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Academic literature on the topic 'Guanylate cyclase activating protein1'

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Journal articles on the topic "Guanylate cyclase activating protein1"

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Pugh, Edward N., Teresa Duda, Ari Sitaramayya, and Rameshwar K. Sharma. "Photoreceptor Guanylate Cyclases: A Review." Bioscience Reports 17, no. 5 (October 1, 1997): 429–73. http://dx.doi.org/10.1023/a:1027365520442.

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Almost three decades of research in the field of photoreceptor guanylate cyclases are discussed in this review. Primarily, it focuses on the members of membrane-bound guanylate cyclases found in the outer segments of vertebrate rods. These cyclases represent a new guanylate cyclase subfamily, termed ROS-GC, which distinguishes itself from the peptide receptor guanylate cyclase family that it is not extracellularly regulated. It is regulated, instead, by the intracellularly-generated Ca2+ signals. A remarkable feature of this regulation is that ROS-GC is a transduction switch for both the low and high Ca2+ signals. The low Ca2+ signal transduction pathway is linked to phototransduction, but the physiological relevance of the high Ca2+ signal transduction pathway is not yet clear; it may be linked to neuronal synaptic activity. The review is divided into eight sections. In Section I, the field of guanylate cyclase is introduced and the scope of the review is briefly explained; Section II covers a brief history of the investigations and ideas surrounding the discovery of rod guanylate cyclase. The first five subsections of Section III review the experimental efforts to quantify the guanylate cyclase activity of rods, including in vitro and in situ biochemistry, and also the work done since 1988 in which guanylate cyclase activity has been determined. In the remaining three subsections an analytical evaluation of the Ca2+ modulation of the rod guanylate cyclase activity related to phototransduction is presented. Section IV deals with the issues of a biochemical nature: isolation and purification, subcellular localization and functional properties of rod guanylate cyclase. Section V summarizes work on the cloning of the guanylate cyclases, analysis of their primary structures, and determination of their location with in situ hybridization. Section VI summarizes studies on the regulation of guanylate cyclases, with a focus on guanylate cyclases activating proteins. In Section VII, the evidence about the localization and functional role of guanylate cyclases in other retinal cells, especially in “on-bipolar” cells, in which guanylate cyclase most likely plays a critical role in electrical signaling, is discussed. The review concludes with Section VIII, with remarks about the future directions of research on retinal guanylate cyclases.
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Yamazaki, Akio, Matsuyo Yamazaki, Russell K. Yamazaki, and Jiro Usukura. "Illuminated Rhodopsin Is Required for Strong Activation of Retinal Guanylate Cyclase by Guanylate Cyclase-Activating Proteins†." Biochemistry 45, no. 6 (February 2006): 1899–909. http://dx.doi.org/10.1021/bi0519396.

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HONKAWA, Hanayo, Osamu HISATOMI, Yoshihiro KISHIDA, and Fumio TOKUNAGA. "Two Guanylate Cyclase Activating Proteins in Medaka Retina." Interdisciplinary Information Sciences 8, no. 1 (2002): 25–32. http://dx.doi.org/10.4036/iis.2002.25.

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Baehr, Wolfgang, and Krzysztof Palczewski. "Focus on Molecules: Guanylate cyclase-activating proteins (GCAPs)." Experimental Eye Research 89, no. 1 (June 2009): 2–3. http://dx.doi.org/10.1016/j.exer.2008.12.016.

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Palczewski, Krzysztof, Izabela Sokal, and Wolfgang Baehr. "Guanylate cyclase-activating proteins: structure, function, and diversity." Biochemical and Biophysical Research Communications 322, no. 4 (October 2004): 1123–30. http://dx.doi.org/10.1016/j.bbrc.2004.07.122.

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Sokal, Izabela, Andrei Alekseev, and Krzysztof Palczewski. "Photoreceptor guanylate cyclase variants: cGMP production under control." Acta Biochimica Polonica 50, no. 4 (December 31, 2003): 1075–95. http://dx.doi.org/10.18388/abp.2003_3633.

