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Journal articles on the topic 'Secretory granula'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

von Zglinicki, Thomas, and Godfried M. Roomans. "X-Ray Microanalysis of the Intestine: Identification of Electrolyte Secreting Cells." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 2 (1990): 342–43. http://dx.doi.org/10.1017/s0424820100135319.

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Frozen dried cryosections of mouse jejunum were investigated. Besides Paneth and Goblet cells, two different types of crypt enterocytes could be distinguished according to clearly different electrolyte concentrations and to the presence (type A) or absence (type B) of small secretion granula in the cytoplasm.Secretion was stimulated by an intraperitoneal injection of either isoproterenol or pilocarpine. In some experiments, isoproterenol stimulation was blocked by alloxan, a potent inhibitor of the adenylate cyclase. Changes of cytoplasmic element concentrations were measured in frozen dried c

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2

Cossu, M., M. S. Lantini, and R. Puxeddu. "Immunocytochemical localization of Lewis blood group antigens in human salivary glands." Journal of Histochemistry & Cytochemistry 42, no. 8 (1994): 1135–42. http://dx.doi.org/10.1177/42.8.8027532.

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We demonstrated the immunohistochemical distribution of Le-a and Le-b blood group antigens in human major and minor salivary glands at the ultrastructural level by applying a post-embedding immunogold staining method. In secretors' glands, a faint Le-a reactivity was found only in mucous droplets, whereas Le-b antigen was intensely stained in secretory granules of most mucous cells, in those of intercalated duct cells, in the pale granular matrix of some serous cells, and, when osmication was omitted, in cytoplasmatic vesicles and cell surfaces of striated ducts. In the submandibular gland of

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3

Skott, O. "Do osmotic forces play a role in renin secretion?" American Journal of Physiology-Renal Physiology 255, no. 1 (1988): F1—F10. http://dx.doi.org/10.1152/ajprenal.1988.255.1.f1.

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Secretory granules swell during exocytosis. Swelling may follow fusion and assist in extrusion of the granular content, or swelling may cause granular fusion with the plasmalemma. A granular proton gradient has been suggested to be involved in such preexocytic granular swelling. Exocytosis of renin from juxtaglomerular cells of isolated preparations is very sensitive to changes in the extracellular osmolality. Extracellular hyposmolality causes swelling of secretory granules, fusions between peripherally located granules and plasmalemma, and an increased number of release episodes. Induction o

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4

Barg, Sebastian, Ping Huang, Lena Eliasson, et al. "Priming of insulin granules for exocytosis by granular Cl− uptake and acidification." Journal of Cell Science 114, no. 11 (2001): 2145–54. http://dx.doi.org/10.1242/jcs.114.11.2145.

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ATP-dependent priming of the secretory granules precedes Ca2+-regulated neuroendocrine secretion, but the exact nature of this reaction is not fully established in all secretory cell types. We have further investigated this reaction in the insulin-secreting pancreatic B-cell and demonstrate that granular acidification driven by a V-type H+-ATPase in the granular membrane is a decisive step in priming. This requires simultaneous Cl− uptake through granular ClC-3 Cl− channels. Accordingly, granule acidification and priming are inhibited by agents that prevent transgranular Cl− fluxes, such as 4,

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Kemter, Elisabeth, Andreas Müller, Martin Neukam, et al. "Sequential in vivo labeling of insulin secretory granule pools in INS-SNAP transgenic pigs." Proceedings of the National Academy of Sciences 118, no. 37 (2021): e2107665118. http://dx.doi.org/10.1073/pnas.2107665118.

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β cells produce, store, and secrete insulin upon elevated blood glucose levels. Insulin secretion is a highly regulated process. The probability for insulin secretory granules to undergo fusion with the plasma membrane or being degraded is correlated with their age. However, the molecular features and stimuli connected to this behavior have not yet been fully understood. Furthermore, our understanding of β cell function is mostly derived from studies of ex vivo isolated islets in rodent models. To overcome this translational gap and study insulin secretory granule turnover in vivo, we have gen

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6

Burgoyne, Robert D., and Alan Morgan. "Secretory Granule Exocytosis." Physiological Reviews 83, no. 2 (2003): 581–632. http://dx.doi.org/10.1152/physrev.00031.2002.

