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Journal articles on the topic 'GCAP1'

Author: Grafiati

Published: 11 March 2023

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1

Ames, James B. "Structural Insights into Retinal Guanylate Cyclase Activator Proteins (GCAPs)." International Journal of Molecular Sciences 22, no. 16 (2021): 8731. http://dx.doi.org/10.3390/ijms22168731.

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Retinal guanylate cyclases (RetGCs) promote the Ca2+-dependent synthesis of cGMP that coordinates the recovery phase of visual phototransduction in retinal rods and cones. The Ca2+-sensitive activation of RetGCs is controlled by a family of photoreceptor Ca2+ binding proteins known as guanylate cyclase activator proteins (GCAPs). The Mg2+-bound/Ca2+-free GCAPs bind to RetGCs and activate cGMP synthesis (cyclase activity) at low cytosolic Ca2+ levels in light-activated photoreceptors. By contrast, Ca2+-bound GCAPs bind to RetGCs and inactivate cyclase activity at high cytosolic Ca2+ levels foun

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Vinberg, Frans, Teemu T. Turunen, Hanna Heikkinen, Marja Pitkänen, and Ari Koskelainen. "A novel Ca2+-feedback mechanism extends the operating range of mammalian rods to brighter light." Journal of General Physiology 146, no. 4 (2015): 307–21. http://dx.doi.org/10.1085/jgp.201511412.

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Sensory cells adjust their sensitivity to incoming signals, such as odor or light, in response to changes in background stimulation, thereby extending the range over which they operate. For instance, rod photoreceptors are extremely sensitive in darkness, so that they are able to detect individual photons, but remain responsive to visual stimuli under conditions of bright ambient light, which would be expected to saturate their response given the high gain of the rod transduction cascade in darkness. These photoreceptors regulate their sensitivity to light rapidly and reversibly in response to

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3

Avesani, Anna, Laura Bielefeld, Nicole Weisschuh, et al. "Molecular Properties of Human Guanylate Cyclase-Activating Protein 3 (GCAP3) and Its Possible Association with Retinitis Pigmentosa." International Journal of Molecular Sciences 23, no. 6 (2022): 3240. http://dx.doi.org/10.3390/ijms23063240.

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The cone-specific guanylate cyclase-activating protein 3 (GCAP3), encoded by the GUCA1C gene, has been shown to regulate the enzymatic activity of membrane-bound guanylate cyclases (GCs) in bovine and teleost fish photoreceptors, to an extent comparable to that of the paralog protein GCAP1. To date, the molecular mechanisms underlying GCAP3 function remain largely unexplored. In this work, we report a thorough characterization of the biochemical and biophysical properties of human GCAP3, moreover, we identified an isolated case of retinitis pigmentosa, in which a patient carried the c.301G>

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Peshenko, Igor V., Elena V. Olshevskaya, and Alexander M. Dizhoor. "GUCY2D mutations in retinal guanylyl cyclase 1 provide biochemical reasons for dominant cone–rod dystrophy but not for stationary night blindness." Journal of Biological Chemistry 295, no. 52 (2020): 18301–15. http://dx.doi.org/10.1074/jbc.ra120.015553.

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Mutations in the GUCY2D gene coding for the dimeric human retinal membrane guanylyl cyclase (RetGC) isozyme RetGC1 cause various forms of blindness, ranging from rod dysfunction to rod and cone degeneration. We tested how the mutations causing recessive congenital stationary night blindness (CSNB), recessive Leber's congenital amaurosis (LCA1), and dominant cone–rod dystrophy-6 (CORD6) affected RetGC1 activity and regulation by RetGC-activating proteins (GCAPs) and retinal degeneration-3 protein (RD3). CSNB mutations R666W, R761W, and L911F, as well as LCA1 mutations R768W and G982VfsX39, disa

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5

Howes, K. A. "GCAP1 rescues rod photoreceptor response in GCAP1/GCAP2 knockout mice." EMBO Journal 21, no. 7 (2002): 1545–54. http://dx.doi.org/10.1093/emboj/21.7.1545.

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6

Gorczyca, Wojciech A., Marcin Kobiałka, Marianna Kuropatwa, and Ewa Kurowska. "Ca2+ differently affects hydrophobic properties of guanylyl cyclase-activating proteins (GCAPs) and recoverin." Acta Biochimica Polonica 50, no. 2 (2003): 367–76. http://dx.doi.org/10.18388/abp.2003_3691.