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Changes in the Ca2+ concentration are thought to affect many processes, including signal transduction in a vast number of biological systems. However, only in few cases the molecular mechanisms by which Ca2+ mediates its action are as well understood as in phototransduction. In dark-adapted photoreceptor cells, the equilibrium level of cGMP is maintained by two opposing activities, such as phosphodiesterase (PDE) and guanylate cyclase (GC). Upon absorption of photons, rhodopsin-G-protein-mediated activation of PDE leads to a transient decrease in [cGMP] and subsequently to lowering of [Ca2+]. In turn, lower [Ca2+] increases net production of cGMP by stimulation of GC until dark conditions are re-established. This activation of GC is mediated by Ca2+ -free forms of Ca2+ -binding proteins termed GC-activating proteins (GCAPs). The last decade brought the molecular identification of GCs and GCAPs in the visual system. Recent efforts have been directed toward understanding the properties of GC at the physiological and structural levels. Here, we summarize the recent progress and present a list of topics of ongoing research.
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Rätscho, Nina, Alexander Scholten, and Karl-Wilhelm Koch. "Expression profiles of three novel sensory guanylate cyclases and guanylate cyclase-activating proteins in the zebrafish retina." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1793, no. 6 (June 2009): 1110–14. http://dx.doi.org/10.1016/j.bbamcr.2008.12.021.

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Shahu, Manisha Kumari, Fabian Schuhmann, Alexander Scholten, Ilia A. Solov’yov, and Karl-Wilhelm Koch. "The Transition of Photoreceptor Guanylate Cyclase Type 1 to the Active State." International Journal of Molecular Sciences 23, no. 7 (April 5, 2022): 4030. http://dx.doi.org/10.3390/ijms23074030.

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Membrane-bound guanylate cyclases (GCs), which synthesize the second messenger guanosine-3′, 5′-cyclic monophosphate, differ in their activation modes to reach the active state. Hormone peptides bind to the extracellular domain in hormone-receptor-type GCs and trigger a conformational change in the intracellular, cytoplasmic part of the enzyme. Sensory GCs that are present in rod and cone photoreceptor cells have intracellular binding sites for regulatory Ca2+-sensor proteins, named guanylate-cyclase-activating proteins. A rotation model of activation involving an α-helix rotation was described as a common activation motif among hormone-receptor GCs. We tested whether the photoreceptor GC-E underwent an α-helix rotation when reaching the active state. We experimentally simulated such a transitory switch by integrating alanine residues close to the transmembrane region, and compared the effects of alanine integration with the point mutation V902L in GC-E. The V902L mutation is found in patients suffering from retinal cone–rod dystrophies, and leads to a constitutively active state of GC-E. We analyzed the enzymatic catalytic parameters of wild-type and mutant GC-E. Our data showed no involvement of an α-helix rotation when reaching the active state, indicating a difference in hormone receptor GCs. To characterize the protein conformations that represent the transition to the active state, we investigated the protein dynamics by using a computational approach based on all-atom molecular dynamics simulations. We detected a swinging movement of the dimerization domain in the V902L mutant as the critical conformational switch in the cyclase going from the low to high activity state.
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Li, Ning, Robert N. Fariss, Kai Zhang, Annie Otto-Bruc, Francoise Haeseleer, Darin Bronson, Ning Qin, et al. "Guanylate-cyclase-inhibitory protein is a frog retinal Ca2+-binding protein related to mammalian guanylate-cyclase-activating proteins." European Journal of Biochemistry 252, no. 3 (March 15, 1998): 591–99. http://dx.doi.org/10.1046/j.1432-1327.1998.2520591.x.

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Marino, Valerio, Giuditta Dal Cortivo, Paolo Enrico Maltese, Giorgio Placidi, Elisa De Siena, Benedetto Falsini, Matteo Bertelli, and Daniele Dell’Orco. "Impaired Ca2+ Sensitivity of a Novel GCAP1 Variant Causes Cone Dystrophy and Leads to Abnormal Synaptic Transmission Between Photoreceptors and Bipolar Cells." International Journal of Molecular Sciences 22, no. 8 (April 14, 2021): 4030. http://dx.doi.org/10.3390/ijms22084030.

