Relevant bibliographies by topics / Secretory compartments

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Secretory compartments'

Author: Grafiati
Published: 19 October 2024
Last updated: 31 July 2025

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Journal articles on the topic "Secretory compartments"

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Schmidt, W. K., and H. P. Moore. "Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells." Molecular Biology of the Cell 6, no. 10 (1995): 1271–85. http://dx.doi.org/10.1091/mbc.6.10.1271.

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Newly synthesized prohormones and their processing enzymes transit through the same compartments before being packaged into regulated secretory granules. Despite this coordinated intracellular transport, prohormone processing does not occur until late in the secretory pathway. In the mouse pituitary AtT-20 cell line, conversion of pro-opiomelanocortin (POMC) to mature adrenocorticotropic hormone involves the prohormone convertase PC1. The mechanism by which this proteolytic processing is restricted to late secretory compartments is unknown; PC1 activity could be regulated by compartment-specif
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Derré, Isabelle, and Ralph R. Isberg. "LidA, a Translocated Substrate of the Legionella pneumophila Type IV Secretion System, Interferes with the Early Secretory Pathway." Infection and Immunity 73, no. 7 (2005): 4370–80. http://dx.doi.org/10.1128/iai.73.7.4370-4380.2005.

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ABSTRACT Legionella pneumophila uses a type IV secretion system to deliver effector molecules into the host cell and establish its replication vacuole. In this study, we investigated the role of LidA, a translocated substrate associated with the surface of the L. pneumophila-containing vacuole. LidA is secreted into the host cell throughout the replication cycle of the bacteria and associates with compartments of the early secretory pathway. When overexpressed in mammalian cells or yeast, LidA interferes with the early secretory pathway, probably via a domain predicted to be rich in coiled-coi
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Bianco, P., M. Riminucci, E. Bonucci, J. D. Termine, and P. G. Robey. "Bone sialoprotein (BSP) secretion and osteoblast differentiation: relationship to bromodeoxyuridine incorporation, alkaline phosphatase, and matrix deposition." Journal of Histochemistry & Cytochemistry 41, no. 2 (1993): 183–91. http://dx.doi.org/10.1177/41.2.8419458.

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We defined two distinct maturational compartments (proliferative and secretory) of osteogenic cells in vivo on the basis of ALP activity, BrdU incorporation, cell shape, and BSP production. BSP immunoreactivity was found to mark cells in the secretory but not in the proliferative compartment. We established the phenotypic similarity of primitive marrow stromal cells with proliferating perichondral cells (fibroblast-like, ALP+, BrdU+, BSP-). This suggests the potential functional equivalence of the two cell types as committed non-secretory osteogenic cells and points to the duality of osteogeni
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Tobin, V. A., and M. Ludwig. "The actin filament and dendritic peptide release." Biochemical Society Transactions 35, no. 5 (2007): 1243–46. http://dx.doi.org/10.1042/bst0351243.

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F-actin remodelling has been implicated in regulated secretion from many cell types, in particular secretion from neuron axon terminals and neuroendocrine cell types. Cortical F-actin has long been postulated to act as a barrier to vesicle movement and hence to inhibit secretion; however, more recent studies point to F-actin remodelling providing both supporting and restraining roles in secretion. Magnocellular neurons of the supraoptic nucleus secrete either oxytocin or vasopressin from their dendrites as well as their axon terminals; and peptide release from these two compartments can be dif
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Naik, Haley B., Melissa Beshire, Breda M. Walsh, Jingjing Liu, and David I. Soybel. "Secretory state regulates Zn2+ transport in gastric parietal cell of the rabbit." American Journal of Physiology-Cell Physiology 297, no. 4 (2009): C979—C989. http://dx.doi.org/10.1152/ajpcell.00577.2008.

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Secretory compartments of neurons, endocrine cells, and exocrine glands are acidic and contain high levels of labile Zn2+. Previously, we reported evidence that acidity is regulated, in part, by the content of Zn2+ in the secretory [i.e., tubulovesicle (TV)] compartment of the acid-secreting gastric parietal cell. Here we report studies focusing on the mechanisms of Zn2+ transport by the TV compartment in the mammalian (rabbit) gastric parietal cell. Uptake of Zn2+ by isolated TV structures was monitored with a novel application of the fluorescent Zn2+ reporter N-(6-methoxy-8-quinolyl)- para-t
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Plutner, H., A. D. Cox, S. Pind, et al. "Rab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments." Journal of Cell Biology 115, no. 1 (1991): 31–43. http://dx.doi.org/10.1083/jcb.115.1.31.