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Regulated exocytosis of secretory granules or dense-core granules has been examined in many well-characterized cell types including neurons, neuroendocrine, endocrine, exocrine, and hemopoietic cells and also in other less well-studied cell types. Secretory granule exocytosis occurs through mechanisms with many aspects in common with synaptic vesicle exocytosis and most likely uses the same basic protein components. Despite the widespread expression and conservation of a core exocytotic machinery, many variations occur in the control of secretory granule exocytosis that are related to the spec

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7

Tooze, John. "Secretory granule formation." Cell Biophysics 19, no. 1 (1991): 117–30. http://dx.doi.org/10.1007/bf02989885.

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8

Möhn, H., V. Le Cabec, S. Fischer, and I. Maridonneau-Parini. "The src-family protein-tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation." Biochemical Journal 309, no. 2 (1995): 657–65. http://dx.doi.org/10.1042/bj3090657.

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The src-family protein-tyrosine kinase p59hck is mainly expressed in neutrophils; however, its functional role in these cells is unknown. Several other src-family members are localized on secretory vesicles and have been proposed to regulate intracellular traffic. We have established here the subcellular localization of p59hck in human neutrophils. Immunoblotting of subcellular fractions showed that approx. 60% of the p59hck per cell is localized on the secretory granules; the other 40% is distributed equally between non-granular membranes and the cytosol. Immunofluorescence of neutrophils and

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9

Alvarez de Toledo, G., and J. M. Fernandez. "Patch-clamp measurements reveal multimodal distribution of granule sizes in rat mast cells." Journal of Cell Biology 110, no. 4 (1990): 1033–39. http://dx.doi.org/10.1083/jcb.110.4.1033.

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Using patch-clamp techniques, we have followed the attributes of the secretory granules of peritoneal mast cells obtained from rats of different ages. The granule attributes were determined by following the step increases in the cell surface membrane area caused by the exocytosis of the granules in GTP gamma S stimulated mast cells. Our data show that the amount of granule membrane available for exocytosis depends exponentially on the weight (age) of the donor rat, reaching a maximum at approximately 300 g. The data are consistent with an exponential growth in the number of granules contained

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10

Sano, K., S. Waguri, N. Sato, E. Kominami, and Y. Uchiyama. "Coexistence of renin and cathepsin B in secretory granules of granular duct cells in male mouse submandibular gland." Journal of Histochemistry & Cytochemistry 41, no. 3 (1993): 433–38. http://dx.doi.org/10.1177/41.3.8429206.

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Cathepsin B, a representative lysosomal cysteine proteinase, has been demonstrated to coexist with renin in secretary granules of rat pituitary LH/FSH cells and renal juxtaglomerular cells. We investigated immunocytochemically the localization of cathepsins B, H, and L in the submandibular gland of male mice, in which active renin is also produced. By light microscopy, granular immunodeposits for cathepsin B were detected in epithelial cells of the gland, particularly in granular duct cells and interstitial cells. Immunoreactivity for cathepsins H and L was mainly found in interstitial cells,

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11

Peng Loh, Y., and Taeyoon Kim. "Neuropeptide secretory granule biogenesis." Neuropeptides 40, no. 6 (2006): 426–27. http://dx.doi.org/10.1016/j.npep.2006.09.011.

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12

Hutton, J. C. "The insulin secretory granule." Diabetologia 32, no. 5 (1989): 271–81. http://dx.doi.org/10.1007/bf00265542.

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13

Datta, Yvonne H., Hagop Youssoufian, Peter W. Marks, and Bruce M. Ewenstein. "Targeting of a Heterologous Protein to a Regulated Secretion Pathway in Cultured Endothelial Cells." Blood 94, no. 8 (1999): 2696–703. http://dx.doi.org/10.1182/blood.v94.8.2696.420k29_2696_2703.

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The stimulation of regulated exocytosis in vascular endothelial cells (EC) by a variety of naturally occurring agonists contributes to the interrelated processes of inflammation, thrombosis, and fibrinolysis. The Weibel-Palade body (WPB) is a well-described secretory granule in EC that contains both von Willebrand factor (vWF) and P-selectin, but the mechanisms responsible for the targeting of these proteins into this organelle remain poorly understood. Through adenoviral transduction, we have expressed human growth hormone (GH) as a model of regulated secretory protein sorting in EC. Immunofl

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14

Tooze, S. A., T. Flatmark, J. Tooze, and W. B. Huttner. "Characterization of the immature secretory granule, an intermediate in granule biogenesis." Journal of Cell Biology 115, no. 6 (1991): 1491–503. http://dx.doi.org/10.1083/jcb.115.6.1491.

