Relevant bibliographies by topics / ATP6AP2

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  2. Dissertations / Theses

Academic literature on the topic 'ATP6AP2'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 February 2022

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Journal articles on the topic "ATP6AP2"

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Guida, Maria Clara, Tobias Hermle, Laurie A. Graham, et al. "ATP6AP2 functions as a V-ATPase assembly factor in the endoplasmic reticulum." Molecular Biology of the Cell 29, no. 18 (2018): 2156–64. http://dx.doi.org/10.1091/mbc.e18-04-0234.

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ATP6AP2 (also known as the [pro]renin receptor) is a type I transmembrane protein that can be cleaved into two fragments in the Golgi apparatus. While in Drosophila ATP6AP2 functions in the planar cell polarity (PCP) pathway, recent human genetic studies have suggested that ATP6AP2 could participate in the assembly of the V-ATPase in the endoplasmic reticulum (ER). Using a yeast model, we show here that the V-ATPase assembly factor Voa1 can functionally be replaced by Drosophila ATP6AP2. This rescue is even more efficient when coexpressing its binding partner ATP6AP1, indicating that these two
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Rujano, Maria A., Magda Cannata Serio, Ganna Panasyuk, et al. "Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with autophagic defects." Journal of Experimental Medicine 214, no. 12 (2017): 3707–29. http://dx.doi.org/10.1084/jem.20170453.

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The biogenesis of the multi-subunit vacuolar-type H+-ATPase (V-ATPase) is initiated in the endoplasmic reticulum with the assembly of the proton pore V0, which is controlled by a group of assembly factors. Here, we identify two hemizygous missense mutations in the extracellular domain of the accessory V-ATPase subunit ATP6AP2 (also known as the [pro]renin receptor) responsible for a glycosylation disorder with liver disease, immunodeficiency, cutis laxa, and psychomotor impairment. We show that ATP6AP2 deficiency in the mouse liver caused hypoglycosylation of serum proteins and autophagy defec
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Pringle, K. G., A. L. Conquest, C. M. Mitchell, T. Zakar, and E. R. Lumbers. "118. THE PRORENIN RECEPTOR/PLZF PATHWAY IN HUMAN AMNION." Reproduction, Fertility and Development 22, no. 9 (2010): 36. http://dx.doi.org/10.1071/srb10abs118.

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Prorenin, despite being inactive, is the major form of renin found in amniotic fluid and reproductive tissues. Prorenin becomes active if it binds to the novel prorenin receptor (ATP6AP2). The prorenin-ATP6AP2 complex has been found to stimulate translocation of Promyelocytic Zinc Finger (PLZF) protein to the nucleus where it increases expression of the p85α subunit of PI3 kinase (PI3K-p85α) and represses the expression of ATP6AP21. Progesterone and glucocorticoids have also been shown to stimulate PLZF2, 3. We aimed to find out if PLZF and the prorenin-ATP6AP2 pathway interact in human reprod
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Abbas, Yazan M., Di Wu, Stephanie A. Bueler, Carol V. Robinson, and John L. Rubinstein. "Structure of V-ATPase from the mammalian brain." Science 367, no. 6483 (2020): 1240–46. http://dx.doi.org/10.1126/science.aaz2924.

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In neurons, the loading of neurotransmitters into synaptic vesicles uses energy from proton-pumping vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases). These membrane protein complexes possess numerous subunit isoforms, which complicates their analysis. We isolated homogeneous rat brain V-ATPase through its interaction with SidK, a Legionella pneumophila effector protein. Cryo–electron microscopy allowed the construction of an atomic model, defining the enzyme’s ATP:proton ratio as 3:10 and revealing a homolog of yeast subunit f in the membrane region, which we tentatively ident
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Figueiredo, Marta, Arezoo Daryadel, Gabin Sihn, et al. "The (pro)renin receptor (ATP6ap2) facilitates receptor-mediated endocytosis and lysosomal function in the renal proximal tubule." Pflügers Archiv - European Journal of Physiology 473, no. 8 (2021): 1229–46. http://dx.doi.org/10.1007/s00424-021-02598-z.

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AbstractThe ATP6ap2 (Pro)renin receptor protein associates with H+-ATPases which regulate organellar, cellular, and systemic acid–base homeostasis. In the kidney, ATP6ap2 colocalizes with H+-ATPases in various cell types including the cells of the proximal tubule. There, H+-ATPases are involved in receptor-mediated endocytosis of low molecular weight proteins via the megalin/cubilin receptors. To study ATP6ap2 function in the proximal tubule, we used an inducible shRNA Atp6ap2 knockdown rat model (Kd) and an inducible kidney-specific Atp6ap2 knockout mouse model. Both animal lines showed highe
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Jin, Xiaosheng, Peipei Cai, Zhengchao Shi, Fangpeng Ye, Tingting Ji, and Rongzhou Li. "MiR-148a-3p suppresses the progression of gastric cancer cells through targeting ATP6AP2." Tropical Journal of Pharmaceutical Research 19, no. 9 (2020): 1821–26. http://dx.doi.org/10.4314/tjpr.v19i9.4.