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Guanylyl cyclase-activating proteins (GCAPs) and recoverin are retina-specific Ca(2+)-binding proteins involved in phototransduction. We provide here evidence that in spite of structural similarities GCAPs and recoverin differently change their overall hydrophobic properties in response to Ca(2+). Using native bovine GCAP1, GCAP2 and recoverin we show that: i) the Ca(2+)-dependent binding of recoverin to Phenyl-Sepharose is distinct from such interactions of GCAPs; ii) fluorescence intensity of 1-anilinonaphthalene-8-sulfonate (ANS) is markedly higher at high [Ca(2+)](free) (10 microM) than at

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Dejda, Agnieszka, Izabela Matczak, and Wojciech A. Gorczyca. "p19 detected in the rat retina and pineal gland is a guanylyl cyclase-activating protein (GCAP)." Acta Biochimica Polonica 49, no. 4 (2002): 899–905. http://dx.doi.org/10.18388/abp.2002_3749.

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The Ca(2+)-dependent activation of retina-specific guanylyl cyclase (retGC) is mediated by guanylyl cyclase-activating proteins (GCAPs). Here we report for the first time detection of a 19 kDa protein (p19) with GCAP properties in extracts of rat retina and pineal gland. Both extracts stimulate synthesis of cGMP in rod outer segment (ROS) membranes at low (30 nM) but not at high (1 microM) concentrations of Ca(2+). At low Ca(2+), immunoaffinity purified p19 activates guanylyl cyclase(s) in bovine ROS and rat retinal membranes. Moreover, p19 is recognized by antibodies against bovine GCAP1 and,

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Imanishi, Yoshikazu, Lili Yang, Izabela Sokal, S?awomir Filipek, Krzysztof Palczewski, and Wolfgang Baehr. "Diversity of Guanylate Cyclase-Activating Proteins (GCAPs) in Teleost Fish: Characterization of Three Novel GCAPs (GCAP4, GCAP5, GCAP7) from Zebrafish (Danio rerio) and Prediction of Eight GCAPs (GCAP1-8) in Pufferfish (Fugu rubripes)." Journal of Molecular Evolution 59, no. 2 (2004): 204–17. http://dx.doi.org/10.1007/s00239-004-2614-y.

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9

Pennesi, M. E., K. A. Howes, W. Baehr, and S. M. Wu. "Guanylate cyclase-activating protein (GCAP) 1 rescues cone recovery kinetics in GCAP1/GCAP2 knockout mice." Proceedings of the National Academy of Sciences 100, no. 11 (2003): 6783–88. http://dx.doi.org/10.1073/pnas.1130102100.

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10

Payne, Annette M., Susan M. Downes, David A. R. Bessant, et al. "Genetic analysis of the guanylate cyclase activator 1B (GUCA1B) gene in patients with autosomal dominant retinal dystrophies: Table 1." Journal of Medical Genetics 36, no. 9 (1999): 691–93. http://dx.doi.org/10.1136/jmg.36.9.691.

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The guanylate cyclase activator proteins (GCAP1 and GCAP2) are calcium binding proteins which by activating Ret-GC1 play a key role in the recovery phase of phototransduction. Recently a mutation in theGUCA1A gene (coding for GCAP1) mapping to the 6p21.1 region was described as causing cone dystrophy in a British family. In addition mutations in Ret-GC1have been shown to cause Leber congenital amaurosis and cone-rod dystrophy. To determine whether GCAP2 is involved in dominant retinal degenerative diseases, the GCAP2 gene was screened in 400 unrelated subjects with autosomal dominant central a

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11

Bonì, Francesco, Valerio Marino, Carlo Bidoia, et al. "Modulation of Guanylate Cyclase Activating Protein 1 (GCAP1) Dimeric Assembly by Ca2+ or Mg2+: Hints to Understand Protein Activity." Biomolecules 10, no. 10 (2020): 1408. http://dx.doi.org/10.3390/biom10101408.

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The guanylyl cyclase-activating protein 1, GCAP1, activates or inhibits retinal guanylyl cyclase (retGC) depending on cellular Ca2+ concentrations. Several point mutations of GCAP1 have been associated with impaired calcium sensitivity that eventually triggers progressive retinal degeneration. In this work, we demonstrate that the recombinant human protein presents a highly dynamic monomer-dimer equilibrium, whose dissociation constant is influenced by salt concentration and, more importantly, by protein binding to Ca2+ or Mg2+. Based on small-angle X-ray scattering data, protein-protein docki

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Abbas, Seher, Valerio Marino, Laura Bielefeld, Karl-Wilhelm Koch та Daniele Dell’Orco. "Constitutive Activation of Guanylate Cyclase by the G86R GCAP1 Variant Is Due to “Locking” Cation-π Interactions that Impair the Activator-to-Inhibitor Structural Transition". International Journal of Molecular Sciences 21, № 3 (2020): 752. http://dx.doi.org/10.3390/ijms21030752.

