Results 31 to 40 of about 9,446 (221)

Receptor Activity-Modifying Proteins: RAMPing up Adrenomedullin Signaling [PDF]

Molecular Endocrinology, 2007
Adrenomedullin (AM) is a 52-amino-acid multifunctional peptide that circulates in the plasma in the low picomolar range and can exert a multitude of biological effects through an autocrine/paracrine mode of action. The mechanism by which AM transduces its signal represents a novel and pharmacologically tractable paradigm in G protein-coupled receptor ...
Carrie, Gibbons, Ryan, Dackor, William, Dunworth, Kimberly, Fritz-Six, Kathleen M, Caron   +4 more
openaire   +2 more sources

Circulating adrenomedullin estimates survival and reversibility of organ failure in sepsis: the prospective observational multinational Adrenomedullin and Outcome in Sepsis and Septic Shock-1 (AdrenOSS-1) study [PDF]

, 2018
Background: Adrenomedullin (ADM) regulates vascular tone and endothelial permeability during sepsis. Levels of circulating biologically active ADM (bio-ADM) show an inverse relationship with blood pressure and a direct relationship with vasopressor ...
Abroug, S., Alcourt, Y., Allam, H., Antonelli, M., Aubrey, A., Bachoumas, K., Bangert, K., Barthelemy, R., Bartoli, C., Baudrillart, L., Bayer, S., Beeken, T., Beeker, T., Begot, E., Beishuizen, A., Beishuizen, B., Berghe, C., Bergmann, A., Berquier, G., Besancenot, H., Blet, A., Bloos, F., Bloos, P., Bodet-Contentin, L., Boivin, A., Bongiovanni, C., Bonnet, F., Border, N., Bos-Burgmeijer, M., Bouadma, L., Bouhours, G., Bourdier, J., Bourzeix, P., Braad, A., Brick, L., Brulls, C., Buelens, I., Calvat, S., Caumon, E., Cayot, S., Chapellas, C., Chassier, C., Chenaf, S., Chousterman, B. G., Clere-Jehl, R., Colin, G., Collienne, C., Constantin, J. -M., Conte, M., Cornet, A., Cracco, C., Cupaciu, A., Cutuli, S. L., D'Arrigo, S., Daix, T., Damoisel, C., De Heer, G., De Schryver, N., Deiler, V., Deisz, R., Delabranche, X., Delmas, J., Denou, F., Dequin, P. F., Desachy, A., Deschamps, A., Deye, N., Dhif, N., Di Somma, S., Digravio, V., Dubief, E., Duchambon, A. -A., Dugernier, T., Dujardin, M. -F., Ehrmann, S., Fally, M. A., Fedou, A. -L., Feld, F., Feliot, E., Fesard, P., Fiancette, M., Fournier, M. -C., Francois, B., Freys, G., Frings, D., Fuhrmann, V., Fullekrug, B., Gaillard, T., Galy, A., Garcon, P., Garot, D., Gaudry, S., Gaugain, S., Gayat, E., Geukens, P., Geven, C., Godet, T., Gonnert, F., Gouhier, C., Goury, A., Guerin, R., Guillon, A., Guyon, M., Hartmann, O., Haucke, A., Hecketsweiler, S., Heenen, S., Hemelaar, P., Henin, P., Henker, R., Henry-Lagarrigue, M., Herafa, I., Heunks, L., Hoedemaekers, A., Hohn, A., Hollinger, A., Huberlant, V., Huot, B., Jabaudon, M., Jacob, L., Janisch, T., Jaschinski, U., Joret, A., Jouan, Y., Kehl, L., Kelly, D. S., Kerdjana, L., Kerinn, M., Kerymel, M., Kluge, S., Kohlberg, K. K., Kolanos, S., Kortgen, A., Kreuser, I., Kummerlen, C., La Combe, B., La Foucher, B., Lacherade, J. -C., Lafon, C., Laissi, M., Laleu, S., Lascarrou, J. -B., Lascarrou, J. B., Lasocki, S., Laterre, P. -F., Laterre, P. F., Launoy, A., Laurent, Y., Lebert, C., Leblanc, D., Lebreton, S., Legall, C., Legrand, M., Legras, A., Lematte, M., Leone, F. E., Lessinger, J. -M., Letrou, S., Lindau, S., Loiez, A., Louadah, B., Lucht, A., Ludes, P. O., Mabilat, C., Magalhaes, E., Mairesse, J., Malissin, I., Mancia, C., Manivet, P., Maquigneau, N., Martin-Levevre, L., Marx, G., Marx, N., Massat, S., Mebazaa, A., Megarbane, B., Meier, B., Meier-Hellmann, A., Meinig, T., Mercier, E., Messika, J., Metzger, C., Meybohm, P., Meyer, A., Meziani, F., Mourvillier, B., Muller, J., Mutlak, H., Navarin, S., Neuville, M., Nierhaus, A., Nouaille, M., Orru, M., Oueslati, H., Papendorp, S., Pascal, J., Perbet, S., Petre, H., Pezechk, J., Pichon, N., Pickkers, P., Pierre, V., Pottecher, J., Quatrocchi, D., Quattrochi, D., Rabouel, Y., Radji, S., Radjou, A., Rahmani, H., Reignier, J., Renard, S., Ricard, J. -D., Ringeis, G., Rinket, M., Robert, A., Robin, L., Rodier, N., Rolhion, C., Rommer, M., Roovers, N., Roszyk, L., Rouleau, S., Rousseau, C., Rouve, E., Roux, D., Ruimy, A., Russo, V., Salmon, C., Schedler, D., Schindler, A., Schnell, D., Schreiber, J., Schroder, D., Schuerholz, T., Schwope, K., Scigalla, P., Sebastien, L., Sensen, B., Siedler, S., Siewecke, A., Simeon-Vieules, V., Simon, T. -P., Simona, S., Singer, B., Soffker, G., Sonneville, R., Soyer, B., Struck, J., Szozot, M., Thibault, S., Thirifays, A., Thomas-Ruddel, D., Timsit, J. -F., Trine, H., Trof, R. J., Vallecoccia, M. S., Van Der Hoeven, H., Van Wezel, H., Varchetta, A., Verlhac, C., Vermeijden, J., Victori, G., Vignon, P., Vinatier, I., Vinetti, M., Voicu, S., Wetsch, W., Wichmann, D., Wittebole, X., Yehia, A., Zacharowski, K. D., Zanquila, M., Zapatero, D. C., Zinzonni, V. E., Zoccoli, G.   +274 more
core   +1 more source