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The events in the biogenesis of secretory granules after the budding of a dense-cored vesicle from the trans-Golgi network (TGN) were investigated in the neuroendocrine cell line PC12, using sulfate-labeled secretogranin II as a marker. The TGN-derived dense-cored vesicles, which we refer to as immature secretory granules, were found to be obligatory organellar intermediates in the biogenesis of the mature secretory granules which accumulate in the cell. Immature secretory granules were converted to mature secretory granules with a half-time of approximately 45 min. This conversion entailed an

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15

Dahlgren, C., S. R. Carlsson, A. Karlsson, H. Lundqvist, and C. Sjölin. "The lysosomal membrane glycoproteins Lamp-1 and Lamp-2 are present in mobilizable organelles, but are absent from the azurophil granules of human neutrophils." Biochemical Journal 311, no. 2 (1995): 667–74. http://dx.doi.org/10.1042/bj3110667.

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The subcellular localization of two members of a highly glycosylated protein group present in lysosomal membranes in most cells, the lysosome-associated membrane proteins 1 and 2 (Lamp-1 and Lamp-2), was examined in human neutrophil granulocytes. Antibodies that were raised against purified Lamp-1 adn Lamp-2 gave a distinct granular staining of the cytoplasm upon immunostaining of neutrophils. Subcellular fractionation was used to separate the azurophil and specific granules from a light-membrane fraction containing plasma membranes and secretory vesicles, and Western blotting was used to dete

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16

Bonnemaison, Mathilde, Nils Bäck, Yimo Lin, Juan S. Bonifacino, Richard Mains, and Betty Eipper. "AP-1A Controls Secretory Granule Biogenesis and Trafficking of Membrane Secretory Granule Proteins." Traffic 15, no. 10 (2014): 1099–121. http://dx.doi.org/10.1111/tra.12194.

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17

Elias, Peter M., Theodora Mauro, Ulrich Rassner, et al. "The Secretory Granular Cell: The Outermost Granular Cell as a Specialized Secretory Cell." Journal of Investigative Dermatology Symposium Proceedings 3, no. 2 (1998): 87–100. http://dx.doi.org/10.1038/jidsymp.1998.20.

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18

LU, JINLING, NATALIA GUSTAVSSON, QIMING LI, GEORGE K. RADDA, THOMAS C. SÜDHOF, and WEIPING HAN. "GENERATION OF TRANSGENIC MICE FOR IN VIVO DETECTION OF INSULIN-CONTAINING GRANULE EXOCYTOSIS AND QUANTIFICATION OF INSULIN SECRETION." Journal of Innovative Optical Health Sciences 02, no. 04 (2009): 397–405. http://dx.doi.org/10.1142/s1793545809000711.

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Insulin secretion is a complex and highly regulated process. Although much progress has been made in understanding the cellular mechanisms of insulin secretion and regulation, it remains unclear how conclusions from these studies apply to living animals. That few studies have been done to address these issues is largely due to the lack of suitable tools in detecting secretory events at high spatial and temporal resolution in vivo. When combined with genetically encoded biosensor, optical imaging is a powerful tool for visualization of molecular events in vivo. In this study, we generated a DNA

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19

Thévenod, Frank. "Ion channels in secretory granules of the pancreas and their role in exocytosis and release of secretory proteins." American Journal of Physiology-Cell Physiology 283, no. 3 (2002): C651—C672. http://dx.doi.org/10.1152/ajpcell.00600.2001.

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Regulated secretion in exocrine and neuroendocrine cells occurs through exocytosis of secretory granules and the subsequent release of stored small molecules and proteins. The introduction of biophysical techniques with high temporal and spatial resolution, and the identification of Ca2+-dependent and -independent “docking” and “fusion” proteins, has greatly enhanced our understanding of exocytosis. The cloning of families of ion channel proteins, including intracellular ion channels, has also revived interest in the role of secretory granule ion channels in exocytotic secretion. Thus secretor

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20

Tranah, Thomas H., Godhev K. Manakkat Vijay, Jennifer M. Ryan, R. Daniel Abeles, Paul K. Middleton, and Debbie L. Shawcross. "Dysfunctional neutrophil effector organelle mobilization and microbicidal protein release in alcohol-related cirrhosis." American Journal of Physiology-Gastrointestinal and Liver Physiology 313, no. 3 (2017): G203—G211. http://dx.doi.org/10.1152/ajpgi.00112.2016.