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Guanylate Cyclase activating protein 1 (GCAP1) mediates the Ca2+-dependent regulation of the retinal Guanylate Cyclase (GC) in photoreceptors, acting as a target inhibitor at high [Ca2+] and as an activator at low [Ca2+]. Recently, a novel missense mutation (G86R) was found in GUCA1A, the gene encoding for GCAP1, in patients diagnosed with cone-rod dystrophy. The G86R substitution was found to affect the flexibility of the hinge region connecting the N- and C-domains of GCAP1, resulting in decreased Ca2+-sensitivity and abnormally enhanced affinity for GC. Based on a structural model of GCAP1,

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13

Marino, Valerio, Giuditta Dal Cortivo, Paolo Enrico Maltese, et al. "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 (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

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14

Roth, Nora, Christoph Faul, Christiane Dorn, et al. "Development of New Autoimmunity Against T Cell Antigens Derived From Retinal Proteins After Allogeneic Hematopoietic Cell Transplantation." Blood 120, no. 21 (2012): 3060. http://dx.doi.org/10.1182/blood.v120.21.3060.3060.

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Abstract Abstract 3060 Introduction: Graft versus host disease (GvHD) is mainly mediated by T cells recognizing major (MHC) and minor (miHAG) histocompatibility antigens (human leukocyte antigens and MHC-restricted epitopes, respectively). The clinical appearance of a GvHD affecting the central nervous system (CNS) and the retina as part of the CNS is rare and evidence is limited to single case reports. Some publications describe the development of new autoimmunity after hematopoietic cell transplantation (HCT) manifested as hemolytic anemia (AIHA), immune thrombocytopenia (ITP) or myasthenia

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15

Marino, Valerio, Alberto Borsatto, Farina Vocke, Karl-Wilhelm Koch, and Daniele Dell'Orco. "CaF2nanoparticles as surface carriers of GCAP1, a calcium sensor protein involved in retinal dystrophies." Nanoscale 9, no. 32 (2017): 11773–84. http://dx.doi.org/10.1039/c7nr03288a.

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16

Biasi, Amedeo, Valerio Marino, Giuditta Dal Cortivo, et al. "A Novel GUCA1A Variant Associated with Cone Dystrophy Alters cGMP Signaling in Photoreceptors by Strongly Interacting with and Hyperactivating Retinal Guanylate Cyclase." International Journal of Molecular Sciences 22, no. 19 (2021): 10809. http://dx.doi.org/10.3390/ijms221910809.

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Guanylate cyclase-activating protein 1 (GCAP1), encoded by the GUCA1A gene, is a neuronal calcium sensor protein involved in shaping the photoresponse kinetics in cones and rods. GCAP1 accelerates or slows the cGMP synthesis operated by retinal guanylate cyclase (GC) based on the light-dependent levels of intracellular Ca2+, thereby ensuring a timely regulation of the phototransduction cascade. We found a novel variant of GUCA1A in a patient affected by autosomal dominant cone dystrophy (adCOD), leading to the Asn104His (N104H) amino acid substitution at the protein level. While biochemical an

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17

Wilkie, Susan E., Inez Stinton, Phillippa Cottrill, et al. "Characterisation of two genes for guanylate cyclase activator protein (GCAP1 and GCAP2) in the Japanese pufferfish, Fugu rubripes." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1577, no. 1 (2002): 73–80. http://dx.doi.org/10.1016/s0167-4781(02)00413-x.

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18

Vladimirov, Vasiliy I., Viktoriia E. Baksheeva, Irina V. Mikhailova, et al. "A Novel Approach to Bacterial Expression and Purification of Myristoylated Forms of Neuronal Calcium Sensor Proteins." Biomolecules 10, no. 7 (2020): 1025. http://dx.doi.org/10.3390/biom10071025.

