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  • 1
    Electronic Resource
    Electronic Resource
    Rod outer segment membrane guanylate cyclase type 1 (ROS-GC1) gene: Structure, organization and regulation by phorbol ester, a protein kinase C activator (1998)
    Springer
    Molecular and cellular biochemistry 189 (1998), S. 63-70 
    Details
    ISSN: 1573-4919
    Keywords: guanylate cyclase ; ROS-GC1 gene regulation ; retina ; protein kinase C
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract At present there are two recognized members of the ROS-GC subfamily of membrane guanylate cyclases. They are ROS-GC1 and ROS-GC2. A distinctive feature of this family is that its members are not switched on by the extracellular peptide hormones; instead, they are modulated by intracellular Ca2+ signals, consistent to their linkage with phototransduction. An intriguing feature of ROS-GC1, which distinguishes it from ROS-GC2, is that it has two Ca2+ switches. One switch inhibits the enzyme at micromolar concentrations of Ca2+, as in phototransduction; the other, stimulates. The stimulatory switch, most likely, is linked to retinal synaptic activity. Thus, ROS-GC1 is linked to both phototransduction and the synaptic activity. The present study describes (1) the almost complete structural identity of 18.5 kb ROS-GC1 gene; (2) its structural organization: the gene is composed of 20 exons and 19 introns with classical GT/AG boundaries; (3) the activity of the ROS-GC1 promoter assayed through luciferase reporter in COS cells; and (4) induction of the gene by phorbol ester, a protein kinase C (PKC) activator. The co-presence of PKC and ROS-GC1 in photoreceptors suggests that regulation of the ROS-GC1 gene by PKC might be a physiologically relevant phenomenon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006944629935
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular and pharmacological identity of the α2D-adrenergic receptor subtype in bovine retina and its photoreceptors (1996)
    Springer
    Molecular and cellular biochemistry 159 (1996), S. 129-138 
    Details
    ISSN: 1573-4919
    Keywords: bovine α2D-adrenergic receptor ; pharmacology ; retina ; photoreceptors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The rat cA2-47 gene encodes the pharmacologically defined α2D-adrenergic receptor (α2D-AR) subtype. Previously, the expression of its mRNA was shown in bovine retina by amplification through the reverse transcription-polymerase chain reaction (RT-PCR) of a region corresponding to the rat α2D-AR, amino acid (aa) residues 382–439, indicating the presence of this subtype in this neural tissue. In the present study, the structure of this gene has been probed and the encoded receptor subtype has been characterized in bovine retina and its photoreceptor cells. The deduced as sequence of the two bovine gene fragments, aa residues 290–375 and as residues 392–434, demonstrates 77% overall identity with the rat α2D AR subtype and 80% overall identity with the mouse α2D-AR. The receptor encoded by the bovine gene was expressed in the retina and its photoreceptors with the typical pharmacological characteristics established for the rat (α2D-AR subtype: The receptor bound rauwolscine with a KD of 14 nM in the retina and with that of 19 nM in the photoreceptor cells; the binding association rate constant, k+1, for the ligand was 0.012 min−1, the dissociation rate constant, k−1, was 0.14 min−1 and the half-time for dissociation was 5 min. Oxymetazoline displaced the bound [3H]-rauwolscine with an EC50 value of 85 nM, while SK & F 104078, and prazosin displaced the bound [3H]-rauwolscine with the respective IC50 values of 900 nM and 3000 nM. The other α2-AR subtypes − α2B-AR, α2C-AR — were not detected in the retina and its photoreceptors. Thus, this study shows that the bovine α2D AR gene is a structural variant of the rat and mouse genes, that the bovine gene encodes the typical pharmacologically defined α2D-AR. subtype, that this subtype is present in its exclusive form in the bovine retina and its photoreceptors, where it may be presynaptic in nature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00420915
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  • 3
    Electronic Resource
    Electronic Resource
    The bovine α2D-adrenergic receptor gene: Structure, expression in retina, and pharmacological characterization of the encoded receptor (1997)
    Springer
    Molecular and cellular biochemistry 177 (1997), S. 113-123 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract This report describes cloning of the bovine α2D-adrenergic receptor (α_2D-AR) gene and determination of the transcription start site, unequivocal presence of the α2D-AR transcript in the retina, and pharmacological characteristics of the encoded product. Furthermore, expression of the gene in selected bovine tissues has also been scrutinized. A genomic clone was isolated from λ EMBL3 library and a 3 kb fragment was subcloned and sequenced. This fragment contained the putative TATA box and the coding region. The encoded receptor was transiently expressed in COS cells. The recombinant receptor expressed pharmacological characteristics almost identical to the wild-type bovine retinal receptor, which were typical of the α2D-AR subtype. RNase protection analysis confirmed the expression of the gene in the retina. The bovine receptor was structurally close to its rat analogue which also encodes the α2D-AR, but, the highest homology was observed with the porcine receptor expressing α2A-AR pharmacological characteristics. Certain structural features of the bovine gene were unique to itself and not shared by any other α2-AR subtype. Among the tissues tested using reverse transcriptase-polymerase chain reaction (RT-PCR), the α2D-AR message was the most abundant in retina, followed by the brain and olfactory lobe. Thus, the availability of the bovine receptor gene probe will become an important additional tool in the elucidation of molecular mechanisms behind the α2D-AR physiology in neurosensory processes such as those occurring in the eye and the brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006830303140
