Publications by authors named "H Feinberg"

Article Synopsis
  • * Dectin-2 activates macrophages during pathogen interaction, while BDCA-2 helps regulate cytokine production in a type of immune cell called plasmacytoid dendritic cells.
  • * Studies using modified versions of these receptors revealed that while the sugar-binding regions have limited direct interactions, they can be stabilized by their neighboring structure, allowing them to effectively cluster and enhance signaling through oligosaccharide binding.
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The number of Americans affected by diabetes continues to increase but the number of endocrinologists with specialty training to treat this population has not kept up with demand. Primary care outpatient visits can also not meet the projected diabetes population demands or the needs for other complex diabetes management issues. Treatments for diabetes including both medications and technologies continue to expand and become more complex.

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The rapid and constant increase in the number of people living with diabetes has outstripped the capacity of specialists to fully address this chronic disease alone. Furthermore, although most people with diabetes are treated in the primary care setting, most primary care providers feel under-prepared and under-resourced to fully address the needs of their patients with diabetes. Addressing this care gap will require a multifaceted approach centering on primary care training in diabetes and its complications.

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The human mannose receptor expressed on macrophages and hepatic endothelial cells scavenges released lysosomal enzymes, glycopeptide fragments of collagen, and pathogenic microorganisms and thus reduces damage following tissue injury. The receptor binds mannose, fucose, or N-acetylglucosamine (GlcNAc) residues on these targets. C-type carbohydrate-recognition domain 4 (CRD4) of the receptor contains the site for Ca-dependent interaction with sugars.

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CD23, the low-affinity IgE receptor found on B lymphocytes and other cells, contains a C-terminal lectin-like domain that resembles C-type carbohydrate-recognition domains (CRDs) found in many glycan-binding receptors. In most mammalian species, the CD23 residues required to form a sugar-binding site are present, although binding of CD23 to IgE does not involve sugars. Solid-phase binding competition assays, glycoprotein blotting experiments, and glycan array analysis employing the lectin-like domains of cow and mouse CD23 demonstrate that they bind to mannose, GlcNAc, glucose, and fucose and to glycoproteins that bear these sugars in nonreducing terminal positions.

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