ArticleCellular and molecular life sciences : CMLS2012
Transthyretin binds to glucose-regulated proteins and is subjected to endocytosis by the pancreatic β-cell.
Article in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- SnRNA-Seq of Pancreas Revealed the Dysfunction of Endocrine and Exocrine Cells in Transgenic Pigs with Prediabetes.International journal of molecular sciences · 2023Article
- Plasma Transthyretin Levels and Risk of Type 2 Diabetes Mellitus and Impaired Glucose Regulation in a Chinese Population.Nutrients · 2022Article
- Review
- Exploring the Physiological Role of Transthyretin in Glucose Metabolism in the Liver.International journal of molecular sciences · 2021Article
- Article
- A FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes.Scientific reports · 2018Article
- Diagnostic performance enhancement of pancreatic cancer using proteomic multimarker panel.Oncotarget · 2017Article
- Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.Nature structural & molecular biology · 2017Article
- Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic Implications.Frontiers in immunology · 2016Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transthyretin (TTR) is a functional protein in the pancreatic β-cell. It promotes insulin release and protects against β-cell death. We now demonstrate by ligand blotting, adsorption to specific magnetic beads, and surface plasmon resonance that TTR binds to glucose-regulated proteins (Grps)78, 94, and 170, which are members of the endoplasmic reticulum chaperone family, but Grps78 and 94 have also been found at the plasma membrane. The effect of TTR on changes in cytoplasmic free Ca(2+) concentration ([Ca(2+)](i)) was abolished if the cells were treated with either dynasore, a specific inhibitor of dynamin GTPase that blocks clathrin-mediated endocytosis, or an antibody against Grp78, that prevents TTR from binding to Grp78. The conclusion is that TTR binds to Grp78 at the plasma membrane, is internalized into the β-cell via a clathrin-dependent pathway, and that this internalization is necessary for the effects of TTR on β-cell function.
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Registered trials
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