Extractions: Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager ... Request Permissions PubMed PubMed Citation Articles by Kumar, K Articles by Lovell, K. The Veterinary Record, Vol 118, Issue 12, 325-327 Caprine beta-mannosidosis: phenotypic features K Kumar, MZ Jones, JG Cunningham, JA Kelley, and KL Lovell The clinical features of caprine beta-mannosidosis were evaluated in 10 newborn goats, one stillborn goat and one goat fetus. The phenotypic abnormalities observed in all 10 live affected animals included an inability to rise from a recumbent position, moderate to marked intention tremor, eye movements resembling pendular nystagmus, clinical deafness, bilateral Horner's syndrome, carpal contractures, pastern joint hyperextension, thickened skin and to a varying degree, a dome-shaped skull. Subjective evaluation suggested that most animals had a decreased muscle mass. Together, these characteristics represent a common phenotype which is expressed at birth in caprine beta-mannosidosis.
Extractions: Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager ... Request Permissions PubMed PubMed Citation Articles by Barlow, R. Articles by Berrett, S The Veterinary Record, Vol 109, Issue 20, 441-445 Mannosidosis in Aberdeen Angus cattle in Britain RM Barlow, A Mackellar, G Newlands, A Wiseman, and S Berrett Mannosidosis, an inherited and lethal lysosomal storage disease of Aberdeen Angus cattle, was diagnosed on a farm in north-east Scotland. Two affected calves were examined in detail. Both were poorly grown and ataxic, though the intention tremor and aggression considered characteristic of the disease were not recorded. Histological examination revealed typical vacuolation of nerve cells, fixed macrophages and epithelial cells of the viscera. Deficiency of the enzyme alpha mannosidase was demonstrated. The epidemiology of the disorder in Scotland is considered and control methods indicated.
The EyePathologist Disease - M mannosidosis Klintworth, Gordon K. mannosidosis type I - Klintworth, Gordon K. mannosidosis type II - Klintworth, Gordon K. http://www.eyepathologist.com/LIST.ASP?Title=M
Www.nlm.nih.gov/cgi/mesh/2K/MB_cgi?term=Mannosidosis Cancer ResourcesCancer News, Cancer Conferences, Cancer Causes Targeted gene therapy effective in alphamannosidosis. Reuters Health Posting Date March 22, 2005. Last Updated 2005-03-22 165509 -0400 (Reuters Health) http://www.nlm.nih.gov/cgi/mesh/2K/MB_cgi?term=Mannosidosis
Extractions: @import url( http://www.lineages.co.uk/wp-layout.css ); Search: search the entire directory search this category only Top Health Mannosidosis See also: Health: Conditions and Diseases: Nutrition and Metabolism Disorders Health: Conditions and Diseases: Rare Disorders - Information about the organization, its mission and services. Provides support, education and research on Alpha Mannosidosis and other similar disorders.
Extractions: Vol. 143 No. 6, June 1, 1983 Featured Link E-mail Alerts ARTICLE Article Options Send to a Friend Similar articles in this journal Literature Track Add to File Drawer Download to Citation Manager PubMed citation Articles in PubMed by Press OW Dickersin CR Contact me when this article is cited O. W. Press, H. Fingert, I. T. Lott and C. R. Dickersin A case of autoimmune pancytopenia is described in a patient with mannosidosis who developed anti-platelet and anti-neutrophil antibodies and a low haptoglobin level. Bone marrow biopsy and 111InCl3 bone marrow scanning demonstrated hypoplasia of the marrow with a paucity of "storage cells." Pathogenic mechanisms and implications for other inborn errors of metabolism are discussed.
Extractions: Printed on: 09/09/2005 Printable version of http://www.esrf.fr/UsersAndScience/Publications/Highlights/2002/MX/MX7/ Lysosomal -mannosidase (LAM) is a member of the glycosyl hydrolase family GH38. It hydrolyses all known -mannosidic linkages in lysosomes. Lysosomes are cellular particles, which are responsible for the breakdown of cellular end products. They have an internal pH of 4.5 and are thus much more acidic than the rest of the cell. Errors in lysosomal processes lead to a number of inherited lysosomal storage diseases, many of which are very serious. These include -mannosidosis, which is a rare disease in humans, cattle, cats and guinea pig. Lack of LAM activity causes swelling of the lysosomal vacuoles, and apparently leaking of the unhydrolysed sugars from these vacuoles causes the symptoms of the disease; mental retardation, skeletal changes, hearing loss and reduced immunity in humans . Two protein level -mannosidosis mutations have been identified in cattle and six in humans.
Extractions: @import "/Common/template/styles/Menu.css"; Contact Phonebook SiteMap Advanced search Macromolecular Crystallography Structure of the Outer-Membrane Mitochondrial Monoamine Oxidase B Structure of the Electron-transfer Complex of Cytochrome c and Cytochrome ... Macromolecular Crystallography Lysosomal -mannosidase (LAM) is a member of the glycosyl hydrolase family GH38. It hydrolyses all known -mannosidic linkages in lysosomes. Lysosomes are cellular particles, which are responsible for the breakdown of cellular end products. They have an internal pH of 4.5 and are thus much more acidic than the rest of the cell. Errors in lysosomal processes lead to a number of inherited lysosomal storage diseases, many of which are very serious. These include -mannosidosis, which is a rare disease in humans, cattle, cats and guinea pig. Lack of LAM activity causes swelling of the lysosomal vacuoles, and apparently leaking of the unhydrolysed sugars from these vacuoles causes the symptoms of the disease; mental retardation, skeletal changes, hearing loss and reduced immunity in humans . Two protein level -mannosidosis mutations have been identified in cattle and six in humans.
Referenes.html Oligosaccharides accumulated in the bovine betamannosidosis kidney Possible beta-mannosidosis chimera. Altered expression of metabolic perturbations http://www.fukuyama-u.ac.jp/life/bio/biochem/paper3.html
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