| pubmed-article:2127306 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2127306 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
| pubmed-article:2127306 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:2127306 | lifeskim:mentions | umls-concept:C0027877 | lld:lifeskim |
| pubmed-article:2127306 | lifeskim:mentions | umls-concept:C0085151 | lld:lifeskim |
| pubmed-article:2127306 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:2127306 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:2127306 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2127306 | pubmed:dateCreated | 1991-4-9 | lld:pubmed |
| pubmed-article:2127306 | pubmed:abstractText | Our previous study disclosed strong immunostaining of brain tissue in neuronal ceroid lipofuscinosis (NCL) with antibodies against amyloid beta-protein and the presence of 31-kDa polypeptide in the storage material. In the present study, we investigated the immunoreactivity of the NCL brain tissue with anti-serum (anti-GID) raised against a synthetic peptide, based on the amyloid beta-protein precursor, with the 175-186 amino acid sequence. Immunocytochemistry was performed on autopsy brain material collected from 15 NCL cases, and from 8 age-matched normal controls. The results showed strong immunoreactivity of nerve cells in the NCL cases, which according to densitometry was 5 times more intense than in the control group (P less than 0.0001 by Student's t-test). Western blot analysis revealed that in protein fractions of NCL brain homogenates anti-GID recognized the protein band of 35 kDa. Thus our present and previously performed studies supplied for the first time data pointing to abnormal processing of amyloid beta-protein precursor in NCL. Moreover, the accumulation of both 31- and 35-kDa polypeptides that was demonstrated provides further support for postulated defective protein metabolism in this disorder. | lld:pubmed |
| pubmed-article:2127306 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2127306 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2127306 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2127306 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2127306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2127306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2127306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2127306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2127306 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2127306 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2127306 | pubmed:issn | 0304-3940 | lld:pubmed |
| pubmed-article:2127306 | pubmed:author | pubmed-author:SaitohTT | lld:pubmed |
| pubmed-article:2127306 | pubmed:author | pubmed-author:KidaEE | lld:pubmed |
| pubmed-article:2127306 | pubmed:author | pubmed-author:WisniewskiK... | lld:pubmed |
| pubmed-article:2127306 | pubmed:author | pubmed-author:Gordon-Majsza... | lld:pubmed |
| pubmed-article:2127306 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2127306 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:2127306 | pubmed:volume | 120 | lld:pubmed |
| pubmed-article:2127306 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2127306 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2127306 | pubmed:pagination | 94-6 | lld:pubmed |
| pubmed-article:2127306 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:meshHeading | pubmed-meshheading:2127306-... | lld:pubmed |
| pubmed-article:2127306 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2127306 | pubmed:articleTitle | Altered amyloid beta-protein precursor processing in brains of patients with neuronal ceroid lipofuscinosis. | lld:pubmed |
| pubmed-article:2127306 | pubmed:affiliation | New York State Office of Mental Retardation and Developmental Disabilities, Department of Pathological Neurobiology, Staten Island 10314. | lld:pubmed |
| pubmed-article:2127306 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2127306 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
