Publications by authors named "Alejandra Martinez-Maldonado"

Neurodegenerative diseases, tauopathies, constitute a serious global health problem. The etiology of these diseases is unclear and an increase in their incidence has been projected in the next 30 years. Therefore, the study of the molecular mechanisms that might stop these neurodegenerative processes is very relevant.

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Efforts have been made to diagnose and predict the course of different neurodegenerative diseases through various imaging techniques. Particularly tauopathies, where the tau polypeptide is a key participant in molecular pathogenesis, have significantly increased their morbidity and mortality in the human population over the years. However, the standard approach to exploring the phenomenon of neurodegeneration in tauopathies has not been directed at understanding the molecular mechanism that causes the aberrant polymeric and fibrillar behavior of the tau protein, which forms neurofibrillary tangles that replace neuronal populations in the hippocampal and cortical regions.

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Article Synopsis
  • Alzheimer's disease (AD) and progressive supranuclear palsy (PSP) are both tauopathies, characterized by abnormal tau protein aggregates; AD features a 1:1 ratio of 4-repeat to 3-repeat tau isoforms, while PSP shows a predominance of the 4-repeat isoform.
  • The study aimed to compare how pathological tau is processed in PSP compared to AD, utilizing double and triple immunofluorescent labeling techniques analyzed through confocal microscopy.
  • Results indicated that phosphorylated tau was similarly abundant in both conditions, but PSP had unique tau truncation patterns and extracellular NFTs that could lead to the identification of distinct biomarkers for differentiating AD from PSP.
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It has been reported that the main function of tau protein is to stabilize microtubules and promote the movement of organelles through the axon in neurons. In Alzheimer's disease, tau protein is the major constituent of the paired helical filament, and it undergoes post-translational modifications including hyperphosphorylation and truncation. Whether other functions of tau protein are involved in Alzheimer's disease is less clear.

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Among the most frequent nosocomial infections associated with polyresistant bacteria and with a worse prognosis, are those produced by Pseudomonas aeruginosa. This bacterium has a high capacity to adapt to adverse conditions such as pH and osmolarity of urine. Pseudomonas aeruginosa is one of the main pathogens involved in nosocomial infections and immunosuppressed patients.

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Aging-related tau astrogliopathy (ARTAG) is defined by the presence of two types of tau-bearing astrocytes: thorn-shaped astrocytes (TSAs) and granular/fuzzy astrocytes in the brain of old-aged individuals. The present study is focused on TSAs in rare forms of ARTAG with no neuronal tau pathology or restricted to entorhinal and transentorhinal cortices, to avoid bias from associated tauopathies. TSAs show 4Rtau phosphorylation at several specific sites and abnormal tau conformation, but they lack ubiquitin and they are not immunostained with tau-C3 antibodies which recognize truncated tau at Asp421.

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