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Patients with alcohol-related cirrhosis (ALD) are prone to infection. Circulating neutrophils in ALD are dysfunctional and predict development of sepsis, organ dysfunction, and survival. Neutrophil granules are important effector organelles containing a toxic array of microbicidal proteins, whose controlled release is required to kill microorganisms while minimizing inflammation and damage to host tissue. We investigated the role of these granular responses in contributing to immune disarray in ALD. Neutrophil granular content and mobilization were measured by flow cytometric quantitation of c

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21

Yoshiyuki Osamura, R., M. Chrétien, and M. Marcinkiewicz. "Ultrastructural localization of secretory granule." Pathology - Research and Practice 183, no. 5 (1988): 617–19. http://dx.doi.org/10.1016/s0344-0338(88)80024-4.

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22

Rajagopal, Chitra, Kathryn L. Stone, Victor P. Francone, Richard E. Mains, and Betty A. Eipper. "Secretory Granule to the Nucleus." Journal of Biological Chemistry 284, no. 38 (2009): 25723–34. http://dx.doi.org/10.1074/jbc.m109.035782.

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23

Kim, Taeyoon, Marjorie C. Gondré-Lewis, Irina Arnaoutova, and Y. Peng Loh. "Dense-Core Secretory Granule Biogenesis." Physiology 21, no. 2 (2006): 124–33. http://dx.doi.org/10.1152/physiol.00043.2005.

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The dense-core secretory granule is a key organelle for secretion of hormones and neuropeptides in endocrine cells and neurons, in response to stimulation. Cholesterol and granins are critical for the assembly of these organelles at the trans-Golgi network, and their biogenesis is regulated quantitatively by posttranscriptional and posttranslational mechanisms.

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24

Germanos, Mark, Andy Gao, Matthew Taper, Belinda Yau, and Melkam A. Kebede. "Inside the Insulin Secretory Granule." Metabolites 11, no. 8 (2021): 515. http://dx.doi.org/10.3390/metabo11080515.

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The pancreatic β-cell is purpose-built for the production and secretion of insulin, the only hormone that can remove glucose from the bloodstream. Insulin is kept inside miniature membrane-bound storage compartments known as secretory granules (SGs), and these specialized organelles can readily fuse with the plasma membrane upon cellular stimulation to release insulin. Insulin is synthesized in the endoplasmic reticulum (ER) as a biologically inactive precursor, proinsulin, along with several other proteins that will also become members of the insulin SG. Their coordinated synthesis enables sy

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25

Watson, E. L., D. DiJulio, D. Kauffman, J. Iversen, M. R. Robinovitch, and K. T. Izutsu. "Evidence for G proteins in rat parotid plasma membranes and secretory granule membranes." Biochemical Journal 285, no. 2 (1992): 441–49. http://dx.doi.org/10.1042/bj2850441.

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G proteins were identified in rat parotid plasma membrane-enriched fractions and in two populations of isolated secretory granule membrane fractions. Both [32P]ADP-ribosylation analysis with bacterial toxins and immunoblot analysis with crude and affinity-purified antisera specific for alpha subunits of G proteins were utilized. Pertussis toxin catalysed the ADP-ribosylation of a 41 kDa substrate in the plasma membrane fraction and both secretory granule membrane fractions. Cholera toxin catalysed the ADP-ribosylation of two substrates with molecular masses of 44 kDa and 48 kDa in the plasma m

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Smelova, I. V., E. S. Golovneva, T. G. Kravchenko, and V. I. Petukhova. "On the Regulatory Capabilities of Thyroid Mast Cells in Thiamazole Model of Hypothyroidism and Infrared Laser Exposure." Journal of Ural Medical Academic Science 18, no. 1 (2021): 20–28. http://dx.doi.org/10.22138/2500-0918-2021-18-1-20-28.

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The regulatory effect of mast cells on the state of thyroid gland in hypothyroidism and laser therapy remains unclear. Aim: to study the secretory processes of mast cells in relationship with the indicators of functional activity of thyroid gland. Materials and methods. Experimental groups: (55 rats) 1) intact rats, 2) hypothyroidism (thiamazole 25mg/kg) 3) hypothyroidism and 0.5W laser exposure, 4) hypothyroidism and 2.0W laser exposure. Histological samples of the thyroid gland were removed on the 1, 7, and 30 days. Histological sections were stained with toluidine blue. Morphometric data an

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Johnson, Jennifer L., Jlenia Monfregola, Gennaro Napolitano, William B. Kiosses, and Sergio D. Catz. "Vesicular trafficking through cortical actin during exocytosis is regulated by the Rab27a effector JFC1/Slp1 and the RhoA-GTPase–activating protein Gem-interacting protein." Molecular Biology of the Cell 23, no. 10 (2012): 1902–16. http://dx.doi.org/10.1091/mbc.e11-12-1001.

