Porcine IPEC-J2 intestinal epithelial cells in microbiological investigations
IPEC-J2 cells are porcine intestinal columnar epithelial cells that were isolated from
neonatal piglet mid-jejunum. This cell line forms polarized monolayers with high …
neonatal piglet mid-jejunum. This cell line forms polarized monolayers with high …
The function of the cellular prion protein in health and disease
The essential role of the cellular prion protein (PrP C) in prion disorders such as Creutzfeldt–
Jakob disease is well documented. Moreover, evidence is accumulating that PrP C may act …
Jakob disease is well documented. Moreover, evidence is accumulating that PrP C may act …
Improvement of neuronal cell survival by astrocyte‐derived exosomes under hypoxic and ischemic conditions depends on prion protein
K Guitart, G Loers, F Buck, U Bork, M Schachner… - Glia, 2016 - Wiley Online Library
Prion protein (PrP) protects neural cells against oxidative stress, hypoxia, ischemia, and
hypoglycemia. In the present study we confirm that cultured PrP‐deficient neurons are more …
hypoglycemia. In the present study we confirm that cultured PrP‐deficient neurons are more …
Current evidence on the transmissibility of chronic wasting disease prions to humans—a systematic review
L Waddell, J Greig, M Mascarenhas… - Transboundary and …, 2018 - Wiley Online Library
A number of prion diseases affect humans, including Creutzfeldt–Jakob disease; most of
these are due to genetic mutations in the affected individual and occur sporadically, but …
these are due to genetic mutations in the affected individual and occur sporadically, but …
Overexpression of PrPc, combined with MGr1‐Ag/37LRP, is predictive of poor prognosis in gastric cancer
L Zhou, Y Shang, C Liu, J Li, H Hu… - … journal of cancer, 2014 - Wiley Online Library
Prion protein (PrPc) has been previously reported to be involved in gastric cancer (GC)
development and progression. However, the association between expression of PrPc and …
development and progression. However, the association between expression of PrPc and …
Emerging roles of the cellular prion protein (PrPC) and 37/67 kDa laminin receptor (RPSA) interaction in cancer biology
A Limone, V Maggisano, D Sarnataro… - Cellular and Molecular …, 2023 - Springer
The cellular prion protein (PrPC) is well-known for its involvement, under its pathogenic
protease-resistant form (PrPSc), in a group of neurodegenerative diseases, known as prion …
protease-resistant form (PrPSc), in a group of neurodegenerative diseases, known as prion …
Proteomics approach to identify the interacting partners of cellular prion protein and characterization of Rab7a interaction in neuronal cells
S Zafar, N von Ahsen, M Oellerich, I Zerr… - Journal of proteome …, 2011 - ACS Publications
The present study was undertaken to identify proteins interacting with PrPC that could
provide new insights into its physiological functions and pathological role. Human PrPC was …
provide new insights into its physiological functions and pathological role. Human PrPC was …
LRP/LR Antibody Mediated Rescuing of Amyloid-β-Induced Cytotoxicity is Dependent on PrP c in Alzheimer's Disease
EC Pinnock, K Jovanovic, MG Pinto… - Journal of …, 2016 - content.iospress.com
The neuronal perturbations in Alzheimer's disease are attributed to the formation of
extracellular amyloid-β (Aβ) neuritic plaques, composed predominantly of the neurotoxic Aβ …
extracellular amyloid-β (Aβ) neuritic plaques, composed predominantly of the neurotoxic Aβ …
Recent advances in the function of the 67 kDa laminin receptor and its targeting for personalized therapy in cancer
A Pesapane, P Ragno, C Selleri… - Current pharmaceutical …, 2017 - ingentaconnect.com
The 67 kDa high affinity laminin receptor (67LR) is a non-integrin cell surface receptor for
laminin, the major component of basement membranes. Interactions between 67LR and …
laminin, the major component of basement membranes. Interactions between 67LR and …
The 37/67kDa laminin receptor (LR) inhibitor, NSC47924, affects 37/67kDa LR cell surface localization and interaction with the cellular prion protein
Abstract The 37/67 kDa laminin receptor (LR) is a non-integrin protein, which binds both
laminin-1 of the extracellular matrix and prion proteins, that hold a central role in prion …
laminin-1 of the extracellular matrix and prion proteins, that hold a central role in prion …