The Experts below are selected from a list of 42 Experts worldwide ranked by ideXlab platform

C. Sprick - One of the best experts on this subject based on the ideXlab platform.

  • Subcutaneous injection of carbachol enhances Brain Graft-induced recovery of memory-function by circumventing the blood-Brain barrier.
    Behavioural brain research, 1991
    Co-Authors: U. Sprick, C. Sprick
    Abstract:

    After bilateral neurotoxic hippocampectomy adult rats received bilateral fetal suspension Grafts at the lesion sites. Functional efficacy of fetal Grafted tissue was substantially improved by subcutaneous administration of carbachol at a dose of 0.01 mg/kg s.c. The drug caused an almost complete restitution of performance in Grafted animals in a Morris water-maze test. The progress of behavioral recovery was studied over 3 months postoperatively. Grafts of fetal hippocampal neurons alone improved lesion-induced spatial learning deficits to a limited degree. These results suggest that peripheral administration of carbachol may be of use in the treatment of central lesions associated with cognitive impairments, allowing or enhancing the development of Graft-induced amelioration of behavioral deficits. The data also support the view that Grafts of embryonic neural tissue may produce a local opening of the blood-Brain barrier allowing drugs which normally act only peripherally to exert central effects. These central effects are probably limited to the Graft site because the rest of the Brain has a blood-Brain barrier which is still intact.

Martin Jeffrey - One of the best experts on this subject based on the ideXlab platform.

  • Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. PLoS Pathog 6: e1000800
    2010
    Co-Authors: Bruce Chesebro, Brent Race, Kimberly Meade-white, Rachel Lacasse, Richard Race, James Striebel, David Dorward, Gillian Mcgovern, Martin Jeffrey
    Abstract:

    Prion diseases are fatal neurodegenerative diseases of humans and animals characterized by gray matter spongiosis and accumulation of aggregated, misfolded, protease-resistant prion protein (PrPres). PrPres can be deposited in Brain in an amyloid-form and/or non-amyloid form, and is derived from host-encoded protease-sensitive PrP (PrPsen), a protein normally anchored to the plasma membrane by glycosylphosphatidylinositol (GPI). Previously, using heterozygous transgenic mice expressing only anchorless PrP, we found that PrP anchoring to the cell membrane was required for typical clinical scrapie. However, in the present experiments, using homozygous transgenic mice expressing two-fold more anchorless PrP, scrapie infection induced a new fatal disease with unique clinical signs and altered neuropathology, compared to non-transgenic mice expressing only anchored PrP. Brain tissue of transgenic mice had high amounts of infectivity, and histopathology showed dense amyloid PrPres plaque deposits without gray matter spongiosis. In contrast, infected non-transgenic mice had diffuse non-amyloid PrPres deposits with significant gray matter spongiosis. Brain Graft studies suggested that anchored PrPsen expression was required for gray matter spongiosis during prion infection. Furthermore, electron and light microscopic studies in infected transgenic mice demonstrated several pathogenic processes not seen in typical prion disease, including cerebral amyloid angiopathy and ultrastructural alterations in perivascular neuropil. These findings were similar to certain human familial prion diseases as well as to non-prion huma

  • Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring.
    Public Library of Science (PLoS), 2010
    Co-Authors: Bruce Chesebro, Brent Race, Kimberly Meade-white, Rachel Lacasse, Richard Race, James Striebel, David Dorward, Gillian Mcgovern, Mikael Klingeborn, Martin Jeffrey
    Abstract:

    Prion diseases are fatal neurodegenerative diseases of humans and animals characterized by gray matter spongiosis and accumulation of aggregated, misfolded, protease-resistant prion protein (PrPres). PrPres can be deposited in Brain in an amyloid-form and/or non-amyloid form, and is derived from host-encoded protease-sensitive PrP (PrPsen), a protein normally anchored to the plasma membrane by glycosylphosphatidylinositol (GPI). Previously, using heterozygous transgenic mice expressing only anchorless PrP, we found that PrP anchoring to the cell membrane was required for typical clinical scrapie. However, in the present experiments, using homozygous transgenic mice expressing two-fold more anchorless PrP, scrapie infection induced a new fatal disease with unique clinical signs and altered neuropathology, compared to non-transgenic mice expressing only anchored PrP. Brain tissue of transgenic mice had high amounts of infectivity, and histopathology showed dense amyloid PrPres plaque deposits without gray matter spongiosis. In contrast, infected non-transgenic mice had diffuse non-amyloid PrPres deposits with significant gray matter spongiosis. Brain Graft studies suggested that anchored PrPsen expression was required for gray matter spongiosis during prion infection. Furthermore, electron and light microscopic studies in infected transgenic mice demonstrated several pathogenic processes not seen in typical prion disease, including cerebral amyloid angiopathy and ultrastructural alterations in perivascular neuropil. These findings were similar to certain human familial prion diseases as well as to non-prion human neurodegenerative diseases, such as Alzheimer's disease

Werner Risau - One of the best experts on this subject based on the ideXlab platform.

