Researchers studying the speech of individuals with probable Alzheimer's disease (PAD) report that morphosyntax is preserved relative to lexical aspects of speech. The current study questions whether dividing all errors into only two categories, morphosyntactic and lexical, is warranted, given the theoretical controversies concerning the production and representation of pronouns and closed-class words in particular. Two experiments compare the speech output of 10 individuals with Alzheimer's disease to that of 15 healthy age- and education-matched speakers. Results of the first experiment indicate that the pattern of errors in the speech of participants with mild PAD reflects an across-the-board increase in the same types of errors made by healthy older speakers, including closed-class and morphosyntactic errors. In the second task, participants produced a grammatical sentence from written stimuli consisting of a transitive verb and two nouns. Only adults with Alzheimer's disease had difficulties with this task, producing many more closed-class word errors than did healthy older adults. Three of the participants with PAD produced nearly agrammatic speech in this task. These 3 people did not differ from the rest of the PAD group in age, education, working memory, or degree of semantic impairment. Further, error rates on the two tasks were highly correlated. We conclude that morphosyntax is not preserved in the speech output of individuals with PAD, but is vulnerable to errors along with all aspects of language that must be generated by the speaker. We suggest that these results best support a model of speech production in which all words are represented by semantic and grammatical features, both of which are vulnerable to failures of activation when there is damage or noise in the system as a result of pathology, trauma, or even divided attention.
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http://dx.doi.org/10.1044/1092-4388(2001/085) | DOI Listing |
Langmuir
January 2025
Faculty of Science, Yamagata University, 1-4-12, Kojirakawa, Yamagata 990-8560, Japan.
The aggregation and accumulation of amyloid β 42 (Aβ42) peptides on the surface of brain cells is associated with Alzheimer's disease (AD); however, the underlying molecular mechanisms remain unclear. Herein, we used a unique brain-mimetic open system that continuously flows Aβ42 solution to analyze the initial aggregation and adsorptive nature of Aβ42 at physiological concentrations on the lipid membrane. The open system accelerated the adsorption and dimerization kinetics.
View Article and Find Full Text PDFPLoS One
January 2025
Laboratory of Analytical and Molecular Chemistry, Faculty of Sciences Ben M'Sik, Hassan II University of Casablanca, Casablanca, Morocco.
Cognitive dysfunction in Alzheimer's disease results from a complex interplay of various pathological processes, including the dysregulation of key enzymes such as acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), and monoamine oxidase B (MAO-B). This study proposes and designs a series of novel molecules derived from 8-hydroxyquinoline (Azo-8HQ) as potential multi-target lead candidates for treating AD. An exhaustive in silico analysis was conducted, encompassing docking studies, ADMET analysis, density functional theory (DFT) studies, molecular dynamics simulations, and subsequent MM-GBSA calculations to examine the pharmacological potential of these molecules with the specific targets of interest.
View Article and Find Full Text PDFJCI Insight
January 2025
Dianne Hoppes Nunnally Laboratory Research Division, Joslin Diabetes Center, Boston, United States of America.
Background: We aimed to characterize factors associated with the under-studied complication of cognitive decline in aging people with long-duration type 1 diabetes (T1D).
Methods: Joslin "Medalists" (n = 222; T1D ≥ 50 years) underwent cognitive testing. Medalists (n = 52) and age-matched non-diabetic controls (n = 20) underwent neuro- and retinal imaging.
Inflammopharmacology
January 2025
Neuropharmacology Division, Department of Pharmacology, ISF College of Pharmacy, Moga, 142001, Punjab, India.
Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by the accumulation of amyloid-β plaques and tau tangles, leading to cognitive decline and dementia. Insulin-like Growth Factor-1 (IGF-1) is similar in structure to insulin and is crucial for cell growth, differentiation, and regulating oxidative stress, synaptic plasticity, and mitochondrial function. IGF-1 exerts its physiological effects by binding to the IGF-1 receptor (IGF-1R) and activating PI3K/Akt pathway.
View Article and Find Full Text PDFACS Chem Neurosci
January 2025
Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea.
The deposition of amyloid-β (Aβ) aggregates and metal ions within senile plaques is a hallmark of Alzheimer's disease (AD). Among the modifications observed in Aβ peptides, -terminal truncation at Phe4, yielding Aβ, is highly prevalent in AD-affected brains and significantly alters Aβ's metal-binding and aggregation profiles. Despite the abundance of Zn(II) in senile plaques, its impact on the aggregation and toxicity of Aβ remains unexplored.
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