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Chemical and Biological Properties of a Protein-Rich Fraction of Bacterial Lipopolysaccharides
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1977
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Protein SecretionMicrobial PathogensBacteriologyBiological PropertiesPolysaccharideBacterial PathogensMedical MicrobiologyAerobic CulturingHealth SciencesHeat LabilityMicrobial ToxinBiochemistryVirulence FactorProtein-rich FractionMembrane BiologyAntimicrobial CompoundClinical MicrobiologyBacterial LipopolysaccharidesPathogenesisMast Cell SecretionMicrobiologyCellular BiochemistryLipid ChemistryMedicineEnvelope Stress Response
Abstract Lipid A-associated protein (LAP) isolated from preparations of bacterial lipopolysaccharides (LPS, endotoxins) has been demonstrated to initiate the release of amines from rat peritoneal mast cells. The release at low concentrations of LAP requires both cellular energy and calcium, and thus appears to be a true secretory response. At higher concentrations the release is independent of these variables. The time required for maximal response is approximately 10 to 15 min at 37°C. The response appears to be a general property of Escherichia coli LAP preparations since LAP isolated from three serotypes of these organisms all have similar activity. On the basis of heat lability at 100°C, the ability of LAP to initiate mast cell secretion appears to be independent of its ability mitogenically to stimulate murine B lymphocytes.