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We have investigated the organization, on the plasma membrane and in detergent-insoluble membrane vesicles, of two neuronal glycosylphosphatidylinositol-anchored (GPI) proteins: Thy-1, a negative regulator of transmembrane signalling; and prion protein, whose rapid endocytosis and Cu(2+) binding suggest that it functions in metal ion uptake. Prion protein(More)
Cellular topography within the highly polarized surface epithelia can be used to identify the location of the stem cells. In some instances, this can be quite precise and allows the characteristics of stem cells to be studied. Our current knowledge of the stem cell population in murine epidermis and small intestinal crypts is reviewed. In the epidermis, the(More)
The distribution of Thy-1 in the retina and optic nerve has been examined immunohistochemically, and compared to that of the astrocytic marker glial fibrillary acidic protein. The axons and cell bodies of ganglion cells were found to be Thy-1 positive as were processes within the inner plexiform layer. Transection of the optic nerve in the neonatal rat(More)
The level of expression of normal cellular prion protein, PrP(c) (cellular prion protein), controls both the rate and the route of neuroinvasive infection, from peripheral entry portal to the CNS. Paradoxically, an overview of the distribution of PrP(c) within tissues outside the CNS is lacking. We have used novel antibodies that recognise cellular prion(More)
Expression of the normal cellular form of prion protein is both necessary and rate-limiting in the spread of prion disease, yet its cellular expression in vivo is poorly understood. To optimise immunohistochemical labelling of this protein in mouse brain, we have developed novel antibodies that recognise cellular prion protein in glutaraldehyde-fixed(More)
The glycoprotein Thy-1 is found on the surface of both neurons, and most fibroblasts, in tissue culture of embryonic or neonatal rat nervous tissue. In adult rat nerves, however, we find the antigen restricted in vivo to neurons and their axons (R. Morris, P. Barber, J. Beech, and G. Raisman, 1983, J. Neurocytol., 12, 1017-1039). We show here that this(More)
THY-1, the smallest member of the immunoglobulin superfamily, is a major cell-surface component expressed by several tissues. The protein, carbohydrate and gene structures of this molecule are known, yet its function is not. It is highly expressed in nervous tissue, where it appears on virtually all neurons after the cessation of axonal growth. Here we show(More)
Foetal mouse hippocampal primordia from mice homozygous for the Thy-1.1 allele were transplanted into the hippocampal region of adult histocompatible mice, homozygous for the Thy-1.2 allele. After survival periods of two months to one year the transplants consisted of a discrete tissue mass, well fused with the host, and distinguished from it by an intense(More)
The cell surface glycoprotein, Thy-1, is present on Purkinje cells at birth, so allowing Thy-1 immunohistochemistry to demonstrate the final stage of migration and the transition to dendritic growth of these cells. In the most caudal lobule of the cerebellar cortex of the newborn rat, migrating Purkinje cells are found. These have a prominent process (up to(More)
Embryonic rat hippocampal primordia from class I and class II major histoincompatible donors were transplanted into the hippocampus of adult rat hosts. The allografts were rejected by a specific host immune response, which was identified by reference to events at a histocompatible hippocampal primordial graft (syngeneic to the host) of similar embryonic age(More)