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Guanylate cyclase-activating protein 1 (GCAP1) is involved in the shutdown of the phototransduction cascade by regulating the enzymatic activity of retinal guanylate cyclase via a Ca2+/cGMP negative feedback. While the phototransduction-associated role of GCAP1 in the photoreceptor outer segment is widely established, its implication in synaptic transmission to downstream neurons remains to be clarified. Here, we present clinical and biochemical data on a novel isolate GCAP1 variant leading to a double amino acid substitution (p.N104K and p.G105R) and associated with cone dystrophy (COD) with an unusual phenotype. Severe alterations of the electroretinogram were observed under both scotopic and photopic conditions, with a negative pattern and abnormally attenuated b-wave component. The biochemical and biophysical analysis of the heterologously expressed N104K-G105R variant corroborated by molecular dynamics simulations highlighted a severely compromised Ca2+-sensitivity, accompanied by minor structural and stability alterations. Such differences reflected on the dysregulation of both guanylate cyclase isoforms (RetGC1 and RetGC2), resulting in the constitutive activation of both enzymes at physiological levels of Ca2+. As observed with other GCAP1-associated COD, perturbation of the homeostasis of Ca2+ and cGMP may lead to the toxic accumulation of second messengers, ultimately triggering cell death. However, the abnormal electroretinogram recorded in this patient also suggested that the dysregulation of the GCAP1–cyclase complex further propagates to the synaptic terminal, thereby altering the ON-pathway related to the b-wave generation. In conclusion, the pathological phenotype may rise from a combination of second messengers’ accumulation and dysfunctional synaptic communication with bipolar cells, whose molecular mechanisms remain to be clarified.
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Dissertations / Theses on the topic "Guanylate cyclase activating protein1"

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BONI', FRANCESCO. "GUANYLATE CYCLASE ACTIVATING PROTEIN 1 MONOMER-DIMER EQUILIBRIUM CONTROLLED BY CA2+ OR MG2+ BINDING: HINTS TO UNDERSTAND RETINAL GUANYLATE CYCLASE REGULATION." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/839565.

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Neuronal calcium sensors play a crucial role in different pathways of Ca2+-mediated neurotransmission. Among them guanylate cyclase-activating protein 1 (GCAP1) is expressed only in photoreceptors and activates or inhibits retinal guanylate cyclase 1 (retGC1) depending on cellular Ca2+ concentrations during phototransduction. To date, 22 pathogenic mutations responsible for retinal dystrophy have been associated to GCAP1, but a complete picture of the molecular determinants of the disease is still missing. The only crystal structure available so far is the wt Ca2+-bound monomeric homologue from chicken and no cure exists for retinal dystrophy. In this work I report for the first time that the recombinant human GCAP1 is characterized by a highly dynamic monomer-dimer equilibrium, whose dissociation constant is influenced by salt concentration and by the nature of the divalent ion bound. Surprisingly, I discovered that also the chicken protein shows a similar mechanism, suggesting that this property could be potentially functional for GCAP1 activity and conserved among different species. Despite the large number of crystallization trials, no diffracting crystal of the human GCAP1 was obtained, probably due to the flexible C-terminal tail and the intrinsic dynamicity of the protein. To overcome this issue, I produced a construct lacking the 12 C-term residues and stabilized by a disulfide bridge between the N- and C-term domains which was successfully crystallized. We showed that such engineered construct is able to regulate retGC1 as well as the wt protein. By combining SAXS, protein-protein docking and molecular dynamics simulation we propose two novel three-dimensional models of Ca2+-bound GCAP1 dimer which are stabilized by some of the residues involved in the interaction with the retGC1. We used a biophysical and biochemical approach to thoroughly investigate three pathogenic variants (D100G, E155A and E155G) characterized by mutations in residues directly involved in Ca2+-coordination. All the three variants were able to form oligomers in solutions, showing a decreased affinity for Ca2+ and constitutively activating retGC1 at physiological calcium concentrations. Besides local structural effects, the mutations perturb also the oligomeric state of GCAP1 suggesting that the multimeric assembly of the protein could affect its proper biological function. A recombinant baculovirus for the expression of the cytoplasmic domain of retGC1 in insect cells was produced with the aim to get atomic structural information on the GCAP1/retGC1 complex. This will facilitate the identification of drug candidates able to recognize the binding region of the pathogenic GCAP1 mutants with the cyclase and to competitively inhibit the constitutive retGC1 activation, restoring the homeostasis of second messengers which is impaired in retinal degenerative diseases. A preliminary molecular docking based on the crystal structure of the chicken protein was performed and I identified four molecules able to bind the wt human GCAP1 in the millimolar/micromolar range. Together these results shed new light on the quaternary assembly of the wt human GCAP1, showing how the structural changes related to the presence of Ca2+ or Mg2+ are reflected in the different measured dimerization constant. Such conformational changes are in turn likely related to the regulatory mechanism of GCAP1 in the modulation of the retGC1 activity. The differences between the oligomerization state of D100G, E155G and E155A variants suggest a correlation between the altered quaternary assembly of GCAP1 and the aberrant activity of the mutants, representing a step forward to dissect the structural bases of the altered regulatory mechanism of GCAP1 in retinal dystrophies.
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Krylov, Dmitri M. "Guanylyl cyclase activating protein-1 and its regulation of retinal guanylyl cyclases : a study by molecular biological methods and a novel mass spectrometry based method /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/9259.

