A novel cellular prion protein isoform present in rapid anterograde axonal transport.

We studied the axonal transport of PrP(C) in hamster retinal and sciatic nerve axons. Our results show that a novel 38kDa form is the predominant form in rapid anterograde axonal transport while the 36kDa and 33kDa PrP(C) forms, abundant in nerve and brain, appear to be either stationary or slowly transported. We did not detect any significant retrograde transport of PrP(C). These results show that 38kDa PrP(C) is the form exported from the cell body to the axonal compartment where it may represent the precursor to the more abundant PrP(C) forms after its modification in nerve fibres or terminals.

Cellular prion protein localization in rodent and primate brain.

The presence of an abnormal, protease-resistant form of the prion protein (PrP) is the hallmark of various forms of transmissible spongiform encephalopathies (TSE) which can affect a number of mammalian species, including humans. The normal, cellular form of this protein, PrPc, while abundant in brain is also present in many tissues and a number of species. In order to address the unresolved question of the precise localization of normal cerebral PrPc, we used a free-floating immunohistochemistry procedure to localize the protein at both the light and the electron microscopic levels in the brain of three TSE-sensitive species: hamster, macaque and humans. This method shows that PrPc is abundant in synaptic terminal fields in olfactory bulb, limbic-associated structures and in the striato-nigral complex, whereas many other regions of the hamster brain are essentially devoid of immunoreactivity. With the striking exception of the olfactory nerve, in which axons are continually growing throughout life, PrPc is not abundant in fibre pathways. PrPc distribution in the primate hippocampus and cortex is very similar to the distribution observed in hamster. PrPc was present at synaptic profiles as shown by immunoelectron microscopy, but was not detectable in neuronal perikaryon either by light or electron microscopy. Our results show that PrPc is abundant in a number of brain structures known for ongoing plasticity, and are consistent with the hypothesis that the protein also plays a role in synaptic function.

Osteopetrose: relato de caso / Osteopetrosis: case report

A osteopetrose é raro distúrbio do metabolismo ósseo, de caráter hereditário, que pode apresentar muitas manifestaçöes clínicas e achados radiológicos característicos. Entre as alteracöes clínicas mais frequentes encontram-se fraturas patológicas, dores ósseas e neuropatia cranianas. Apresentamos, a seguir, o relato do caso de uma paciente com diagnóstico de osteopetrose em sua forma dominante

Iron-rich Basal sediments from the eastern equatorial pacific: leg 16, deep sea drilling project.

Iron-rich sediments chemically similar to those forming at present on the crest of the East Pacific Rise have been found just above basement at widely separated drill sites in the eastern equatorial Pacific, including three sites of Leg 16 of the Deep Sea Drilling Project. These sediments were probably formed when the basement was at the crest of this rise and have moved to their present location as a result of sea-floor spreading.