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Cyp27c1 Red-Shifts the Spectral Sensitivity of Photoreceptors by Converting Vitamin A1 into A2.
Enright JM, Toomey MB, Sato SY, Temple SE, Allen JR, Fujiwara R, Kramlinger VM, Nagy LD, Johnson KM, Xiao Y, How MJ, Johnson SL, Roberts NW, Kefalov VJ, Guengerich FP, Corbo JC
(2015) Curr Biol 25: 3048-57
MeSH Terms: Amphibian Proteins, Animals, Cytochrome P-450 Enzyme System, Infrared Rays, Photoreceptor Cells, Vertebrate, Rana catesbeiana, Transcriptome, Visual Perception, Vitamin A, Zebrafish, Zebrafish Proteins
Show Abstract · Added March 14, 2018
Some vertebrate species have evolved means of extending their visual sensitivity beyond the range of human vision. One mechanism of enhancing sensitivity to long-wavelength light is to replace the 11-cis retinal chromophore in photopigments with 11-cis 3,4-didehydroretinal. Despite over a century of research on this topic, the enzymatic basis of this perceptual switch remains unknown. Here, we show that a cytochrome P450 family member, Cyp27c1, mediates this switch by converting vitamin A1 (the precursor of 11-cis retinal) into vitamin A2 (the precursor of 11-cis 3,4-didehydroretinal). Knockout of cyp27c1 in zebrafish abrogates production of vitamin A2, eliminating the animal's ability to red-shift its photoreceptor spectral sensitivity and reducing its ability to see and respond to near-infrared light. Thus, the expression of a single enzyme mediates dynamic spectral tuning of the entire visual system by controlling the balance of vitamin A1 and A2 in the eye.
Copyright © 2015 Elsevier Ltd. All rights reserved.
0 Communities
1 Members
0 Resources
11 MeSH Terms
Cloning and chromosomal mapping of the murine norepinephrine transporter.
Fritz JD, Jayanthi LD, Thoreson MA, Blakely RD
(1998) J Neurochem 70: 2241-51
MeSH Terms: Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cattle, Chromosome Mapping, Cloning, Molecular, DNA, Complementary, Exons, Humans, Introns, Mice, Molecular Sequence Data, Norepinephrine, Norepinephrine Plasma Membrane Transport Proteins, Placenta, Polymerase Chain Reaction, Rana catesbeiana, Rats, Species Specificity, Symporters
Show Abstract · Added July 10, 2013
The norepinephrine (NE) transporter (NET), a target of many clinically prescribed antidepressants, regulates noradrenergic neurotransmission by efficiently clearing NE from synaptic spaces after release. To advance our understanding of NET gene structure, regulation, and potential associations with complex behavioral trait loci, we amplified a mouse norepinephrine transporter (mNET) cDNA from placenta total RNA and utilized mNET probes to isolate and characterize the mNET gene. Inferred translation of the major open reading frame of the mNET cDNA predicts a 617-amino acid protein with 12 putative membrane-spanning regions and 94% identity to human NET. The coding exons of the mNET cDNA were found to be spread across >36 kb of 129/Svj genomic DNA, with exon-intron boundaries bearing consensus gt/ag splice sites. Sequence upstream (202 bp) of the inferred translation initiation site matched the sequence of 5' rapid amplification of cDNA ends products from brain mRNA with no evidence for intervening introns and is preceded by a TATA box and canonical transcriptional regulatory elements that may play a role in mNET expression in vivo. Probes derived from mNET cDNA identified species-specific MspI restriction fragment length variations within the mNET gene that were utilized to position the gene (Slc6a5) to murine chromosome 8, one recombinant distal to D8Mit15. This site is within a recently defined quantitative trait locus defined for ethanol sensitivity in LSXSS recombinant inbred mice, Lore4. The status of Slc6a5 as a candidate gene for alcohol sensitivity is discussed with respect to studies noting ethanol-induced alterations in brain NE receptors, NE receptor-linked adenylate cyclase, and NE transport.
1 Communities
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21 MeSH Terms
Structural diversity in the catecholamine transporter gene family: molecular cloning and characterization of an L-epinephrine transporter from bullfrog sympathetic ganglia.
Blakely RD, Apparsundaram S
(1998) Adv Pharmacol 42: 206-10
MeSH Terms: Amphibian Proteins, Animals, Base Sequence, Binding, Competitive, Carrier Proteins, Cloning, Molecular, Conserved Sequence, Dopamine Uptake Inhibitors, Epinephrine, Ganglia, Sympathetic, Genetic Variation, HeLa Cells, Humans, Kinetics, Models, Structural, Multigene Family, Neurons, Norepinephrine, Protein Structure, Secondary, Rana catesbeiana, Recombinant Proteins, Transfection
Added July 10, 2013
1 Communities
1 Members
0 Resources
22 MeSH Terms
Molecular cloning and characterization of an L-epinephrine transporter from sympathetic ganglia of the bullfrog, Rana catesbiana.