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Purpose: Gastric cancer (GC) is one of the most frequent tumors with high mortality rate, worldwide. A proper understanding of the mechanism underlying its progression is required for its diagnosis and development of novel treatment option. MicroRNAs are associated with the development and advancement of different types of cancer, including GC. The current research was aimed at investigating the molecular and biological function of miR-148a-3p in GC development.Methods: A human normal gastric epithelial cell line, GES-1 (control) as well as four GC cell lines (NUGC-4, SNU-520, STKM-2 and MKN-7
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Binger, Katrina J., Martin Neukam, Sudhir Gopal Tattikota та ін. "Atp6ap2 deletion causes extensive vacuolation that consumes the insulin content of pancreatic β cells". Proceedings of the National Academy of Sciences 116, № 40 (2019): 19983–88. http://dx.doi.org/10.1073/pnas.1903678116.

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Pancreatic β cells store insulin within secretory granules which undergo exocytosis upon elevation of blood glucose levels. Crinophagy and autophagy are instead responsible to deliver damaged or old granules to acidic lysosomes for intracellular degradation. However, excessive consumption of insulin granules can impair β cell function and cause diabetes. Atp6ap2 is an essential accessory component of the vacuolar ATPase required for lysosomal degradative functions and autophagy. Here, we show that Cre recombinase-mediated conditional deletion of Atp6ap2 in mouse β cells causes a dramatic accum
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von Bohlen und Halbach, Oliver, and Alexander Bracke. "Roles and functions of Atp6ap2 in the brain." Neural Regeneration Research 13, no. 12 (2018): 2038. http://dx.doi.org/10.4103/1673-5374.241428.

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Wang, Y., K. G. Pringle, Y. Chen, T. Zakar, and E. R. Lumbers. "311. REGULATION OF THE RENIN ANGIOTENSIN SYSTEM (RAS) IN A TROPHOBLAST CELL LINE BY CYCLIC ADENOSINE MONOPHOSPHATE (cAMP) AND 5'-AZA-2'-DEOXYCYTIDINE (AZA)." Reproduction, Fertility and Development 22, no. 9 (2010): 111. http://dx.doi.org/10.1071/srb10abs311.

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Renin and renin-like activities have been detected in early gestation placentae1,2. To explore what regulates RAS expression in trophoblasts we studied the effects of cAMP and AZA (DNA demethylating agent) on the expression of mRNAs for prorenin receptor (ATP6AP2), prorenin (REN), angiotensinogen (AGT), angiotensin converting enzyme (ACE), ACE2, angiotensin II type 1 receptor (AGTR1), and a downstream target of the prorenin receptor, cyclooxygenase-2 (PTGS2) in the early human trophoblast cell line HTR-8/SVneo. Cells were cultured for 24 or 48 h with vehicle, 0.5 mM cAMP or 15 mM AZA. Messenge
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Delforce, Sarah J., Eugenie R. Lumbers, Celine Corbisier de Meaultsart, et al. "Expression of renin–angiotensin system (RAS) components in endometrial cancer." Endocrine Connections 6, no. 1 (2017): 9–19. http://dx.doi.org/10.1530/ec-16-0082.

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A dysfunctional endometrial renin–angiotensin system (RAS) could aid the growth and spread of endometrial cancer. To determine if the RAS is altered in endometrial cancer, we measured RAS gene expression and protein levels in 30 human formalin-fixed, paraffin-embedded (FFPE) endometrioid carcinomas and their adjacent endometrium. All components of the RAS were expressed in most tumours and in adjacent endometrium; mRNA levels of (pro)renin receptor (ATP6AP2), angiotensin II type 1 receptor (AGTR1), angiotensin-converting enzyme (ACE1) and angiotensin-converting enzyme 2 (ACE2) mRNA levels were
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Dissertations / Theses on the topic "ATP6AP2"

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Rousselle, Anthony. "Role of the (Pro)renin Receptor [(P)RR/ATP6ap2] in Osteoclast and Macrophage Physiology." Doctoral thesis, Humboldt-Universität zu Berlin, 2017. http://dx.doi.org/10.18452/18599.

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Vor zehn Jahren wurde der (Pro)Renin-Rezeptor [(P)RR] entdeckt und als neuer Bestandteil des Renin-Angiotensin-Systems beschrieben. Neuere Studien ergaben, dass der (P)RR mit der vakuolären H+-ATPase (V-ATPase) assoziiert sein kann, weshalb er auch V-ATPase associated protein 2 (ATP6ap2) genannt wird. In Osteoklasten befinden sich V-ATPase hauptsächlich an der zur Knochenoberfläche gerichteten Plasmamembran und transportieren Protonen in den extrazellulären Raum. Mäuse mit genetischer Deletion verschiedener V-ATPase-Untereinheiten charakterisiert durch einen Anstieg von Knochenmasse (Osteopet
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Burckle, Céline. "Le Récepteur de la prorénine/rénine-RR/ATP6AP2 : données de biologie cellulaire : poids moléculaire, topologie, localisation subcellulaire : approche fonctionnelle." Paris 7, 2006. http://www.theses.fr/2006PA077227.