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N-terminal myristoylation is a common co-and post-translational modification of numerous eukaryotic and viral proteins, which affects their interaction with lipids and partner proteins, thereby modulating various cellular processes. Among those are neuronal calcium sensor (NCS) proteins, mediating transduction of calcium signals in a wide range of regulatory cascades, including reception, neurotransmission, neuronal growth and survival. The details of NCSs functioning are of special interest due to their involvement in the progression of ophthalmological and neurodegenerative diseases and thei

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19

Newbold, R. J., E. C. Raux, C. E. Walker, et al. "Why a new mutation in human GCAP1 causes retinal degeneration." Biochemical Society Transactions 28, no. 5 (2000): A380. http://dx.doi.org/10.1042/bst028a380a.

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20

Lim, Sunghyuk, Igor V. Peshenko, Alexander M. Dizhoor, and James B. Ames. "Structural Insights for Activation of Retinal Guanylate Cyclase by GCAP1." PLoS ONE 8, no. 11 (2013): e81822. http://dx.doi.org/10.1371/journal.pone.0081822.

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21

Surguchov, Andrei, J. Darin Bronson, Poulabi Banerjee, et al. "The Human GCAP1 and GCAP2 Genes Are Arranged in a Tail-to-Tail Array on the Short Arm of Chromosome 6 (p21.1)." Genomics 39, no. 3 (1997): 312–22. http://dx.doi.org/10.1006/geno.1996.4513.

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22

Sokal, Izabela, Ning Li, Irina Surgucheva, et al. "GCAP1(Y99C) Mutant Is Constitutively Active in Autosomal Dominant Cone Dystrophy." Molecular Cell 2, no. 1 (1998): 129–33. http://dx.doi.org/10.1016/s1097-2765(00)80121-5.

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23

Peshenko, Igor V., and Alexander M. Dizhoor. "Two clusters of surface-exposed amino acid residues enable high-affinity binding of retinal degeneration-3 (RD3) protein to retinal guanylyl cyclase." Journal of Biological Chemistry 295, no. 31 (2020): 10781–93. http://dx.doi.org/10.1074/jbc.ra120.013789.

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Retinal degeneration-3 (RD3) protein protects photoreceptors from degeneration by preventing retinal guanylyl cyclase (RetGC) activation via calcium-sensing guanylyl cyclase–activating proteins (GCAP), and RD3 truncation causes severe congenital blindness in humans and other animals. The three-dimensional structure of RD3 has recently been established, but the molecular mechanisms of its inhibitory binding to RetGC remain unclear. Here, we report the results of probing 133 surface-exposed residues in RD3 by single substitutions and deletions to identify side chains that are critical for the in

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Jiang, Li, Tansy Z. Li, Shannon E. Boye, William W. Hauswirth, Jeanne M. Frederick, and Wolfgang Baehr. "RNAi-Mediated Gene Suppression in a GCAP1(L151F) Cone-Rod Dystrophy Mouse Model." PLoS ONE 8, no. 3 (2013): e57676. http://dx.doi.org/10.1371/journal.pone.0057676.

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Peshenko, Igor V., Elena V. Olshevskaya, and Alexander M. Dizhoor. "Binding of Guanylyl Cyclase Activating Protein 1 (GCAP1) to Retinal Guanylyl Cyclase (RetGC1)." Journal of Biological Chemistry 283, no. 31 (2008): 21747–57. http://dx.doi.org/10.1074/jbc.m801899200.

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Peshenko, Igor V., Elena V. Olshevskaya, Sunghyuk Lim, James B. Ames, and Alexander M. Dizhoor. "Identification of Target Binding Site in Photoreceptor Guanylyl Cyclase-activating Protein 1 (GCAP1)." Journal of Biological Chemistry 289, no. 14 (2014): 10140–54. http://dx.doi.org/10.1074/jbc.m113.540716.

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27

Dell’Orco, Daniele, Stefan Sulmann, Patrick Zägel, Valerio Marino, and Karl-Wilhelm Koch. "Impact of cone dystrophy-related mutations in GCAP1 on a kinetic model of phototransduction." Cellular and Molecular Life Sciences 71, no. 19 (2014): 3829–40. http://dx.doi.org/10.1007/s00018-014-1593-4.

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28

Sokal, Izabela, Ning Li, Candice S. Klug, et al. "Calcium-sensitive Regions of GCAP1 as Observed by Chemical Modifications, Fluorescence, and EPR Spectroscopies." Journal of Biological Chemistry 276, no. 46 (2001): 43361–73. http://dx.doi.org/10.1074/jbc.m103614200.

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29

Yang, Sufang, Alexander Dizhoor, David J. Wilson, and Grazyna Adamus. "GCAP1, Rab6, and HSP27: Novel Autoantibody Targets in Cancer-Associated Retinopathy and Autoimmune Retinopathy." Translational Vision Science & Technology 5, no. 3 (2016): 1. http://dx.doi.org/10.1167/tvst.5.3.1.