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We report an essential role for the ras-related small GTP-binding protein rab1b in vesicular transport in mammalian cells. mAbs detect rab1b in both the ER and Golgi compartments. Using an assay which reconstitutes transport between the ER and the cis-Golgi compartment, we find that rab1b is required during an initial step in export of protein from the ER. In addition, it is also required for transport of protein between successive cis- and medial-Golgi compartments. We suggest that rab1b may provide a common link between upstream and downstream components of the vesicular fission and fusion m
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Raote, Ishier, and Vivek Malhotra. "Protein transport by vesicles and tunnels." Journal of Cell Biology 218, no. 3 (2019): 737–39. http://dx.doi.org/10.1083/jcb.201811073.

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Palade’s corpus placed small vesicles as the sole means to transport proteins across stable distinct compartments of the secretory pathway. We suggest that cargo, spatial organization of secretory compartments, and the timing of fission of cargo-filled containers dictate the design of transport intermediates that can be vesicles and transient direct tunnels.
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Oyarce, A. M., and B. A. Eipper. "Identification of subcellular compartments containing peptidylglycine alpha-amidating monooxygenase in rat anterior pituitary." Journal of Cell Science 108, no. 1 (1995): 287–97. http://dx.doi.org/10.1242/jcs.108.1.287.

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Both soluble and integral membrane forms of peptidylglycine alpha-amidating monooxygenase (PAM) are expressed in the rat anterior pituitary, making it an ideal model system for studying the routing of proteins into secretory granules. To identify the subcellular compartments involved in the routing of integral membrane PAM, we used subcellular fractionation, metabolic labeling and immunoblot analysis. Mature secretory granules were found to contain full-length integral membrane PAM along with a significant amount of soluble PAM generated by endoproteolytic cleavage. PAM proteins were not co-di
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Diekwisch, Thomas G. H. "Subunit Compartments of Secretory Stage Enamel Matrix." Connective Tissue Research 38, no. 1-4 (1998): 101–11. http://dx.doi.org/10.3109/03008209809017026.

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Saraste, Jaakko. "Introduction: Enigmatic compartments of the secretory pathway." Seminars in Cell Biology 3, no. 5 (1992): 299. http://dx.doi.org/10.1016/1043-4682(92)90016-o.

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Dissertations / Theses on the topic "Secretory compartments"

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Chehayeb, James. "Proteomic analysis of «Ascaris suum» fluid compartments and secretory products." Thesis, McGill University, 2014. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=123155.

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Ascaris lumbricoides infects at least 10% of the world's population and is a public health issue in most low-to-middle income countries. Survival of this parasite in its host is mediated at least in part by materials exported to the host in secretions. Although very little is known about the composition of these secretions, defining their contents and functions could shed light on the host-parasite interactions that lead to parasite establishment and persistence in the host. Ascaris suum, a parasite of pigs, was used as a model organism because its genome has been sequenced and it is closely r
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Al-Qatabi, Noha. "Caractérisation de protéines atypiques à domaine BAR codées par Toxoplasma gondii." Electronic Thesis or Diss., Université Côte d'Azur, 2024. http://www.theses.fr/2024COAZ6006.

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Toxoplasma gondii, l'agent pathogène causant la toxoplasmose, infecte et se réplique à l'intérieur de cellules hôtes grâce à sa capacité à sécréter des facteurs stockés dans des organites sécrétoires uniques (rhoptries, micronèmes, granules denses). Ces facteurs permettent au parasite de moduler le système immunitaire de l'hôte et d'en capturer certains éléments. La formation de ces organites uniques et les processus de sécrétion et de capture dépendent d'événements de trafic vésiculaire dont les bases moléculaires restent peu connues. Notamment, il n'existe pratiquement aucune caractérisation
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Jonikas, Martin Casimir. "The anatomy of a cellular folding compartment: Genetic dissection of protein folding in the secretory pathway." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3390051.

