Affiliations 

  • 1 College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, UK
  • 2 School of Health Sciences and Technology, University of Petroleum and Energy Studies, Bidholi, Dehradun, India. tapanbehl31@gmail.com
  • 3 Department of Pharmaceutics, Faculty of Pharmacy, Sree Balaji Medical College and Hospital, Chromepet, Chennai, Tamil Nadu, India
  • 4 Faculty of Pharmacy, Sree Balaji Medical College and Hospital Campus, Bharath Institute of Higher Education and Research, Chennai, Tamil Nadu, India
  • 5 Department of Pharmaceutical Chemistry, JKKMMRFs-Amnai JKK Sampoorani Ammal College of Pharmacy, Komarapalayam, Tamil Nadu, India
  • 6 Faculty of Pharmaceutical Sciences, DAV University, Jalandhar, Punjab, India
  • 7 School of Pharmaceutical Sciences, Department of Pharmaceutical Sciences, Chhatrapti Shahu Ji Maharaj University, Uttar Pradesh, Kanpur, India
  • 8 Department of Pharmaceutics, College of Pharmacy, Prince Sattam Bin Abdulaziz University, Alkharj, Saudi Arabia
  • 9 Faculty of Pharmacy, AIMST University, Bedong, Kedah, Malaysia
  • 10 GHG Khalsa College of Pharmacy, Gurusar Sadhar, Punjab, India
  • 11 School of Pharmaceutical Sciences, Lovely Professional University, Phagwara, Punjab, 1444411, India
  • 12 Department of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, Qassim University, Buraydah, 52571, Kingdom of Saudi Arabia. S.Chigurupati@qu.edu.sa
Neurotox Res, 2023 Oct 17.
PMID: 37847429 DOI: 10.1007/s12640-023-00670-3

Abstract

Alzheimer's disease contributes to 60-70% of all dementia cases in the general population. Belonging to the BIN1/amphiphysin/RVS167 (BAR) superfamily, the bridging integrator (BIN1) has been identified to impact two major pathological hallmarks in Alzheimer's disease (AD), i.e., amyloid beta (Aβ) and tau accumulation. Aβ accumulation is found to increase by BIN1 knockdown in cortical neurons in late-onset AD, due to BACE1 accumulation at enlarged early endosomes. Two BIN1 mutants, KR and PL, were identified to exhibit Aβ accumulation. Furthermore, BIN1 deficiency by BIN1-related polymorphisms impairs the interaction with tau, thus elevating tau phosphorylation, altering synapse structure and tau function. Even though the precise role of BIN1 in the neuronal tissue needs further investigation, the authors aim to throw light on the potential of BIN1 and unfold its implications on tau and Aβ pathology, to aid AD researchers across the globe to examine BIN1, as an appropriate target gene for disease management.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.