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Cytoskeleton remodeling is important for the regulation of vesicular transport associated with exocytosis, but a direct association between granular secretory proteins and actin-remodeling molecules has not been shown, and this mechanism remains obscure. Using a proteomic approach, we identified the RhoA-GTPase–activating protein Gem-interacting protein (GMIP) as a factor that associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. GMIP down-regulation induced RhoA activation and actin polymerization. Importantly, GMIP-down-regulated cells showed impaired ves

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Farias, Maria De Fatima Diniz Baptista, and Simone Chinicz Cohen. "Estudos ultraestruturais da glândula de Mehlis de Metamicrocotyla macracantha (Monogenea, Microcotylidae) parasito de Mugil liza (Teleostei)." Brazilian Journal of Veterinary Research and Animal Science 42, no. 5 (2005): 367. http://dx.doi.org/10.11606/issn.1678-4456.bjvras.2005.26413.

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A ultraestrutura da glândula de Mehlis de Metamicrocotyla macracantha, parasita de brânquia coletado de Mugil liza do Rio de Janeiro, Brasil, foi estudado através da microscopia eletrônica de transmissão. A glândula de Mehlis consiste de dois tipos de células secretoras, S1 e S2, cada uma produzindo um corpo secretor diferente. Os corpos S1 são esféricos, em forma de lamelas e observados em diferentes estágios de desenvolvimentos no citoplasma dessas células. Os corpos S2 são esféricos a ovais com conteúdos densos, apresentando uma estrutura cristalina. O citoplasma das células da glândula de

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Beuret, Nicole, Hansruedi Stettler, Anja Renold, Jonas Rutishauser, and Martin Spiess. "Expression of Regulated Secretory Proteins Is Sufficient to Generate Granule-like Structures in Constitutively Secreting Cells." Journal of Biological Chemistry 279, no. 19 (2004): 20242–49. http://dx.doi.org/10.1074/jbc.m310613200.

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The formation of secretory granules and regulated secretion are generally assumed to occur only in specialized endocrine, neuronal, or exocrine cells. We discovered that regulated secretory proteins such as the hormone precursors pro-vasopressin, pro-oxytocin, and pro-opiomelanocortin, as well as the granins secretogranin II and chromogranin B but not the constitutive secretory protein α1-protease inhibitor, accumulate in granular structures at the Golgi and in the cell periphery in transfected COS-1 fibroblast cells. The accumulations were observed in 30–70% of the transfected cells expressin

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Turgeon, J. L., and R. H. Cooper. "Protein kinase C and an endogenous substrate associated with adenohypophyseal secretory granules." Biochemical Journal 237, no. 1 (1986): 53–61. http://dx.doi.org/10.1042/bj2370053.

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Secretory granules isolated from anterior pituitary glands were examined for Ca2+/phospholipid-dependent protein kinase (protein kinase C) activity as well as the occurrence of granule-associated substrate proteins. Sheep adenohypophyses were fractionated by differential and sucrose-density-gradient centrifugation to yield a granule fraction enriched for luteinizing-hormone (lutropin)-containing secretory granules. Marker-enzyme analysis showed no detectable cytosolic contamination, although there were small amounts of plasma membranes (2-4%) and lysosomes (4-6%) associated with the preparatio

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Bruinsma, Stephen, Declan J. James, Melanie Quintana Serrano, et al. "Small molecules that inhibit the late stage of Munc13-4–dependent secretory granule exocytosis in mast cells." Journal of Biological Chemistry 293, no. 21 (2018): 8217–29. http://dx.doi.org/10.1074/jbc.ra117.001547.