CGRP Receptor Family and Accessory Protein Localization: Implications for Predicted Function

The Scientific World Journal, 2001
Calcitonin gene-related peptide (CGRP), adrenomedullin, amylin, and calcitonin are functionally related neuropeptides. Certain of these peptides mediate their action through receptors which have common components, such as the receptor activity modifying ...
K.R. Oliver
doaj   +1 more source

Adrenomedullin and its receptors are expressed in mouse pancreatic β-cells and suppresses insulin synthesis and secretion.

PLoS ONE, 2022
Gestational diabetes mellitus (GDM) is associated with defective pancreatic β-cell adaptation in pregnancy, but the underlying mechanism remains obscure.
Yuanlin Dong, Simone Hernandez Ruano, Akansha Mishra, Kathleen A Pennington, Chandrasekhar Yallampalli   +4 more
doaj   +1 more source

Differential roles of calcitonin family peptides in the dendrite formation and spinogenesis of the cerebral cortex in vitro [PDF]

, 2011
We examined roles of calcitonin family peptides in the initial stages of dendrite formation and the maturation of dendritic spines in the rat cerebral cortex in vitro.
Harigai Yuichi, Li Fei, Natsume Masaki, Ohtani Akiko, Senzaki Kouji, Shiga Takashi, 先崎 浩次, 志賀 隆   +7 more
core   +1 more source

The ADMR receptor mediates the effects of adrenomedullin on pancreatic cancer cells and on cells of the tumor microenvironment. [PDF]

PLoS ONE, 2009
Adrenomedullin (AM) is highly expressed in pancreatic cancer and stimulates pancreatic cancer cells leading to increased tumor growth and metastasis. The current study examines the role of specific AM receptors on tumor and cells resembling the tumor ...
Vijaya Ramachandran, Thiruvengadam Arumugam, Robert Langley, Rosa F Hwang, Pablo Vivas-Mejia, Anil K Sood, Gabriel Lopez-Berestein, Craig D Logsdon   +7 more
doaj   +1 more source

Calcitonin gene-related peptide (CGRP) receptors are important to maintain cerebrovascular reactivity in chronic hypertension. [PDF]

PLoS ONE, 2015
Cerebral blood flow autoregulation (CA) shifts to higher blood pressures in chronic hypertensive patients, which increases their risk for brain damage. Although cerebral vascular smooth muscle cells express the potent vasodilatatory peptides calcitonin ...
Zhenghui Wang, Belén Cantó Martorell, Thomas Wälchli, Olga Vogel, Jan Fischer, Walter Born, Johannes Vogel   +6 more
doaj   +1 more source

Accelerated Development With Increased Bone Mass and Skeletal Response to Loading Suggest Receptor Activity Modifying Protein-3 as a Bone Anabolic Target

Frontiers in Endocrinology, 2022
Knockout technologies provide insights into physiological roles of genes. Studies initiated into endocrinology of heteromeric G protein-coupled receptors included deletion of receptor activity modifying protein-3, an accessory protein that alters ligand ...
Suruchi Pacharne, Matthew Livesey, Mahita Kadmiel, Ning Wang, Kathleen M. Caron, Gareth O. Richards, Tim M. Skerry   +6 more
doaj   +1 more source

The role of ECL2 in CGRP receptor activation: a combined modelling and experimental approach [PDF]

, 2013
The calcitonin gene-related peptide (CGRP) receptor is a complex of a calcitonin receptor-like receptor (CLR), which is a family B G-protein-coupled receptor (GPCR) and receptor activity modifying protein 1.
Alex C. Conner, Barwell J, Bruck Taddese, Christopher A. Reynolds, Conner AC, David R. Poyner, Debbie L. Hay, Harriet A. Watkins, James Barwell, Kevin J. Smith, Michael. J. Woolley, Urano D, Watkins HA, Z. Gamze Karakullukcu   +13 more
core   +2 more sources

Reassessing the adrenomedullin scavenging function of ACKR3 in lymphatic endothelial cells.

PLoS ONE, 2023
Atypical chemokine receptor 3 (ACKR3) is a scavenger of the chemokines CXCL11 and CXCL12 and of several opioid peptides. Additional evidence indicates that ACKR3 binds two other non-chemokine ligands, namely the peptide hormone adrenomedullin (AM) and ...
Elena C Sigmund, Aline Bauer, Barbara D Jakobs, Hazal Tatliadim, Carlotta Tacconi, Marcus Thelen, Daniel F Legler, Cornelia Halin   +7 more
doaj   +1 more source