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MechanismB2 receptor antagonists |
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Active Indication- |
Inactive Indication- |
Drug Highest PhasePreclinical |
First Approval Ctry. / Loc.- |
First Approval Date- |
100 Clinical Results associated with Scios Nova, Inc.
0 Patents (Medical) associated with Scios Nova, Inc.
01 Jan 1997·Alzheimer Disease
β-App-751 Transgenic Mice: Deficits in Learning and Memory
Author: Barbara Cordell ; Paula M. Moran ; Paul C. Moser ; Linda S. Higgins
While the etiology of Alzheimer’s disease (AD) is unknown, one of the primary histopathological features of the disease is the accumulation in brain of extracellular deposits of the peptide s-amyloid (s-A4). This peptide is produced by the proteolytic processing of the larger precursor protein s-amyloid precursor protein (s-APP).
01 Aug 1996·The American journal of pathologyQ2 · MEDICINE
P3 beta-amyloid peptide has a unique and potentially pathogenic immunohistochemical profile in Alzheimer's disease brain.
Q2 · MEDICINE
Article
Author: Higgins, L S ; Murphy, G M ; Cordell, B ; Catalano, R ; Forno, L S
The presence of beta-amyloid in brain tissue is characteristic of Alzheimer's disease (AD). A naturally occurring derivative of the beta-amyloid peptide, p3, possesses all of the structural determinants required for fibril assembly and neurotoxicity. p3-specific antibodies were used to examine the distribution of this peptide in brain. p3 reactivity was absent or sparse in aged non-AD brains but was prevalent in selected areas of AD brain in diffuse deposits and in a subset of dystrophic neurites. p3-reactive dystrophic neurites were found both independent in the neuropil and associated with plaques. Little or no reactivity was observed to amyloid cores in classical plaques or to amyloid in the cerebral vasculature. The exclusive appearance of p3 reactivity in AD brain plus the selective localization of p3 reactivity to abnormal structures in the temporal lobe limbic system suggests that p3 may be a contributing factor to AD pathology.
01 Jan 1996·The Journal of pharmacology and experimental therapeutics
Novel anti-inflammatory compounds prevent CD11b/CD18, alpha M beta 2 (Mac-1)-dependent neutrophil adhesion without blocking activation-induced changes in Mac-1.
Article
Author: Feng, Y ; Perumattam, J ; Bryant, C M ; Endemann, G ; Hamilton, G S ; Mewshaw, R E ; Liu, D Y
Leumedins are small organic molecules with anti-inflammatory properties in vivo. We report here that leumedins inhibit the CD11b/CD18 alpha M beta 2 (Mac-1)-dependent adherence of neutrophils to serum proteins. The activation of neutrophils leading to adherence via Mac-1 is associated with an increase in cell surface Mac-1 level, and with an increased affinity of Mac-1 for adhesion partners. Inhibition of neutrophil adherence by leumedins does not require blocking the recruitment of Mac-1 from intracellular granules to the cell surface. Furthermore, leumedins do not block the expression on Mac-1 of the epitope for an "activation-specific" antibody (CBRM1/5). Time course studies show that leumedins inhibit adherence by targeting an event which occurs concurrently with changes in Mac-1 level and induction of the CBRM1/5 epitope. Therefore, leumedins block an unknown process which is permissive for Mac-1-dependent adherence.
100 Deals associated with Scios Nova, Inc.
100 Translational Medicine associated with Scios Nova, Inc.