Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals.
AuthorsWeksler ME, Relkin N, Turkenich R, LaRusse S, Zhou L, Szabo P
JournalExp Gerontol
PubMed ID12086704
'Active immunization with the human amyloid peptide (Abeta42) or passive immunization with anti-Abeta42 antibodies protects mice that express a mutant human amyloid precursor protein (APP) transgene from cerebral amyloid deposits. If anti-Abeta42 antibodies protect APP-transgenic mice, a model of Alzheimer''s disease (AD), a high titer of anti-Abeta42 antibodies may protect ... More
Sporadic inclusion body myositis correlates with increased expression and cross-linking by transglutaminases 1 and 2.
AuthorsChoi YC, Park GT, Kim TS, Sunwoo IN, Steinert PM, Kim SY,
JournalJ Biol Chem
PubMed ID10722712
'Sporadic inclusion body myositis (SIBM) is characterized by vacuolar degeneration of muscle fibers and intrafiber clusters of paired helical filaments with abnormal amyloid deposition. Because of their potential involvement in other degenerative disorders, we have examined the expression of transglutaminases (TGases) in normal and SIBM tissues. We report that at ... More
Glutamate receptor subunit 3 is modified by site-specific limited proteolysis including cleavage by gamma-secretase.
AuthorsMeyer EL, Strutz N, Gahring LC, Rogers SW,
JournalJ Biol Chem
PubMed ID12700243
'Ionotropic glutamate receptor (GluR) expression and function is regulated through multiple pre- and post-translational mechanisms. We find that limited proteolytic cleavage of GluR3 at two distinct sites generates stable GluR3 short forms that are glycosylated and found in association with other full-length GluRs in the mouse brain and cultured primary ... More
Genetic modulation of soluble Aß rescues cognitive and synaptic impairment in a mouse model of Alzheimer's disease.
An unresolved debate in Alzheimer's disease (AD) is whether amyloid plaques are pathogenic, causing overt physical disruption of neural circuits, or protective, sequestering soluble forms of amyloid-ß (Aß) that initiate synaptic damage and cognitive decline. Few animal models of AD have been capable of isolating the relative contribution made by ... More
Distinct binding sites in the structure of alpha 2-macroglobulin mediate the interaction with beta-amyloid peptide and growth factors.
AuthorsMettenburg JM, Webb DJ, Gonias SL,
JournalJ Biol Chem
PubMed ID11823454
Alpha(2)-macroglobulin (alpha(2)M) and its receptor, low density lipoprotein receptor-related protein (LRP), function together to facilitate the cellular uptake and degradation of beta-amyloid peptide (Abeta). In this study, we demonstrate that Abeta binds selectively to alpha(2)M that has been induced to undergo conformational change by reaction with methylamine. Denatured alpha(2)M subunits, ... More
Amyloid-beta deposition in skeletal muscle of transgenic mice: possible model of inclusion body myopathy.
AuthorsFukuchi K, Pham D, Hart M, Li L, Lindsey JR,
JournalAm J Pathol
PubMed ID9846958
Inclusion body myopathy is a progressive muscle disorder characterized by nuclear and cytoplasmic inclusions and vacuolation of muscle fibers. Affected muscle fibers contain deposits of congophilic amyloid, amyloid-beta immunoreactive filaments, and paired helical filaments, all of which are pathological hallmarks of Alzheimer's disease in brain. Accumulations of amyloid-beta and its ... More
Astroglial connexin immunoreactivity is specifically altered at ß-amyloid plaques in ß-amyloid precursor protein/presenilin1 mice.
AuthorsMei X, Ezan P, Giaume C, Koulakoff A,
JournalNeuroscience
PubMed ID20813165
Activation of astrocytes surrounding amyloid plaques is a hallmark of Alzheimer disease (AD) with consequences yet poorly understood. Astrocytes are characterized by a high level of intercellular communication mediated by two gap-junction forming proteins, connexin-43 and connexin-30. As astroglial connexins (Cxs) are involved in neuronal dysfunctions and death, we have ... More