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Ca2+-dependent secretory granule fusion with the plasma membrane is the final step for the exocytic release of inflammatory mediators, neuropeptides, and peptide hormones. Secretory cells use a similar protein machinery at late steps in the regulated secretory pathway, employing protein isoforms from the Rab, Sec1/Munc18, Munc13/CAPS, SNARE, and synaptotagmin protein families. However, no small-molecule inhibitors of secretory granule exocytosis that target these proteins are currently available but could have clinical utility. Here we utilized a high-throughput screen of a 25,000-compound lib

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ARVAN, Peter, and David CASTLE. "Sorting and storage during secretory granule biogenesis: looking backward and looking forward." Biochemical Journal 332, no. 3 (1998): 593–610. http://dx.doi.org/10.1042/bj3320593.

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Secretory granules are specialized intracellular organelles that serve as a storage pool for selected secretory products. The exocytosis of secretory granules is markedly amplified under physiologically stimulated conditions. While granules have been recognized as post-Golgi carriers for almost 40 years, the molecular mechanisms involved in their formation from the trans-Golgi network are only beginning to be defined. This review summarizes and evaluates current information about how secretory proteins are thought to be sorted for the regulated secretory pathway and how these activities are po

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Williams, John A., Xuequn Chen, and Maria E. Sabbatini. "Small G proteins as key regulators of pancreatic digestive enzyme secretion." American Journal of Physiology-Endocrinology and Metabolism 296, no. 3 (2009): E405—E414. http://dx.doi.org/10.1152/ajpendo.90874.2008.

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Small GTP-binding (G) proteins act as molecular switches to regulate a number of cellular processes, including vesicular transport. Emerging evidence indicates that small G proteins regulate a number of steps in the secretion of pancreatic acinar cells. Diverse small G proteins have been localized at discrete compartments along the secretory pathway and particularly on the secretory granule. Rab3D, Rab27B, and Rap1 are present on the granule membrane and play a role in the steps leading up to exocytosis. Whether the function of these G proteins is simply to ensure appropriate targeting or if t

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Castle, J. D., P. Arvan, and R. Cameron. "Protein Production and Secretion in Exocrine Cells." Journal of Dental Research 66, no. 1_suppl (1987): 633–37. http://dx.doi.org/10.1177/00220345870660s105.

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Acinar cells of exocrine glands are highly specialized for producing, storing, and discharging secretory proteins for use on surfaces that represent interfaces between the organism and the surrounding environment. These functions are achieved through the secretory pathway that includes a series of functionally distinct intracellular compartments — The endoplasmic reticulum, subcompartmenls of the Go/gi complex, and the secretion granule in which exportable macromolecules are stored at high concentrations. Most secretion occurs by granule exocytosis in response to external hormonal or neural st

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Castle, J. D., P. Arvan, and R. Cameron. "Protein Production and Secretion in Exocrine Cells." Journal of Dental Research 66, no. 2_suppl (1987): 633–37. http://dx.doi.org/10.1177/00220345870660s205.

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Acinar cells of exocrine glands are highly specialized for producing, storing, and discharging secretory proteins for use on surfaces that represent interfaces between the organism and the surrounding environment. These functions are achieved through the secretory pathway that includes a series of functionally distinct intracellular compartments — the endoplasmic reticulum, subcompartments of the Golgi complex, and the secretion granule in which exportable macromolecules are stored at high concentrations. Most secretion occurs by granule exocytosis in response to external hormonal or neural st

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Barbeck, Mike, Marie-Luise Schröder, Said Alkildani, Ole Jung, and Ronald E. Unger. "Exploring the Biomaterial-Induced Secretome: Physical Bone Substitute Characteristics Influence the Cytokine Expression of Macrophages." International Journal of Molecular Sciences 22, no. 9 (2021): 4442. http://dx.doi.org/10.3390/ijms22094442.

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In addition to their chemical composition various physical properties of synthetic bone substitute materials have been shown to influence their regenerative potential and to influence the expression of cytokines produced by monocytes, the key cell-type responsible for tissue reaction to biomaterials in vivo. In the present study both the regenerative potential and the inflammatory response to five bone substitute materials all based on β-tricalcium phosphate (β-TCP), but which differed in their physical characteristics (i.e., granule size, granule shape and porosity) were analyzed for their ef

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Sobota, Jacqueline A., Francesco Ferraro, Nils Bäck, Betty A. Eipper, and Richard E. Mains. "Not All Secretory Granules Are Created Equal: Partitioning of Soluble Content Proteins." Molecular Biology of the Cell 17, no. 12 (2006): 5038–52. http://dx.doi.org/10.1091/mbc.e06-07-0626.