Apparsundaram S, Moore KR, Malone MD, Hartzell HC, Blakely RD
(1997) J Neurosci 17: 2691-702
MeSH Terms: Amino Acid Sequence, Amphibian Proteins, Animals, Base Sequence, Carrier Proteins, Cattle, Cloning, Molecular, Conserved Sequence, DNA Primers, Dopamine Plasma Membrane Transport Proteins, Epinephrine, Ganglia, Sympathetic, HeLa Cells, Humans, Kinetics, Membrane Glycoproteins, Membrane Transport Proteins, Mice, Molecular Sequence Data, Nerve Tissue Proteins, Norepinephrine Plasma Membrane Transport Proteins, Organ Specificity, Polymerase Chain Reaction, Rana catesbeiana, Rats, Recombinant Proteins, Sequence Homology, Amino Acid, Serotonin Plasma Membrane Transport Proteins, Symporters, Transfection
Show Abstract · Added July 10, 2013
Chemical signaling by dopamine (DA) and L-norepinephrine (L-NE) at synapses is terminated by uptake via specialized presynaptic transport proteins encoded by the DA transporter (DAT) and L-NE transporter (NET) genes, respectively. In some vertebrate neurons, particularly the sympathetic neurons of amphibians, L-NE is converted to L-epinephrine (L-Epi, adrenaline) and released as the primary neurotransmitter. Although evidence exists for a molecularly distinct L-Epi transporter (ET) in the vertebrate brain and peripheral nervous system, a transporter specialized for extracellular L-Epi clearance has yet to be identified. To pursue this issue, we cloned transporter cDNAs from bullfrog (Rana catesbiana) paravertebral sympathetic ganglia and characterized functional properties via heterologous expression in non-neuronal cells. A cDNA of 2514 bp (fET) was identified for which the cognate 3.1 kb mRNA is highly enriched in frog sympathetic ganglia. Sequence analysis of the fET cDNA reveals an open reading frame coding for a protein of 630 amino acids. Inferred fET protein sequence bears 75, 66, and 48% amino acid identity with human NET, DAT, and the 5-hydroxytryptamine transporter (SERT), respectively. Transfection of fET confers Na+- and Cl--dependent catecholamine uptake in HeLa cells. Uptake of [3H]-L-NE by fET is inhibited by catecholamines in a stereospecific manner. L-Epi and DA inhibit fET-mediated [3H]-L-NE uptake more potently than they inhibit [3H]-L-NE uptake by human NET (hNET), whereas L-NE exhibits equivalent potency between the two carriers. Moreover, fET exhibits a greater maximal velocity (Vmax) for the terminal products of catecholamine biosynthesis (L-Epi > L-NE > DA), unlike hNET, in which a Vmax rank order of L-NE > DA > L-Epi is observed. fET-mediated transport of catecholamines is sensitive to cocaine and tricyclic antidepressants, with antagonist potencies significantly correlated with hNET inhibitor sensitivity. Amino acid conservation and divergence of fET with mammalian catecholamine transporters help define residues likely to be involved in catecholamine recognition and translocation as well as blockade by selective reuptake inhibitors.
1 Communities
2 Members
0 Resources
30 MeSH Terms
Protein complement of rod outer segments of frog retina.
Hamm HE, Bownds MD
(1986) Biochemistry 25: 4512-23
MeSH Terms: Animals, Cell Separation, Centrifugation, Density Gradient, Electrophoresis, Polyacrylamide Gel, Molecular Weight, Photoreceptor Cells, Povidone, Proteins, Rana catesbeiana, Rod Cell Outer Segment, Silicon Dioxide
Show Abstract · Added December 10, 2013
Rod outer segments (ROS) from frog retina have been purified by Percoll density gradient centrifugation, a procedure that preserves their form and intactness. One- and two-dimensional electrophoretic analysis reveals a smaller number of proteins than is observed in many cell organelles and permits quantitation of the 20 most abundant polypeptides. Rhodopsin accounts for 70% of the total protein (3 X 10(9) copies/outer segment), and approximately 70 other polypeptides are present at more than 6 X 10(4) copies/outer segment. Another 17% of the total protein is accounted for by the G-protein (3 X 10(8) copies/outer segment) that links rhodopsin bleaching and the activation of cyclic GMP phosphodiesterase (PDE). The phosphodiesterase accounts for 1.5% of the protein (1.5 X 10(7) copies/outer segment), and a 48,000-dalton component that binds to the membrane in the light accounts for a further 2.6%. The function of approximately 90% of the total protein in the outer segment is known, and two-thirds of the non-rhodopsin protein is accounted for by enzyme activities associated with cyclic GMP metabolism. The relative molar abundance of rhodopsin, G-protein, and PDE is 100:10:1. Apart from these major membrane-associated proteins, most of the other proteins are cytosolic. Thirteen other polypeptides are found at an abundance of one or more copies per 1000 rhodopsins, nine soluble and four membrane-bound, and their abundance relative to rhodopsin has been quantitated. ROS have been separated into subcellular fractions which resolve three classes of soluble, extrinsic membrane, and integral membrane proteins. A listing of the proteins that are phosphorylated and their subcellular localization is given. Approximately 25 phosphopeptides are detected, and most are in the soluble fraction. Fewer phosphorylated proteins are associated with the purified outer segments than with crude ROS. Distinct patterns of phosphorylation are associated with intact rods incubated with [32P]Pi and broken rods incubated with [gamma-32P]ATP.
0 Communities
1 Members
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11 MeSH Terms