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In vivo, la fonction du récepteur de la rénine (RR/ATP6AP2) n'est pas connue. Des résultats divergents concernant sa localisation sub-cellulaire fragilisent l'hypothèse d'un récepteur de surface. Ainsi, nous avons repris la question de la localisation cellulaire du RR/ATP6AP2 endogène. Afin d'étudier la fonction de RR/ATP6AP2 in vivo, nous avons transitoirement supprimer son expression chez le poisson zèbre, et avons généré des rats surexprimant RR/ATP6AP2 dans les cellules musculaires lisses. Nos résultats suggèrent une double fonction pour RR/ATP6AP2, reflétant une possible divergence au cou
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Cannata, Serio Magda. "Mutations in V-ATPase assembly factors cause Congenital Disorder of Glycosylation (CDG) with autophagic liver disease Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with autophagic defects Mutations in the V-ATPase assembly factor VMA21 cause a congenital disorder of glycosylation with autophagic liver disease." Thesis, Sorbonne Paris Cité, 2019. https://wo.app.u-paris.fr/cgi-bin/WebObjects/TheseWeb.woa/wa/show?t=2277&f=17696.

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La pompe protonique V-ATPase est un complexe impliqué dans l'acidification intracellulaire. Elle est formée par le secteur V0 pour le transport des protons et le secteur V1 pour l'hydrolyse de l'ATP. Des études pionnières chez S. cerevisiae montrent que l'assemblage du secteur V0 commence dans le réticulum endoplasmique (ER) grâce au contrôle de 5 facteurs d'assemblage: Vma21p, Vma12p, Vma22p, Pkr1p et Voa1p. Une fois assemblé, le secteur V0 est transporté par Vma21p jusqu'au cis-Golgi, où, avec le secteur V1, constitue un holoenzyme fonctionnel. Ce processus chez l'homme n¿est pas encore clai
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Rousselle, Anthony [Verfasser], Michael [Gutachter] Bader, Achim [Gutachter] Leutz, and Uwe [Gutachter] Kornak. "Role of the (Pro)renin Receptor [(P)RR/ATP6ap2] in Osteoclast and Macrophage Physiology / Anthony Rousselle ; Gutachter: Michael Bader, Achim Leutz, Uwe Kornak." Berlin : Humboldt-Universität zu Berlin, 2017. http://d-nb.info/1189328143/34.

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Schäfer, Simon Thomas [Verfasser]. "ATP6AP2 is critically involved in adult hippocampal neurogenesis and reveals stage-specific functions for Wnt/ß-Catenin and Wnt/Planar Cell Polarity (PCP) signaling / Simon Thomas Schäfer." Greifswald : Universitätsbibliothek Greifswald, 2015. http://d-nb.info/1069389331/34.

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Dau, Andressa Minussi Pereira. "Sistema renina-angiotensina nas células da teca e granulosa durante a ovulação e luteinização em bovinos." Universidade Federal de Santa Maria, 2017. http://repositorio.ufsm.br/handle/1/11578.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPES<br>The objective of present study was to investigate (Pro)renin receptor function in the theca and granulosa cells during the preovulatory period and luteinization in cattle. During the initial preovulatory period, prorenin induced the resumption of oocyte meiosis even in the presence of follicular hemisections or forskolin. In granulosa cells, pró-renina did not increase LHinduced epiregulin (EREG) mRNA after 6 h of culture. Treatment with prorenin plus LH increased amphiregulin (AREG) and prostaglandin synthase 2 (PTGS2
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Vogel, Lukas Hermann [Verfasser], Jörg [Akademischer Betreuer] Peters, Jörg [Gutachter] Peters, and Sigrid [Gutachter] Hoffmann. "Einfluss der (Pro)Renin Rezeptor ((P)RR, ATP6ap2) Downregulation auf primäre Zilien und den Zellzyklus in As4.1 Zellen / Lukas Hermann Vogel ; Gutachter: Jörg Peters, Sigrid Hoffmann ; Betreuer: Jörg Peters." Greifswald : Universität Greifswald, 2021. http://d-nb.info/1230552936/34.

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Morch, Anica [Verfasser], Jörg [Akademischer Betreuer] Peters, Michael [Gutachter] Bader, and Jörg [Gutachter] Peters. "Die Lokalisation des (Pro)Reninrezeptors in renalen, kardialen und neuronalen Zellen und Geweben sowie seine Funktion als akzessorisches Protein ATP6ap2 der vakuolären H+-ATPase / Anica Morch ; Gutachter: Michael Bader, Jörg Peters ; Betreuer: Jörg Peters." Greifswald : Universität Greifswald, 2019. http://d-nb.info/1195140894/34.

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Dimitrov, Bianca [Verfasser], and Sabine [Akademischer Betreuer] Strahl. "Klinische, molekularbiologische und biochemische Charakterisierung eines neuen Patientendefekts im „ATPase H+-transporting accessory protein 1“ (ATP6AP1)-Gen / Bianca Dimitrov ; Betreuer: Sabine Strahl." Heidelberg : Universitätsbibliothek Heidelberg, 2017. http://d-nb.info/1177689944/34.

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