The agglutinating and immunofluorescent antibodies of antileptospiral rabbit sera.
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Biomedical subjects
Publications and source records attributed to P Roch.
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The formation of brown bodies in the coelomic cavity may result from an aggregation of coelomocytes around offending foreign cells such as bacteria, gregarines, incompatible graft fragments, and altered self structures such as setae or necrotic muscle cells. The initial nodule rapidly increases in volume by aggregation of new coelomocytes and various waste particles. When a brown body has reached a diameter of 1-2 mm, its external cells flatten and lose their adhesiveness toward free coelomocytes or waste particles and its pigment rapidly darkens. Brown bodies play an important role in homeostasis.
Fluorescence spectra of the supernatant of adherent haemocyte monolayers from Mytilus galloprovincialis, supplemented with homovanillic acid or with a tyrosyl peptide glycylglycyltyrosine (GGY), were recorded before and after stimulation by zymosan. The formation of fluorescent derivatives was observed to have spectral characteristics similar to those of fluorescent compounds generated by the exposure of homovanillic acid or GGY to a horseradish peroxidase/hydrogen peroxide system in vitro. Lucigenine-enhanced chemiluminescence (CLluc) of M. galloprovincialis haemocytes stimulated by zymosan or by phorbol ester (PMA) was measured in the presence and absence of sodium azide, a peroxidase inhibitor. Sodium azide inhibited the CLluc of haemocytes stimulated by zymosan, an effective stimulus for myeloperoxidase secretion in human polymorphonuclear leukocytes, but not the CLluc of haemocytes stimulated by PMA, indicating the presence of peroxidases with some properties of myeloperoxidase, in adherent haemocytes from M. galloprovincialis.
We have purified and characterized the serine protease inhibitor activity contained in the coelomic fluid of the earthworms, Eisenia. Serine protease inhibitor activity was stable between pH3 and 9.5, not flocculable by pH 3.0 and resistant to 100 degrees C for 15 min. or to 4 degrees C for 24 h. Ten microL of coelomic fluid was sufficient to inhibit in vitro the protease activity of 0.12 microgram of trypsin. Injection of living bacteria into earthworms resulted in increased serine protease activity 1-2 days post-injection, and increased serine protease inhibitor activity on day 4, suggesting that serine protease inhibitor is responsible for serine protease neutralization. Purified to homogeneity by affinity chromatography on trypsin, the serine protease inhibitor of Eisenia is a monomer of 14 kDa. Its partial NH2 amino acid sequence revealed a basic hydrophobic fragment which shared 68-75% homologies and 47-60% identities with several plant serine protease inhibitors. Eisenia cytotoxic activity due to the two fetidins of 40 and 45 kDa was stimulable in vitro by several serine proteases. Incubation with soybean trypsin inhibitor variant a (STIa) resulted in less cytotoxicity. The inhibitory effect occurred only when STIa was added before cell disruption. Interpretative cytotoxic scheme involving the release of intracellular cytotoxic proteins, intracellular trypsin-like activator and extracellular serine protease inhibitor suggests regulatory mechanisms for cellular/humoral immune system of earthworms.