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Moutaux, Eve. "Régulation du transport axonal par l'activité neuronale : Implication pour le développement des réseaux neuronaux Neuronal activity recruits an axon-resident pool of secretory vesicles to regulate axon branching Reconstituting Corticostriatal Network on-a-Chip Reveals the Contribution of the Presynaptic Compartment to Huntington’s Disease Neuronal network maturation differently affects secretory vesicles and mitochondria transport in axons ALG-2 interacting protein-X (Alix) is required for activity-dependent bulk endocytosis at brain synapses An integrated microfluidic/microelectrode array for the study of activity-dependent intracellular dynamics in neuronal networks." Thesis, Université Grenoble Alpes, 2020. https://thares.univ-grenoble-alpes.fr/2020GRALV024.pdf.

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Pendant le développement, les projections axonales à longue distance se ramifient pour se connecter à leurs cibles. L’établissement et le remodelage de ces connexions est notamment régulé par l’activité neuronale. L’adaptation de la morphologie de l’axone nécessite alors des quantités importantes de matériel sécrétoire et de facteur trophiques comme le BDNF (brain derived neurotrophic factor). Ce matériel est transporté dans des vésicules le long de l’axone depuis le corps cellulaire où il est synthétisé, vers les sites actifs à l’extrémité de l’axone. Si le relargage de vésicules sécrétoires
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Titus, Brian John. "p22 associates with compartments of the early secretory pathway and with the microtubule cytoskeleton : evidence for a role in membrane trafficking /." 2003. http://wwwlib.umi.com/dissertations/fullcit/3073575.

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Waldron, Elaine [Verfasser]. "LRP1 modulates APP trafficking and APP metabolism within compartments of the secretory pathway : increased AICD generation is ineffective in nuclear translocation and transcriptional activation / Elaine Waldron." 2008. http://d-nb.info/987171437/34.

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Book chapters on the topic "Secretory compartments"

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Hendriks, Rob J. M., and Stephen D. Fuller. "Compartments of the Early Secretory Pathway." In Subcellular Biochemistry. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2401-4_4.

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Gooris, Peter J. J., and Carl-Peter Cornelius. "Anatomy of the Orbit: Overall Aspects of the Peri- and Intra Orbital Soft Tissues." In Surgery in and around the Orbit. Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-40697-3_3.

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AbstractSoft tissue systems in and around the orbit are presented in detail. The complexity of the soft tissue structures and its topographical location provides optimal environment for the delicate globe and supportive elements.Anatomic aspects and the protective and physiological function of the eyelids are described. The secretory lacrimal system and the spread of aqueous fluid along the globe and final drainage will be discussed. Anatomical features of the globe and the accompanying extraocular musculature are highlighted. The involved musculature allows for a most efficient guarantee of f
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Hamilton, R. L., R. J. Havel, C. A. Hornick, et al. "Subcellular Dissection and Characterization of Plasma Lipoprotein Secretory (Golgi) and Endocytic (Multivesicular Bodies) Compartments of Rat Hepatocytes." In Receptor-Mediated Uptake in the Liver. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70956-2_23.

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Ghanem, Esther, and Sebastian Springer. "Determining the Activity of the Transporter Associated with Antigen Processing in the Compartments of the Secretory Pathway." In Antigen Processing. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-218-6_11.

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Graham, T., and S. Emr. "SEC18." In Secretory Pathway. Oxford University PressOxford, 1994. http://dx.doi.org/10.1093/oso/9780198599425.003.0082.

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Abstract sec18 mutant cells were originally described to exhibit a temperature-sensitive block in protein transport from the ER to the Golgi complex and to accumulate ER and small vesicles12. The phenotype of double sec mutants (e.g. sec18 sec23) suggests that Sec18p is not required to form transport vesicles from the ER, but is required for the targeting and/or fusion of these transport vesicles with an early Golgi compartment3. Further studies indicate that the sec18 mutant exhibits a temperature-sensitive block at most, if not all, intercompartmental transport steps along the secretory path
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Rothblatt, Jonathan, Peter Novick, and Tom H. Stevens. "Entering the secretory pathway." In Secretory Pathway. Oxford University PressOxford, 1994. http://dx.doi.org/10.1093/oso/9780198599425.003.0001.

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Abstract In prokaryotic and eukaryotic cells, specialized processes such as secretion and signal transduction, as well as the enzymatic reactions of intermediary metabolism, are organized into membranes and membrane-enclosed compartments. The unique biochemical make-up of each compartment and the specificity and directionality of the secretory process can be maintained only if mechanisms exist for selective targeting of newly-made proteins to their correct subcellular location, for their active transport across impermeant membrane barriers and for their covalent and conformational modification
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Schwaninger, Ruth. "In vitro reconstitution of vesicular transport from the endoplasmic reticulum to the cis Golgi in semi-intact cells." In Protein Targeting. Oxford University PressOxford, 1992. http://dx.doi.org/10.1093/oso/9780199632060.003.0009.