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30

Lim, Sunghyuk, Igor V. Peshenko, Alexander M. Dizhoor, and James B. Ames. "Backbone 1H, 13C, and 15N resonance assignments of guanylyl cyclase activating protein-1, GCAP1." Biomolecular NMR Assignments 7, no. 1 (2012): 39–42. http://dx.doi.org/10.1007/s12104-012-9373-2.

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31

Pertzev, Alexandre, Teresa Duda, and Rameshwar K. Sharma. "Ca2+Sensor GCAP1: A Constitutive Element of the ONE-GC-Modulated Odorant Signal Transduction Pathway." Biochemistry 49, no. 34 (2010): 7303–13. http://dx.doi.org/10.1021/bi101001v.

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32

Coleman, Jason E., Yan Zhang, Gary A. J. Brown, and Susan L. Semple-Rowland. "Cone Cell Survival and Downregulation of GCAP1 Protein in the Retinas of GC1 Knockout Mice." Investigative Opthalmology & Visual Science 45, no. 10 (2004): 3397. http://dx.doi.org/10.1167/iovs.04-0392.

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33

Buch, Prateek K., Marija Mihelec, Phillippa Cottrill, et al. "Dominant Cone-Rod Dystrophy: A Mouse Model Generated by Gene Targeting of the GCAP1/Guca1a Gene." PLoS ONE 6, no. 3 (2011): e18089. http://dx.doi.org/10.1371/journal.pone.0018089.

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34

Jiang, Li, Dianna Wheaton, Grzegorz Bereta, et al. "A novel GCAP1(N104K) mutation in EF-hand 3 (EF3) linked to autosomal dominant cone dystrophy." Vision Research 48, no. 23-24 (2008): 2425–32. http://dx.doi.org/10.1016/j.visres.2008.07.016.

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35

Dell’Orco, Daniele, Petra Behnen, Sara Linse, and Karl-Wilhelm Koch. "Calcium binding, structural stability and guanylate cyclase activation in GCAP1 variants associated with human cone dystrophy." Cellular and Molecular Life Sciences 67, no. 6 (2010): 973–84. http://dx.doi.org/10.1007/s00018-009-0243-8.

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36

Newbold, R. J. "The destabilization of human GCAP1 by a proline to leucine mutation might cause cone-rod dystrophy." Human Molecular Genetics 10, no. 1 (2001): 47–54. http://dx.doi.org/10.1093/hmg/10.1.47.

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37

Abbas, Seher, Valerio Marino, Nicole Weisschuh, et al. "Neuronal Calcium Sensor GCAP1 Encoded by GUCA1A Exhibits Heterogeneous Functional Properties in Two Cases of Retinitis Pigmentosa." ACS Chemical Neuroscience 11, no. 10 (2020): 1458–70. http://dx.doi.org/10.1021/acschemneuro.0c00111.

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38

Nishiguchi, Koji M., Izabela Sokal, Lili Yang, et al. "A Novel Mutation (I143NT) in Guanylate Cyclase-Activating Protein 1 (GCAP1) Associated with Autosomal Dominant Cone Degeneration." Investigative Opthalmology & Visual Science 45, no. 11 (2004): 3863. http://dx.doi.org/10.1167/iovs.04-0590.

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39

Sokal, Izabela, William J. Dupps, Michael A. Grassi, et al. "A Novel GCAP1 Missense Mutation (L151F) in a Large Family with Autosomal Dominant Cone-Rod Dystrophy (adCORD)." Investigative Opthalmology & Visual Science 46, no. 4 (2005): 1124. http://dx.doi.org/10.1167/iovs.04-1431.

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Peshenko, Igor V., Elena V. Olshevskaya, Suxia Yao, Hany H. Ezzeldin, Steven J. Pittler, and Alexander M. Dizhoor. "Activation of Retinal Guanylyl Cyclase RetGC1 by GCAP1: Stoichiometry of Binding and Effect of New LCA-Related Mutations." Biochemistry 49, no. 4 (2010): 709–17. http://dx.doi.org/10.1021/bi901495y.

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Lim, Sunghyuk, Igor V. Peshenko, Elena V. Olshevskaya, Alexander M. Dizhoor, and James B. Ames. "Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State." Journal of Biological Chemistry 291, no. 9 (2015): 4429–41. http://dx.doi.org/10.1074/jbc.m115.696161.