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Stephen, Ricardo H. "Structural characterization of guanylate cyclase activating proteins, calcium ion-dependent regulators of phototransduction." Connect to online resource, 2008. 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:3303874.

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Hwang, Ji-Young. "Biochemical and biophysical studies on guanylate cyclase activating protein 1, a Ca2+-sensor in Phototransduction." [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=962777412.

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López, del Hoyo Natalia. "Role of Guanylate Cyclase Activating Proteins in photoreceptor cells of the retina in health and disease." Doctoral thesis, Universitat de Barcelona, 2014. http://hdl.handle.net/10803/283566.

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In the last two decades, it has been done a thoroughly research about the role of Guanylate Cyclase Activating Proteins (GCAPs) in photoreceptor cells of the retina as activity regulators of Retinal Guanylate Cyclase (RetGC), which allow to restore cGMP levels to darkness ones when intracellular Ca2+ falls. However, little is known about: a) ¿What determines GCAPs distribution within the cell?, b) ¿Which other functions GCAP proteins, GCAP1 and GCAP2, carry out at other cellular compartments different from the sensory one? and c) ¿How they cause cell death when they are mutated? In this study we want address these questions. 1. First of all, we own a mouse model that expresses a GCAP2 mutated form unable to bind Ca2+ (bEF-GCAP2). Other mutations described for GCAP1 and present in some autosomic dominant Cone Rod Dystrophies (adCORD), prevent Ca2+ binding to some of its EF-hand domains which produces the constitutive activation of RetGC, and consequently, high cGMP levels that result in toxicity for the cell. However, we observe that our model causes the death by other mechanism, as RetGC is not activated by GCAP2, because GCAP2 is retained in the inner segment and does not translocate to the sensory compartment. We want to identify interactions that GCAP2 establish differentially in this compartment and could be retaining it. We find out 14-3-3 family of proteins by mass-spectrometry and liquid chromatography. Furthermore, bEF-GCAP2 is abnormally phosphorylated in vivo and GCAP2 phosphorylation promotes its binding to 14-3-3 binding. We demonstrate that GCAP2 phosphorylation in residue serine 201 is the cause of its retention in the inner segment, avoiding its translocation to the outer segment, and when we mutate serine 201 into a glycine, this retention is reverted in vivo. Finally, we propose that GCAP2 phosphorylation and its binding to 14-3-3 is what retains GCAP2 in the inner segment, and this happens in a balance way during dark/light day cycles. When this system overloads will cause retinal degeneration by the formation of aggregates. We believe that mutations in GCAP2 or light conditions promoting GCAP2 accumulation in its Ca2+-free form in the inner segment of the cell, bring to cell death by GCAP2 conformational instability. Most important, we propose that this will also apply for genetic scenarios mimicking the effects to constant light exposure, the so called “equivalent-light” scenarios. 