The Chromogranins

Kb, Helle

doi:10.1007/0-306-46837-9_1

Cited by 23 publications

(6 citation statements)

References 122 publications

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“…In these DCGs, secretory proteins, such as catecholamines in adrenal chromaffin granules, are highly condensed and can reach levels of 0.5-1.0 mM [8]. Chromogranin A (CgA) in DCGs represents up to 50% of the soluble protein content of adrenal chromaffin granules at concentrations reaching 2 mM [9-11]. The condensation process is part of the biogenesis of secretory granules and requires the coordination of several granin family members, including CgA, chromogranin B (CgB), secretogranin II (SgII or Scg2) and Scg3 [6, 12].…”

Section: The Granin Familymentioning

confidence: 99%

Secretogranin III: a diabetic retinopathy-selective angiogenic factor

Webster

LeBlanc

et al. 2017

Cell. Mol. Life Sci.

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Secretogranin III (Scg3) is a member of the granin protein family that regulates the biogenesis of secretory granules. Scg3 was recently discovered as an angiogenic factor, expanding its functional role to extrinsic regulation. Unlike many other known angiogenic factors, the pro-angiogenic actions of Scg3 are restricted to pathological conditions. Among thousands of quantified endothelial ligands, Scg3 has the highest binding activity ratio to diabetic vs. healthy mouse retinas and lowest background binding to normal vessels. In contrast, vascular endothelial growth factor binds to and stimulates angiogenesis of both diabetic and control vasculature. Consistent with its role in pathological angiogenesis, Scg3-neutralizing antibodies alleviate retinal vascular leakage in mouse models of diabetic retinopathy and retinal neovascularization in oxygen-induced retinopathy mice. This review summarizes our current knowledge of Scg3 as a regulatory protein of secretory granules, highlights its new role as a highly disease-selective angiogenic factor, and envisions Scg3 inhibitors as "selective angiogenesis blockers" for targeted therapy.

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Section: The Granin Familymentioning

confidence: 99%

Secretogranin III: a diabetic retinopathy-selective angiogenic factor

Webster

LeBlanc

et al. 2017

Cell. Mol. Life Sci.

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“…Our understanding of granule protein sorting, either in the Golgi (sorting by entry) or in the immature granule (sorting by retention), in both healthy and disease contexts is limited, in part, because the regulatory mechanisms are not well defined (Dikeakos and Reudelhuber, 2007;Arvan and Castle, 1998;Chung et al, 1989). Aside from (pro)insulin, the most abundant proteins in the granule lumen are granin proteins, including chromogranin A (CgA, also known as CHGA), chromogranin B (CgB, also known as CHGB) and VGF (non-acronymic, unrelated to VEGF) (Helle, 2000;Bartolomucci et al, 2011;Suckale and Solimena, 2010). Granin proteins have been proposed to stimulate granulogenesis by clustering at trans-Golgi network (TGN) subdomains through direct and indirect associations with cholesterol-rich lipid rafts (Hosaka et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Chromogranin B regulates early-stage insulin granule trafficking from the Golgi in pancreatic islet β-cells

Bearrows

Bauchle

Becker

et al. 2019

Journal of Cell Science

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Chromogranin B (CgB, also known as CHGB) is abundantly expressed in dense core secretory granules of multiple endocrine tissues and has been suggested to regulate granule biogenesis in some cell types, including the pancreatic islet β-cell, though the mechanisms are poorly understood. Here, we demonstrate a critical role for CgB in regulating secretory granule trafficking in the β-cell. Loss of CgB impairs glucosestimulated insulin secretion, impedes proinsulin processing to yield increased proinsulin content, and alters the density of insulin-containing granules. Using an in situ fluorescent pulse-chase strategy to track nascent proinsulin, we show that loss of CgB impairs Golgi budding of proinsulin-containing secretory granules, resulting in a substantial delay in trafficking of nascent granules to the plasma membrane with an overall decrease in total plasma membrane-associated granules. These studies demonstrate that CgB is necessary for efficient trafficking of secretory proteins into the budding granule, which impacts the availability of insulin-containing secretory granules for exocytic release. This article has an associated First Person interview with the first author of the paper.

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“…In contrast, a negative selection mechanism called “sorting by retention” involves aggregation of proteins in the granule lumen to promote cargo retention during retrieval of proteins from ISGs not destined for regulated secretion (Arvan and Castle, 1998). Much attention has been paid to the granin proteins, chromogranin A (CgA) and chromogranin B (CgB), as key determinants of granule biogenesis, in part because these proteins comprise a major component of the secretory granule in multiple endocrine and neuroendocrine cell types (Helle, 2000). CgA has been suggested to play a key regulatory role in granule formation in some cell types (Kim et al, 2001, Kim et al, 2002), but its potential role in the islet β-cell is not well defined.…”

Section: Introductionmentioning

confidence: 99%

The Prohormone VGF Regulates β Cell Function via Insulin Secretory Granule Biogenesis

et al. 2017

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Summary The prohormone VGF is expressed in neuroendocrine and endocrine tissues and regulates nutrient and energy status both centrally and peripherally. We and others have shown that VGF-derived peptides have direct action on the islet β-cell as secretagogues and cytoprotective agents; however the endogenous function of VGF in the β-cell has not been described. Here we demonstrate that VGF regulates secretory granule formation. VGF loss of function studies in both isolated islets and conditional knockout mice reveal a profound decrease in stimulus-coupled insulin secretion. Moreover, VGF is necessary to facilitate efficient exit of granule cargo from the trans-Golgi network and proinsulin processing. It also functions to replenish insulin granule stores following nutrient stimulation. Our data support a model in which VGF operates at a critical node of granule biogenesis in the islet β-cell to coordinate insulin biosynthesis with β-cell secretory capacity.

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The Chromogranins

Cited by 23 publications

References 122 publications

Secretogranin III: a diabetic retinopathy-selective angiogenic factor

Secretogranin III: a diabetic retinopathy-selective angiogenic factor

Chromogranin B regulates early-stage insulin granule trafficking from the Golgi in pancreatic islet β-cells

The Prohormone VGF Regulates β Cell Function via Insulin Secretory Granule Biogenesis

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