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42

Sokal, Izabela, Annie E. Otto-Bruc, Irina Surgucheva, et al. "Conformational Changes in Guanylyl Cyclase-activating Protein 1 (GCAP1) and Its Tryptophan Mutants as a Function of Calcium Concentration." Journal of Biological Chemistry 274, no. 28 (1999): 19829–37. http://dx.doi.org/10.1074/jbc.274.28.19829.

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43

Dal Cortivo, Giuditta, Valerio Marino, Francesco Bonì, Mario Milani, and Daniele Dell'Orco. "Missense mutations affecting Ca2+-coordination in GCAP1 lead to cone-rod dystrophies by altering protein structural and functional properties." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1867, no. 10 (2020): 118794. http://dx.doi.org/10.1016/j.bbamcr.2020.118794.

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44

Wilkie, Susan E., Yang Li, Evelyne C. Deery, et al. "Identification and Functional Consequences of a New Mutation (E155G) in the Gene for GCAP1 That Causes Autosomal Dominant Cone Dystrophy." American Journal of Human Genetics 69, no. 3 (2001): 471–80. http://dx.doi.org/10.1086/323265.

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45

Olshevskaya, E. V., I. V. Peshenko, A. B. Savchenko, and A. M. Dizhoor. "Retinal Guanylyl Cyclase Isozyme 1 Is the Preferential In Vivo Target for Constitutively Active GCAP1 Mutants Causing Congenital Degeneration of Photoreceptors." Journal of Neuroscience 32, no. 21 (2012): 7208–17. http://dx.doi.org/10.1523/jneurosci.0976-12.2012.

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46

Peshenko, Igor V., Artur V. Cideciyan, Alexander Sumaroka, et al. "A G86R mutation in the calcium-sensor protein GCAP1 alters regulation of retinal guanylyl cyclase and causes dominant cone-rod degeneration." Journal of Biological Chemistry 294, no. 10 (2019): 3476–88. http://dx.doi.org/10.1074/jbc.ra118.006180.

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47

Stephen, Ricardo, Krzysztof Palczewski, and Marcelo C. Sousa. "The Crystal Structure of GCAP3 Suggests Molecular Mechanism of GCAP-linked Cone Dystrophies." Journal of Molecular Biology 359, no. 2 (2006): 266–75. http://dx.doi.org/10.1016/j.jmb.2006.03.042.

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48

Semple-Rowland, Susan L., Wojciech A. Gorczyca, Janina Buczylko, et al. "Expression of GCAP 1 and GCAP2 in the retinal degeneration (rd ) mutant chicken retina." FEBS Letters 385, no. 1-2 (1996): 47–52. http://dx.doi.org/10.1016/0014-5793(96)00345-6.

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49

Solessio, Eduardo, Shobana S. Mani, Nicolas Cuenca, Gustav A. Engbretson, Robert B. Barlow, and Barry E. Knox. "Developmental regulation of calcium-dependent feedback in Xenopus rods." Journal of General Physiology 124, no. 5 (2004): 569–85. http://dx.doi.org/10.1085/jgp.200409162.

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The kinetics of activation and inactivation in the phototransduction pathway of developing Xenopus rods were studied. The gain of the activation steps in transduction (amplification) increased and photoresponses became more rapid as the rods matured from the larval to the adult stage. The time to peak was significantly shorter in adults (1.3 s) than tadpoles (2 s). Moreover, adult rods recovered twice as fast from saturating flashes than did larval rods without changes of the dominant time constant (2.5 s). Guanylate cyclase (GC) activity, determined using IBMX steps, increased in adult rods f

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Hoylaerts, M. F., T. Manes, and J. L. Millán. "Allelic Amino Acid Substitutions Affect the Conformation and Immunoreactivity of Germ-Cell Alkaline Phosphatase Phenotypes." Clinical Chemistry 38, no. 12 (1992): 2493–500. http://dx.doi.org/10.1093/clinchem/38.12.2493.

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Abstract:

Abstract The gene encoding placental alkaline phosphatase (PLAP) displays a well-documented allelic polymorphism. Likewise, different phenotypes exist for the PLAP-related germ-cell alkaline phosphatase (GCAP). We investigated the extent to which various allelic GCAP positions are critical in determining the enzymatic, structural, and immunological properties of GCAP phenotypes. Three homozygous GCAP phenotypes [JEG3, BeWo, and wild-type (wt) GCAP] were analyzed and compared with a "core" GCAP mutant that contains the seven amino acid substitutions that are consistently different between PLAP

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