2. Secondly, as a result of the identification of GCAP2 interaction to RIBEYE (Venkatesan et al. 2010) the major component of synaptic ribbons in the photoreceptor cell terminal, we developed an ultrastructural study of the role that GCAP2 may play in this compartment. Through confocal and electronic microscopy we have demonstrated the presence of GCAP1 and GCAP2 in rod synaptic ribbons. However, GCAP1 and GCAP2 are not necessary during synaptic ribbons assembling and basic maintenance. As GCAP2 overexpression in the wildtype background (which means a higher GCAP2:GCAP1 ratio) promotes ribbons disassembling, we propose that GCAP2 may play a role mediating the morphological changes that take place in the synaptic ribbons in response to variations in [Ca2+].
En las dos últimas décadas se ha investigado a fondo el papel que juegan las Proteínas Activadoras de Guanilato Ciclasa (GCAPs) en las células fotorreceptor de la retina como proteínas encargadas de regular la actividad de la Guanilato Ciclasa (GC). Sin embargo se sabe poco acerca de: a) ¿Qué determina la distribución de GCAPs en la célula?, b) ¿Qué otras funciones ejercen GCAP1 y GCAP2 en otros compartimentos celulares distintos al segmento sensorial? y c) ¿Cómo dan lugar a muerte celular cuando están mutadas? En este estudio hemos querido encarar estas preguntas. 1. En primer lugar, poseemos un modelo de ratón que expresa una forma mutante de GCAP2 que no une Ca2+ (bEF-GCAP2). A diferencia de otras mutaciones descritas para GCAP1, en que se ha observado que la muerte celular es producida por niveles tóxicos de cGMP, observamos que nuestro modelo produce la muerte celular por otro mecanismo en que GCAP2 se acumula en el segmento interno. Identificamos abundantemente las distintas isoformas de 14-3-3 como interactores diferenciales de bEF-GCAP2, que a su vez está anormalmente fosforilada in vivo. Tras una serie de experimentos para caracterizar esta interacción, proponemos que la fosforilación de GCAP2 y su unión a 14-3-3 retienen a GCAP2 en el segmento interno, y si este mecanismo se sobrecarga por a) mutaciones en GCAP2, b) condiciones de luz que promuevan la acumulación de GCAP2 en su forma libre de Ca2+ en el segmento interno o c) condiciones genéticas que mimeticen los efectos de exposición a luz prolongada, tendría lugar la degeneración de la retina por la formación de agregados debido a la inestabilidad conformacional de GCAP2. 2. En segundo lugar, tras la identificación de la interacción de GCAP2 con RIBEYE (Venkatesan et al. 2010), el componente mayoritario de las cintillas sinápticas de fotorreceptores, realizamos un estudio ultrastructural del papel que puede estar jugando GCAP2 en este compartimento mediante microscopia electrónica y confocal, demostrando la presencia de GCAP1 y GCAP2 en las cintillas sinápticas de bastones. GCAP1 y GCAP2 son prescindibles en el ensamblaje y mantenimiento básico de las cintillas sinápticas, pero la sobreexpresión de GCAP2 en el fenotipo salvaje, que incrementa el ratio GCAP2:GCAP1, promueve el desensamblaje de las cintillas. Proponemos que GCAP2 podría jugar un papel mediando cambios morfológicos en las cintillas sinápticas promovidas por cambios en [Ca2+].
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Faria, Wagner Mendes 1972. "Caracterização farmacológica do ativador da guanilato ciclase solúvel, BAY 60-2770, em artéria pulmonar isolada de coelho." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/309253.