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Secretory granules carrying fluorescent cargo proteins are widely used to study granule biogenesis, maturation, and regulated exocytosis. We fused the soluble secretory protein peptidylglycine α-hydroxylating monooxygenase (PHM) to green fluorescent protein (GFP) to study granule formation. When expressed in AtT-20 or GH3 cells, the PHM-GFP fusion protein partitioned from endogenous hormone (adrenocorticotropic hormone, growth hormone) into separate secretory granule pools. Both exogenous and endogenous granule proteins were stored and released in response to secretagogue. Importantly, we foun

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Hashimoto, S., G. Fumagalli, A. Zanini, and J. Meldolesi. "Sorting of three secretory proteins to distinct secretory granules in acidophilic cells of cow anterior pituitary." Journal of Cell Biology 105, no. 4 (1987): 1579–86. http://dx.doi.org/10.1083/jcb.105.4.1579.

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The distribution of three proteins discharged by regulated exocytosis--growth hormone (GH), prolactin (PRL), and secretogranin II (SgII)--was investigated by double immunolabeling of ultrathin frozen sections in the acidophilic cells of the bovine pituitary. In mammotrophs, heavy PRL labeling was observed over secretory granule matrices (including the immature matrices at the trans Golgi surface) and also over Golgi cisternae. In contrast, in somatotrophs heavy GH labeling was restricted to the granule matrices; vesicles and tubules at the trans Golgi region showed some and the Golgi cisternae

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Leblond, F. A., G. Viau, J. Lainé, and D. Lebel. "Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: implication of GP-2." Biochemical Journal 291, no. 1 (1993): 289–96. http://dx.doi.org/10.1042/bj2910289.

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Regulated secretory proteins are thought to be sorted in the trans-Golgi network (TGN) via selective aggregation. To elucidate the biogenesis of the secretory granule in the exocrine pancreas, we reconstituted in vitro the conditions of pH and ions believed to exist in the TGN using the end product of this sorting process, the zymogen granule contents. Protein aggregation was dependent on pH (acidic) and on the presence of cations (10 mM Ca2+, 150 mM K+) to reproduce the pattern of proteins found in the granule. The constitutive secretory protein IgG was excluded from these aggregates. Zymogen

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Henningsson, Frida, Sonja Hergeth, Robert Cortelius, Magnus Åbrink, and Gunnar Pejler. "A role for serglycin proteoglycan in granular retention and processing of mast cell secretory granule components." FEBS Journal 273, no. 21 (2006): 4901–12. http://dx.doi.org/10.1111/j.1742-4658.2006.05489.x.

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Wong, J. G., K. T. Izutsu, M. R. Robinovitch, J. M. Iversen, M. E. Cantino, and D. E. Johnson. "Microprobe analysis of maturation-related elemental changes in rat parotid secretory granules." American Journal of Physiology-Cell Physiology 261, no. 6 (1991): C1033—C1041. http://dx.doi.org/10.1152/ajpcell.1991.261.6.c1033.

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Electron probe X-ray microanalysis was use to quantitate the elemental and mass changes that take place during the secretory granule maturation process. A single injection of isoproterenol stimulated the depletion of secretory granules from rat parotid acinar cells. Granules at different stages of maturation were analyzed as they reaccumulated within the cells over time. Dry mass measurements revealed that secretory material becomes concentrated about twofold within maturing granules. Nearly all of the increase in mass concentration could be attributed to a reduction in water space. Data are p

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Venkatesh, S. G., and S. U. Gorr. "A sulfated proteoglycan is necessary for storage of exocrine secretory proteins in the rat parotid gland." American Journal of Physiology-Cell Physiology 283, no. 2 (2002): C438—C445. http://dx.doi.org/10.1152/ajpcell.00552.2001.

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Sulfated proteoglycans have been proposed to play a role in the sorting and storage of secretory proteins in exocrine secretory granules. Rat parotid acinar cells expressed a 40- to 60-kDa proteoglycan that was stored in secretory granules. Treatment of the tissue with the proteoglycan synthesis inhibitor paranitrophenyl xyloside resulted in the complete abrogation of the sulfated proteoglycan. Pulse-chase experiments in the presence of the xyloside analog showed a significant reduction in the stimulated secretion and granule storage of the newly synthesized regulated secretory proteins amylas

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Courel, Maïté, Carrie Rodemer, Susan T. Nguyen, et al. "Secretory Granule Biogenesis in Sympathoadrenal Cells." Journal of Biological Chemistry 281, no. 49 (2006): 38038–51. http://dx.doi.org/10.1074/jbc.m604037200.

