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Upregulation of ribosome complexes at the blood-brain barrier in Alzheimer's disease patients. | LitMetric

AI Article Synopsis

  • Researchers studied the molecular mechanisms behind Alzheimer's disease (AD) using advanced proteomics to analyze brain capillaries from both AD patients and control donors.
  • They discovered that 28 out of 29 ribosomal proteins were significantly increased in AD brain capillaries, indicating changes in protein synthesis specifically in this region.
  • Additionally, proteins related to protein processing and N-glycosylation were also upregulated in the capillaries, showing a link between ribosome activity and these processes in the context of Alzheimer's disease.

Article Abstract

The cerebrovascular-specific molecular mechanism in Alzheimer's disease (AD) was investigated by employing comprehensive and accurate quantitative proteomics. Highly purified brain capillaries were isolated from cerebral gray and white matter of four AD and three control donors, and examined by SWATH (sequential window acquisition of all theoretical fragment ion spectra) proteomics. Of the 29 ribosomal proteins that were quantified, 28 (RPLP0, RPL4, RPL6, RPL7A, RPL8, RPL10A, RPL11, RPL12, RPL14, RPL15, RPL18, RPL23, RPL27, RPL27A, RPL31, RPL35A, RPS2, RPS3, RPS3A, RPS4X, RPS7, RPS8, RPS14, RPS16, RPS20, RPS24, RPS25, and RPSA) were significantly upregulated in AD patients. This upregulation of ribosomal protein expression occurred only in brain capillaries and not in brain parenchyma. The protein expression of protein processing and N-glycosylation-related proteins in the endoplasmic reticulum (DDOST, STT3A, MOGS, GANAB, RPN1, RPN2, SEC61B, UGGT1, LMAN2, and SSR4) were also upregulated in AD brain capillaries and was correlated with the expression of ribosomal proteins. The findings reported herein indicate that the ribosome complex, the subsequent protein processing and N-glycosylation-related processes are significantly and specifically upregulated in the brain capillaries of AD patients.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9580172PMC
http://dx.doi.org/10.1177/0271678X221111602DOI Listing

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