Interactions between bacterial pyrogen and proteolipid extracted from the cerebrum (I).

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Abstract
Proteolipid of the myelin sheath and its parent glial membrane may possibly interact with bacterial [Escherichia coli] pyrogen (lipopolysaccharide, LPS) during penetration into the brain. Thus, the interaction of LPS with proteolipid derived from the cerebrum of rabbits, rats and chickens was investigated. I.v. administration of LPS (1 .mu.g/kg) produced a febrile response in rabbits but not in rats and chickens. Marked hyperthermia was observed in these 3 animals after intracisternal administration of LPS (0.01-0.1 .mu.g/kg). Dinitrophenol (30 mg/kg s.c.) induced a high fever in these 3 animals (particularly in the chickens). The pyrogenicity of LPS given i.v. to rabbits was inactivated by incubation of LPS with proteolipid in vitro. Inactivation effects of extracted proteolipid, in decreasing order, was seen in chickens, rats and rabbits. In rats, the inactivation effects of proteolipid from the adult animal were more potent than in the case of newborn animals. The febrile response induced by dinitrophenol and leukocytic pyrogen in rabbits, however, was not suppressed by incubation with proteolipid extracted from rabbit brain. Proteolipids may play an important role in the mechanism of penetration of LPS into the brain.

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