  • Developing Brain cells produce factors capable of inducing the HT7 antigen, a blood-Brain barrier-specific molecule, in chick endothelial cells
    Neuroscience letters, 1996
    Co-Authors: Eiji Ikeda, Ingo Flamme, Werner Risau
    Abstract:

    Homeostasis of the neural microenvironment is maintained by the blood-Brain barrier (BBB). To analyze the molecular mechanisms by which the BBB is induced during embryonic development, we have taken advantage of an in vivo model of BBB induction based on the expression of the HT7 cell surface protein. This protein is a transmembrane glycoprotein of the immunoglobulin superfamily. It is expressed in the chick BBB-forming endothelial cells, but not in peripheral endothelial cells. Here we show that the HT7 protein is induced in vessels which had vascularized a quail embryonic Brain Graft transplanted in the coelomic cavity of chick embryo. The quail Brain Graft was vascularized by both chick and quail-derived vessels. All chick host-derived vessels in the Brain transplant were found to express HT7 while the neighboring chick vessels were negative. We conclude that the invading host endothelial cells differentiated into BBB-forming vessels under the influence of developing quail Brain cells. This model reproduces the BBB induction during development. It may be useful for further approaches to study the molecular mechanisms involved in BBB induction.

U. Sprick - One of the best experts on this subject based on the ideXlab platform.

  • Subcutaneous injection of carbachol enhances Brain Graft-induced recovery of memory-function by circumventing the blood-Brain barrier.
    Behavioural brain research, 1991
    Co-Authors: U. Sprick, C. Sprick
    Abstract:

    After bilateral neurotoxic hippocampectomy adult rats received bilateral fetal suspension Grafts at the lesion sites. Functional efficacy of fetal Grafted tissue was substantially improved by subcutaneous administration of carbachol at a dose of 0.01 mg/kg s.c. The drug caused an almost complete restitution of performance in Grafted animals in a Morris water-maze test. The progress of behavioral recovery was studied over 3 months postoperatively. Grafts of fetal hippocampal neurons alone improved lesion-induced spatial learning deficits to a limited degree. These results suggest that peripheral administration of carbachol may be of use in the treatment of central lesions associated with cognitive impairments, allowing or enhancing the development of Graft-induced amelioration of behavioral deficits. The data also support the view that Grafts of embryonic neural tissue may produce a local opening of the blood-Brain barrier allowing drugs which normally act only peripherally to exert central effects. These central effects are probably limited to the Graft site because the rest of the Brain has a blood-Brain barrier which is still intact.

Bruce Chesebro - One of the best experts on this subject based on the ideXlab platform.

  • Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. PLoS Pathog 6: e1000800
    2010
    Co-Authors: Bruce Chesebro, Brent Race, Kimberly Meade-white, Rachel Lacasse, Richard Race, James Striebel, David Dorward, Gillian Mcgovern, Martin Jeffrey
    Abstract:

    Prion diseases are fatal neurodegenerative diseases of humans and animals characterized by gray matter spongiosis and accumulation of aggregated, misfolded, protease-resistant prion protein (PrPres). PrPres can be deposited in Brain in an amyloid-form and/or non-amyloid form, and is derived from host-encoded protease-sensitive PrP (PrPsen), a protein normally anchored to the plasma membrane by glycosylphosphatidylinositol (GPI). Previously, using heterozygous transgenic mice expressing only anchorless PrP, we found that PrP anchoring to the cell membrane was required for typical clinical scrapie. However, in the present experiments, using homozygous transgenic mice expressing two-fold more anchorless PrP, scrapie infection induced a new fatal disease with unique clinical signs and altered neuropathology, compared to non-transgenic mice expressing only anchored PrP. Brain tissue of transgenic mice had high amounts of infectivity, and histopathology showed dense amyloid PrPres plaque deposits without gray matter spongiosis. In contrast, infected non-transgenic mice had diffuse non-amyloid PrPres deposits with significant gray matter spongiosis. Brain Graft studies suggested that anchored PrPsen expression was required for gray matter spongiosis during prion infection. Furthermore, electron and light microscopic studies in infected transgenic mice demonstrated several pathogenic processes not seen in typical prion disease, including cerebral amyloid angiopathy and ultrastructural alterations in perivascular neuropil. These findings were similar to certain human familial prion diseases as well as to non-prion huma

  • Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring.
    Public Library of Science (PLoS), 2010
    Co-Authors: Bruce Chesebro, Brent Race, Kimberly Meade-white, Rachel Lacasse, Richard Race, James Striebel, David Dorward, Gillian Mcgovern, Mikael Klingeborn, Martin Jeffrey
    Abstract:

    Prion diseases are fatal neurodegenerative diseases of humans and animals characterized by gray matter spongiosis and accumulation of aggregated, misfolded, protease-resistant prion protein (PrPres). PrPres can be deposited in Brain in an amyloid-form and/or non-amyloid form, and is derived from host-encoded protease-sensitive PrP (PrPsen), a protein normally anchored to the plasma membrane by glycosylphosphatidylinositol (GPI). Previously, using heterozygous transgenic mice expressing only anchorless PrP, we found that PrP anchoring to the cell membrane was required for typical clinical scrapie. However, in the present experiments, using homozygous transgenic mice expressing two-fold more anchorless PrP, scrapie infection induced a new fatal disease with unique clinical signs and altered neuropathology, compared to non-transgenic mice expressing only anchored PrP. Brain tissue of transgenic mice had high amounts of infectivity, and histopathology showed dense amyloid PrPres plaque deposits without gray matter spongiosis. In contrast, infected non-transgenic mice had diffuse non-amyloid PrPres deposits with significant gray matter spongiosis. Brain Graft studies suggested that anchored PrPsen expression was required for gray matter spongiosis during prion infection. Furthermore, electron and light microscopic studies in infected transgenic mice demonstrated several pathogenic processes not seen in typical prion disease, including cerebral amyloid angiopathy and ultrastructural alterations in perivascular neuropil. These findings were similar to certain human familial prion diseases as well as to non-prion human neurodegenerative diseases, such as Alzheimer's disease