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Huh, Yang Hoon, Soung Hoo Jeon, and Seung Hyun Yoo. "Chromogranin B-induced Secretory Granule Biogenesis." Journal of Biological Chemistry 278, no. 42 (2003): 40581–89. http://dx.doi.org/10.1074/jbc.m304942200.

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Austin, C., R. Demaimay, I. Hinners, C. Panaretou, F. Wendler, and S. Tooze. "Molecular dissection of secretory granule biogenesis." Biochemical Society Transactions 29, no. 3 (2001): A62. http://dx.doi.org/10.1042/bst029a062.

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Kelly, Regis B. "Secretory granule and synaptic vesicle formation." Current Opinion in Cell Biology 3, no. 4 (1991): 654–60. http://dx.doi.org/10.1016/0955-0674(91)90037-y.

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Marino, C. R., J. D. Castle, and F. S. Gorelick. "Regulated phosphorylation of secretory granule membrane proteins of the rat parotid gland." American Journal of Physiology-Gastrointestinal and Liver Physiology 259, no. 1 (1990): G70—G77. http://dx.doi.org/10.1152/ajpgi.1990.259.1.g70.

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An antiserum raised against purified rat parotid secretory granule membrane proteins has been used to identify organelle-specific protein phosphorylation events following stimulation of intact cells from the rat parotid gland. After lobules were prelabeled with [32P]orthophosphate and exposed to secretagogues, phosphoproteins were immunoprecipitated with the granule membrane protein antiserum, separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and visualized by autoradiography. Parallel studies of stimulated amylase release were performed. Isoproterenol treatment of paroti

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POULI, Aristea E., Evaggelia EMMANOUILIDOU, Chao ZHAO, Christina WASMEIER, John C. HUTTON, and Guy A. RUTTER. "Secretory-granule dynamics visualized in vivo with a phogrin–green fluorescent protein chimaera." Biochemical Journal 333, no. 1 (1998): 193–99. http://dx.doi.org/10.1042/bj3330193.

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To image the behaviour in real time of single secretory granules in neuroendocrine cells we have expressed cDNA encoding a fusion construct between the dense-core secretory-granule-membrane glycoprotein, phogrin (phosphatase on the granule of insulinoma cells), and enhanced green fluorescent protein (EGFP). Expressed in INS-1 β-cells and pheochromocytoma PC12 cells, the chimaera was localized efficiently (up to 95%) to dense-core secretory granules (diameter 200–1000 nm), identified by co-immunolocalization with anti-(pro-)insulin antibodies in INS-1 cells and dopamine β-hydroxylase in PC12 ce

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Tompkins, Linda S., Kevin D. Nullmeyer, Sean M. Murphy, Craig S. Weber, and Ronald M. Lynch. "Regulation of secretory granule pH in insulin-secreting cells." American Journal of Physiology-Cell Physiology 283, no. 2 (2002): C429—C437. http://dx.doi.org/10.1152/ajpcell.01066.2000.

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Luminal acidification is important for the maturation of secretory granules, yet little is known regarding the regulation of pH within them. A pH-sensitive green fluorescent protein (EGFP) was targeted to secretory granules in RIN1046-38 insulinoma cells by using a construct in which the EGFP gene was preceded by the nucleotide sequence for human growth hormone. Stimulatory levels of glucose doubled EGFP secretion from cell cultures, and potentiators of glucose-induced insulin secretion enhanced EGFP release. Thus this targeted EGFP is useful for population measurements of secretion. However,

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Chock, S. P., E. A. Schmauder-Chock, E. Cordella-Miele, L. Miele, and A. B. Mukherjee. "The localization of phospholipase A2 in the secretory granule." Biochemical Journal 300, no. 3 (1994): 619–22. http://dx.doi.org/10.1042/bj3000619.

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A heat-resistant phospholipase A2 has been detected in the secretory granules of the mast cell [Chock, Rhee, Tang and Schmauder-Chock (1991) Eur. J. Biochem. 195, 707-713]. By using ultrastructural immunocytochemical techniques, we have now localized this enzyme to the matrix of the secretory granule. Like the cyclo-oxygenase [Schmauder-Chock and Chock (1989) J. Histochem. Cytochem. 37, 1319-1328], this enzyme also adheres tightly to the ribbon-like granule matrix components. The results from Western-blot analysis suggest that it has a molecular mass of about 14 kDa. The localization of the ph

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