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Orientador: Fabíola Taufic Monica Iglesias
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Ciências Médicas
Made available in DSpace on 2018-08-23T16:27:39Z (GMT). No. of bitstreams: 1 Faria_WagnerMendes_M.pdf: 1252281 bytes, checksum: ad80513967190699e0001046decc7731 (MD5) Previous issue date: 2013
Resumo: Duas classes de medicamentos denominadas estimuladores e ativadores da guanilato ciclase solúvel (GCs) foram desenvolvidas para uso terapêutico em situações patológicas onde há menor formação ou biodisponibilidade NO ou tolerância farmacológica. A GCs é uma enzima heterodímera, composta pelas subunidades alfa (?) e beta (?), nas quais há a presença do grupo prostético heme e que catalisa a conversão da guanosina trifosfato (GTP) em guanosina monofosfato cíclico (GMPc) pela ação do NO. Em situações patológicas o átomo de ferro pode encontrar-se na sua forma oxidada (Fe3+), diminuindo assim a resposta máxima do óxido nítrico (NO). A principal diferença entre os moduladores da GCs é que os ativadores (BAY 58-2667, HMR 1766, BAY 60-2770) atuam de maneira mais eficaz mesmo quando a enzima encontra-se no estado oxidado. O objetivo do presente trabalho foi caracterizar funcionalmente o relaxamento induzido pelo BAY 60-2770 em artéria pulmonar isolada de coelho. O BAY 60-2770 (0,0001-100 ?M) relaxou de maneira potente (10,1 ± 0.04) e eficaz (105 ± 0,9 %) a artéria pulmonar, sendo este efeito significativamente potencializado na presença dos inibidores da GCs (ODQ, 10 ?M, 4,9 vezes), da fosfodiesterase tipo 5 (tadalafil, 100 ?M, 5,6 vezes) ou da sintase de óxido nítrico (LNAME, 100 ?M, 3,0 vezes). A presença do sequestrador de NO, do doador de NO, da indometacina, do bloqueador do canal de potássio ou a remoção endotelial não interferiram no relaxamento induzido pelo BAY 60-2770. A fenilefrina (0,00001-3 mM) e a estimulação elétrica (4-16 Hz) produziram contração dependente da concentração e frequência, respectivamente. Na presença de tetrodotoxina (TTX, 1 ?M) e fentolamina (1 ?M) houve abolição da resposta contrátil a estimulação elétrica, mostrando a liberação neurogênica de catecolamina. Na presença de BAY 60-2770 co-incubado com ODQ uma redução significativa na contração induzida pela estimulação elétrica foi observada. Apesar desta mesma redução ter sido observada na presença do L-NAME, a mesma não foi estatisticamente significante em comparação aos anéis incubados somente com BAY 60-2770 (1 ?M). Nossos resultados mostraram que a oxidação do grupamento heme, a inibição da fosfodiesterase e a ausência do NO favoreceram a resposta relaxante do BAY 60-2770
Abstract: Soluble guanylate cyclase (sGC) stimulators and activators have been developed for use in pathophysiological condition when NO formation or bioavailability are impaired or when NO tolerance gas developed. Soluble guanylate cyclase is a heterodimer enzyme composed by alpha (?) and beta (?) subunits and a prostetic heme group. Soluble guanylate cyclase converts guanosine triphosphate (GTP) into cyclic guanosine monophosphate (GMPc) after nitric oxide (NO) activaton. Under pathophysiological conditions heme can be oxidized (Fe3+), thus reduzing NO efficacy. The main difference between stimulators and activators (BAY 58-2667, BAY 60-2770 and HMR 1766) is that the latter class of drugs is more efficacious when heme is oxidized. The aim of the present study is to characterize the relaxation induced by BAY 60-2770 in isolated pulmonary artery from rabbit. BAY 60-2770 (0.0001-100 ?M) produced concentration dependent relaxation with potency and maxima response values of 10,1 ± 0.04 and 105 ± 0.9%, respectively. The inhibition of sGC (ODQ, 10 ?M) or phosphodiesterase type 5 (tadalafil, 100 ?M) or the nitric oxide synthase (L-NAME, 100 ?M) produced significantly leftward shifts by, approximately, 4.9, 5.4 and 3.0, respectively. The NO-scavenger, the NO-donor, the cyclooxygenase inhibition, the potassium channel blocker or endothelial removal did not interfere on the pharmacological parameters of BAY 60-2770. Phenylephrine (PE, 0.0001- 3 mM) and electrical field stimulation (EFS, 4-16 Hz) induced concentration and frequency dependent-contraction, respectively. Phentolamine (1 ?M) and tetrodotoxin (TTX, 1 ??) practically abolished EFS-induced contraction, showing the neurogenic source of catecholamines. Co-treatment with BAY 60-2770 with ODQ reduced significantly the EFS-induced contraction in comparison with BAY 60- 2770 (1 ?M) alone. Although we have observed a tendency of reduction in the amplitude of contraction when BAY 60-2770 was co-incubated with L-NAME, it was not statistically significant. Therefore, our results showed that the oxidation of heme group, the inhibition of phosphodiesterase and lower levels of NO favoured the relaxing response of BAY 60- 2770 in isolated rabbit pulmonary artery
Mestrado
Farmacologia
Mestre em Farmacologia
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Guo, Beichu. "Interaction of PKCbeta with CARMA1 mediates B cell receptor-induced NF-kappaB activation /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/8348.

