Serum-affine components have been detected in the sera of healthy donors and patients with diabetes mellitus. Human serum has been ascertained to contain insulin-binding component. The latter has not been shown to be immunoglobulin, i.e. it contains no insulin-specific antibodies. The experimental findings suggest that there are human serum proteins that are involved in the transport of insulin.
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ACS Omega
September 2024
Department of Chemical Engineering, Auburn University, Auburn, Alabama 36849, United States.
Developing a continuous insulin-monitoring biosensor is of great importance for both the cellular biomanufacturing industry and for treating diabetes mellitus. Such a sensor needs to be able to effectively monitor insulin across a range of temperatures and pHs and with varying concentrations of competing analytes. One of the two main components of any biosensor is the recognition element, which is responsible for interacting with the molecule of interest.
View Article and Find Full Text PDFMol Pharm
April 2019
Department of Chemistry , University of Kansas, 1251 Wescoe Hall Drive , Lawrence , Kansas 66045 , United States.
Autoimmune diseases are believed to be highly dependent on loss of immune tolerance to self-antigens. Currently, no treatments have been successful clinically in inducing autoantigen-specific tolerance, including efforts to utilize antigen-specific immunotherapy (ASIT) to selectively correct the aberrant autoimmunity. Soluble antigen arrays (SAgAs) represent a novel autoantigen delivery system composed of a linear polymer, hyaluronic acid (HA), displaying multiple copies of conjugated autoantigen.
View Article and Find Full Text PDFMol Pharmacol
July 2018
Department of Pharmacology and Nutritional Sciences, Markey Cancer Center, University of Kentucky College of Medicine, Lexington, Kentucky
The insulin receptor (IR) is a ligand-activated receptor tyrosine kinase that has a key role in metabolism, cellular survival, and proliferation. Progesterone receptor membrane component 1 (PGRMC1) promotes cellular signaling via receptor trafficking and is essential for some elements of tumor growth and metastasis. In the present study, we demonstrate that PGRMC1 coprecipitates with IR.
View Article and Find Full Text PDFDrug Discov Today
July 2017
Department of Structural Biology, University of Pittsburgh, Pittsburgh, PA 15260, USA; Division of Metabolic and Vascular Health & Systems, Medical School, University of Warwick, Coventry CV4 7AL, UK. Electronic address:
Recently, major progress has been made in uncovering the mechanisms of how insulin engages its receptor and modulates downstream signal transduction. Here, we present in detail the current structural knowledge surrounding the individual components of the complex, binding sites, and dynamics during the activation process. A novel kinase triggering mechanism, the 'bow-arrow model', is proposed based on current knowledge and computational simulations of this system, in which insulin, after its initial interaction with binding site 1, engages with site 2 between the fibronectin type III (FnIII)-1 and -2 domains, which changes the conformation of FnIII-3 and eventually translates into structural changes across the membrane.
View Article and Find Full Text PDFJ Biomol Struct Dyn
March 2017
a Institute of Health and Biomedical Innovation , Queensland University of Technology, Brisbane , Australia.
The insulin receptor (IR) plays critical roles in metabolism and growth, directed by the binding of insulin. Decades of research to understand the mechanism of insulin binding and activation of the IR have identified a region of the receptor, the C-terminal (CT) peptide, to be crucial for insulin binding. In particular, a truncated IR consisting of the first three domains fused to the CT peptide was found to bind insulin with nanomolar affinity, with undetectable binding in the absence of fused or soluble CT peptide.
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