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Abstract Proteins destined for the plasma membrane, lysosomes, and endosomes, or the extracellular fluid are transported between organelles of the exocytic or secretory pathway of eukaryotic cells by vesicles that bud from one compartment and fuse with another. A high degree of specificity for this sequential budding, targeting, and fusion of transport vesicles must be maintained, or the cell would rapidly destroy its highly compartmental organization. Progression of newly synthesized proteins along this pathway can be followed by observing the maturation of N-linked oligosaccharide chains of
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Mellman, I. "Rab4." In Secretory Pathway. Oxford University PressOxford, 1994. http://dx.doi.org/10.1093/oso/9780198599425.003.0183.

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Abstract Rab4 was first localized to early endosomes by screening subcellular fractions prepared from CHO cells using the original panel of polyclonal anti-rab antibodies prepared by Bruno Goud3 Free-flow electrophoresis fractions were analyzed by immunoblotting, and only antibody to rab4 was found to yield a clear signal in the anodally-shifted fractions that co-migrated with transferrin receptor. This localization was confirmed by immunofluorescence performed on cells (Hela, CHO) stably or transiently transfected with wild type rab4a cDNAs. lmmunoelectron microscopy (immuno-EM) on frozen thi
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Cramer, Louise P., and Daniel F. Cutler. "Sorting between exocytic pathways in PC12 cells." In Protein Targeting. Oxford University PressOxford, 1992. http://dx.doi.org/10.1093/oso/9780199632060.003.0003.

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Abstract Exocytic protein traffic in neuronal and endocrine cells is complicated by the presence of more than one route to the cell surface. In addition to the constitutive secretory pathway, regulated secretory routes are also present in these cells. Regulated secretion is characterized by the intracellular storage of secretory material which is only released from the cell following the application of an external stimulus. This is in contrast to constitutive secretion in which proteins are not stored inside the cell but are constantly released. The organelles acting as storage compartments in
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Benarroch, Eduardo E. "Vesicular Trafficking." In Neuroscience for Clinicians, edited by Eduardo E. Benarroch. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780190948894.003.0007.

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Normal cell function depends on the appropriate synthesis, maturation, sorting, and delivery of fully processed proteins and other macromolecules to specific intracellular compartments; uptake of material from the cell exterior; and regulated intracellular processing and degradation of proteins, lipids, complex carbohydrates, abnormal aggregates, and senescent organelles. These fundamental functions involve secretory, endocytic, and autophagic pathways. The secretory pathway is responsible for protein maturation, sorting, and delivery of transmembrane and secreted proteins from their site of s
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Conference papers on the topic "Secretory compartments"

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Beznoussenko, Galina. "Re-examination of the secretory compartments in the study of transport organelles in mitotic cells with correlative light, immune and three-dimensional electron microscopy." In European Microscopy Congress 2020. Royal Microscopical Society, 2021. http://dx.doi.org/10.22443/rms.emc2020.960.

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Liu, Yen-Cheng, Saeid Ansaryan, Xiaokang Li, Eduardo R. Arvelo, and Hatice Altug. "High-throughput optofluidic nanoplasmonic biosensor array for monitoring single-cell secretion in real-time." In CLEO: Applications and Technology. Optica Publishing Group, 2022. http://dx.doi.org/10.1364/cleo_at.2022.am2i.6.

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We report a high-throughput biosensing microarray platform integrating ultrasensitive nanoplasmonic substrate and microwell compartments for label-free and real-time secretome monitoring. Interleukin-2 from hundreds of single EL4 cells were measured and a statistical analysis was done.
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Patscheke, H., and G. Mathieu. "MONITORING OF THE PLATELET ALPHA-GRANULE SECRETION IN THE AGGREGOMETER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643492.

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If platelets are stimulated to secrete and the aggregation is prevented by EDTA and no stirring, the optical density (OD) decreases as a consequence of secretion (Patscheke et al. Thromb. Res. 33: 314, 1984). The purpose of this study was to determine which secretory compartment causes the change in OD and to analyze the quantitative relationship between decrease in OD and granule discharge. Human washed platelets were stimulated with thrombin and A 23187 in a Lumi-Aggregometer (Chrono-Log) which permitted simultaneous recording of the change in OD and of the ATP release from dense granules. A
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