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    Wyświetlanie 1-3 z 3
    Tytuł:
    Alzheimers disease: Its origin at the membrane, evidence and questions.
    Autorzy:
    Buchet, Rene
    Pikuła, Sławomir
    Powiązania:
    https://bibliotekanauki.pl/articles/1044315.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    β-amyloid precursor protein
    membrane proteases
    Alzheimer's disease
    lipid composition
    membrane microdomains
    Opis:
    Numerous results on membrane lipid composition from different regions of autopsied Alzheimer's disease brains in comparison with corresponding fractions isolated from control brains revealed significant differences in serine- and ethanolamine-containing glycerophospholipid as well as in glycosphingolipid content. Changes in membrane lipid composition are frequently accompanied by alterations in membrane fluidity, hydrophobic mismatch, lipid signaling pathways, transient formation and disappearance of lipid microdomains, changes in membrane permeability to cations and variations of other membrane properties. In this review we focus on possible implications of altered membrane composition on β-amyloid precursor protein (APP) and on proteolysis of APP leading eventually to the formation of neurotoxic β-amyloid (Aβ) peptides, the major proteinaceous component of extracellular senile plaques, directly involved in Alzheimer's disease pathogenesis.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 3; 725-733
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Genetic study of familial cases of Alzheimers disease.
    Autorzy:
    Kowalska, Anna
    Pruchnik-Wolińska, Danuta
    Florczak, Jolanta
    Modestowicz, Renata
    Szczech, Józef
    Kozubski, Wojciech
    Rossa, Grzegorz
    Wender, Mieczysław
    Powiązania:
    https://bibliotekanauki.pl/articles/1043353.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    neurodegeneration
    dementia
    presenilin 1 gene
    amyloid precursor protein gene
    Alzheimer's disease
    mutation
    presenilin 2 gene
    Opis:
    A small number (1-5%) of Alzheimer's disease (AD) cases associated with the early-onset form of the disease (EOAD) appears to be transmitted as a pure genetic, autosomal dominant trait. To date, three genes responsible for familial EOAD have been identified in the human genome: amyloid precursor protein (APP), presenilin 1 (PS1), and presenilin 2 (PS2). Mutations in these genes account for a significant fraction (18 to 50%) of familial cases of early onset AD. The mutations affect APP processing causing increased production of the toxic Aβ42 peptide. According to the "amyloid cascade hypothesis", aggregation of the Aβ42 peptide in brain is a primary event in AD pathogenesis. In our study of twenty AD patients with a positive family history of dementia, 15% (3 of 20) of the cases could be explained by coding sequence mutations in the PS1 gene. Although a frequency of PS1 mutations is less than 2% in the whole population of AD patients, their detection has a significant diagnostic value for both genetic counseling and treatment in families with AD.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 1; 245-242
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Chromatin acetylation, β-amyloid precursor protein and its binding partner FE65 in DNA double strand break repair
    Autorzy:
    Szumiel, Irena
    Foray, Nicolas
    Powiązania:
    https://bibliotekanauki.pl/articles/1039940.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    chromatin acetylation
    FE65
    MOF acetyltransferase
    DNA double strand break repair
    β-amyloid precursor protein
    Tip60 histone acetyltransferase
    heterochromatin protein 1
    Opis:
    Among post-translational modifications of chromatin proteins taking place in DNA double strand break (DSB) repair, acetylation plays a prominent role. This review lists several facts and hypotheses concerning this process. Lack of acetyltransferase TIP60 (HIV-Tat interacting protein of 60 kDa) activity results in cells with defective DSB repair. The enzyme is present in the nucleus in a multimeric protein complex. TIP60 dependent activation of ATM (ataxia telangiectasia mutated kinase) is an early event in the response to DNA breakage. Other important acetylations are those of histones H4 and γH2AX. Correct reconstruction of the damaged site is critical for survival and prevention of genetic and epigenetic changes in the cell that may affect the function of its daughter cells. Recently, two proteins with previously unsuspected functions in DSB repair have been identified as active in this process: Alzheimer β-amyloid precursor protein (APP) and its binding partner FE65, β-amyloid precursor binding protein. Their participation in DSB repair in both neuronal and non-neuronal cells is related to acetylation carried out by the acetyltransferase complex. The same function is ascribed to heterochromatin protein 1 (HP1). So far, the relations (if any) between TIP60 activation by HP1 and by the FE65 complex remain unidentified.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 1; 11-18
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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