so called CH50, in HEMOLYTIC COMPLEMENT units per milliliter, which is the dilution of serum required to lyse 50 percent of the erythrocytes in the assay.

An hereditary hemolytic uremic syndrome associated with variations in the gene that encodes COMPLEMENT FACTOR H, or the related proteins CFHR1 and CFHR3. Disease often progresses to CHRONIC KIDNEY FAILURE without the prodromal symptoms of ENTEROCOLITIS and DIARRHEA that characterize typical hemolytic uremic syndrome.

Serine proteases that cleave COMPLEMENT C3 into COMPLEMENT C3A and COMPLEMENT C3B, or cleave COMPLEMENT C5 into COMPLEMENT C5A and COMPLEMENT C5B. These include the different forms of C3/C5 convertases in the classical and the alternative pathways of COMPLEMENT ACTIVATION. Both cleavages take place at the C-terminal of an ARGININE residue.

Complement activation initiated by the binding of COMPLEMENT C1 to ANTIGEN-ANTIBODY COMPLEXES at the COMPLEMENT C1Q subunit. This leads to the sequential activation of COMPLEMENT C1R and COMPLEMENT C1S subunits. Activated C1s cleaves COMPLEMENT C4 and COMPLEMENT C2 forming the membrane-bound classical C3 CONVERTASE (C4B2A) and the subsequent C5 CONVERTASE (C4B2A3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.

A serine protease that is the complex of COMPLEMENT C3B and COMPLEMENT FACTOR BB. It cleaves multiple COMPLEMENT C3 into COMPLEMENT C3A (anaphylatoxin) and COMPLEMENT C3B in the ALTERNATIVE COMPLEMENT ACTIVATION PATHWAY.

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