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Hwang, Ji-Young [Verfasser]. "Biochemical and biophysical studies on guanylate cyclase activating protein 1, a Ca2+-sensor in Phototransduction / vorgelegt von Ji-Young Hwang." 2001. http://d-nb.info/962777412/34.

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Book chapters on the topic "Guanylate cyclase activating protein1"

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Newbold, Richard J., Evelyne C. Deery, Annette M. Payne, Susan E. Wilkie, David M. Hunt, and Martin J. Warren. "Guanylate Cyclase Activating Proteins, Guanylate Cyclase and Disease." In Advances in Experimental Medicine and Biology, 411–38. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0121-3_25.

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Baehr, Wolfgang, Iswari Subbaraya, Wojciech A. Gorczyca, and Krzysztof Palczewski. "Guanylate Cyclase-Activating Protein (GCAP)." In Degenerative Diseases of the Retina, 339–47. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1897-6_38.

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Koch, Karl-Wilhelm. "GCAP (Guanylate Cyclase–Activating Protein)." In Encyclopedia of Signaling Molecules, 2041–45. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_12.

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Koch, Karl-Wilhelm. "GCAP (Guanylate Cyclase–Activating Protein)." In Encyclopedia of Signaling Molecules, 1–5. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_12-1.

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Meigs, Thomas E., Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, et al. "GCAP (Guanylate Cyclase–Activating Protein)." In Encyclopedia of Signaling Molecules, 769–73. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_12.

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Koch, Karl-Wilhelm. "Target Recognition of Guanylate Cyclase By Guanylate Cyclase-Activating Proteins." In Advances in Experimental Medicine and Biology, 349–60. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0121-3_21.

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Ames, James B., Mitsuhiko Ikura, and Lubert Stryer. "[8] Molecular structure of membrane-targeting calcium sensors in vision: Recoverin and guanylate cyclase-activating protein 2." In Methods in Enzymology, 121–32. Elsevier, 2000. http://dx.doi.org/10.1016/s0076-6879(00)16720-5.

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Pal, Biswajit, and Teizo Kitagawa. "Resonance Raman Studies of the Activation Mechanism of Soluble Guanylate Cyclase." In The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins, 540–63. Elsevier, 2008. http://dx.doi.org/10.1016/b978-044452839-1.50021-8.

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Sitaramayya, Ari, Nikolay Pozdnyakov, Alexander Margulis, and Akiko Yoshida. "[48] Calcium-dependent activation of membrane guanylate cyclase by S100 proteins." In Methods in Enzymology, 730–42. Elsevier, 2000. http://dx.doi.org/10.1016/s0076-6879(00)15878-1.

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Becker, Richard C., and Frederick A. Spencer. "Aggrenox and Cilostazol." In Fibrinolytic and Antithrombotic Therapy. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195155648.003.0015.

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Abstract:
The dipyridamole component of Aggrenox and cilostazol, both phosphodiesterase inhibitors, are used predominantly in patients with peripheral vascular and cerebrovascular disease. Aggrenox is a combination platelet antagonist that includes aspirin (25 mg) and dipyridamole (200 mg extended-release preparation). It is typically taken twice daily. Aspirin’s mechanism of action has been discussed previously. Dipyridamole inhibits cyclic adenosine monophosphate (cAMP)-phosphodiesterase (PDE) and cyclic-3´, 5´- guanylate monophospate (GMP)-PDE (Bunag et al., 1964). The pharmacokinetic profile of aspirin has been summarized previously. Peak dipyridamole levels in plasma are achieved within several hours of oral administration (400 mg dose of Aggrenox). Extensive metabolism via conjugation with glucuronic acid occurs in the liver. There are no significant pharmacokinetic interactions between aspirin and dipyridamole coadministered as Aggrenox. Dipyridamole inhibits platelet aggregation by two distinct mechanisms. First, it attenuates adenosine uptake into platelets (as well as endothelial cells and erythrocytes). The resulting increase elicits a rise in cellular adenylate cyclase concentrations, resulting in elevated cAMP levels, which inhibit platelet activation to several agonists, including adenosine diphosphate (ADP), collagen, and platelet-activating factor. Dipyridamole also inhibits PDE. The subsequent increase in cAMP elevates nitric oxide concentration, facilitating platelet inhibitory potential (Eisert, 2001). The European Stroke Prevention Study (ESPS)-2 reported that 79.9% of patients experienced at least one on-treatment adverse event. The most common side effects were gastrointestinal complaints and headache. Dipyridamole has vasodilatory effects and should be used with caution in patients with severe coronary artery disease in whom episodes of angina pectoris may increase. Patients receiving Aggrenox should not be given adenosine for myocardial perfusion studies. Plasma concentrations of dipyridamole are approximately 40% higher in patients greater than 65 years of age compared with younger individuals. Aggrenox has not been studied in patients with acute coronary syndrome (ACS). The ESPS-2 included 6,602 patients with ischemic stroke (76% of the total population) or transient ischemic attack who were randomized to receive Aggrenox, dipyridamole alone, aspirin alone, or placebo. Aggrenox reduced the risk of stroke by 22.1% compared with aspirin and by 24.4% compared with dipyridamole. Both differences were statistically significant (p = .008 and p = .002, respectively) (Diener et al., 1996).
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