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  • 4
    Electronic Resource
    Electronic Resource
    A role for amino acid residues in the third cytoplasmic loop in defining the ligand binding characteristics of the α2D-adrenergic receptor (1997)
    Springer
    Molecular and cellular biochemistry 177 (1997), S. 125-129 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract In this report, 5 amino acid residues (aa) in the third cytoplasmic loop of the α2D-adrenergic receptor are identified which (individually or together) alter its ligand-binding characteristics. An important structural discrepancy exists in the third cytoplasmic loop of the α2D-ARs encoded by the rat cDNA and the rat gene - five aa are different. The newly identified bovine receptor as well as the mouse receptor contained the 5 aa identical to that encoded by the rat cDNA. Site-directed mutation of these residues to those of the rat gene encoded receptor resulted in alteration of binding characteristics: significant changes in the ability of the mutant receptor to bind to a number of agonists and antagonists were observed - ranging from a decrease by half in the case of oxymetazoline, to near total loss of binding in the case of prasozin. Thus, the mutant receptor was no longer pure α2D-AR. This indicated a hitherto unrealized role of the third cytoplasmic loop in defining the ligand-binding characteristics of the receptor, and also suggested that the rat gene sequence was most probably in error.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006882319978
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  • 5
    Electronic Resource
    Electronic Resource
    Three dimensional atomic model and experimental validation for the ATP-regulated module (ARM) of the atrial natriuretic factor receptor guanylate cyclase (2000)
    Springer
    Molecular and cellular biochemistry 214 (2000), S. 7-14 
    Details
    ISSN: 1573-4919
    Keywords: ANF-RGC ; ATP ; ARM ; allosteric regulation ; phosphorylation ; three-dimensional model
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Atrial natriuretic factor (ANF) receptor guanylate cyclase (ANF-RGC) is a single chain transmembrane-spanning protein, containing both ANF binding and catalytic activities. ANF binding to the extracellular receptor domain activates the cytosolic catalytic domain, generating the second messenger cyclic GMP. Obligatory in this activation process is an intervening transduction step, which is regulated by the binding of ATP to the cyclase. The partial structural motif of the ATP binding domain of the cyclase has been elucidated and has been termed ATP Regulatory Module (ARM). The crystal structures of the tyrosine kinase domains of the human insulin receptor and haematopoietic cell kinase were used to derive a homology-based model of the ARM domain of ANF-RGC. The model identifies the precise configuration of the ATP-binding pocket in the ARM domain, accurately represents its ATP-dependent features, and shows that the ATP-dependent transduction phenomenon is a two-step mechanism. In the first step, ATP binds to its pocket and changes its configuration; in the second step, via an unknown protein kinase, it phosphorylates the cyclase for its full activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007144328682
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  • 6
    Electronic Resource
    Electronic Resource
    Juvenile hormone action to suppress gene transcription and influence message stability (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 323-332 
    Details
    ISSN: 0192-253X
    Keywords: mRNA stability ; mRNA translatability ; metamorphosis ; gene regulation ; hexamerins ; storage proteins ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Proteins normally expressed in high abundance only at larval-pupal metamorphosis in Trichoplusia ni were examined in a comparative analysis of the role and level of hormonal control of their expression. Some related proteins in the hemocyanin-superfamily (i.e., an acidic protein [AJHSP1] and two basic proteins [BJHSP1, BJHSP2]) were shown by nuclear run-on analysis to be specifically transcriptionally suppressed by juvenile hormone (JH), while transcription of another member of that family which is also metamorphosis-associated (arylphorin) was not specifically sensitive to JH. The stability of the mRNA for those members transcriptionally down-regulated by JH appeared to decrease under high JH conditions. While each protein was resorbed to some extent by the prepupal fat body, only the two basic proteins were quantitatively cleared from prepupal hemolymph. The JH-sensitive proteins studied appear to be encoded in single copy genes not immediately juxtaposed in the genome. These and previous studies now permit a more comprehensive understanding of the different combinations of mechanisms involving transcription, mRNA stability, translation, and protein clearance that operate to regulate these metamorphosis-associated proteins. © 1993Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140410
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  • 7
    Electronic Resource
    Electronic Resource
    Regulation of juvenile hormone esterase gene transcription by juvenile hormone (1994)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 15 (1994), S. 391-400 
    Details
    ISSN: 0192-253X
    Keywords: Juvenile hormone ; juvenile hormone esterase ; transcription ; Trichoplusiani ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Juvenile hormone (JH) is a major hormone regulating insect development. We have obtained a cDNA and a genomic clone for juvenile hormone esterase (JHE), the enzyme that is involved in the degradation of juvenile hormone and which is critical for insect development. Analysis of the regulation of JHE during the final larval stadium in the cabbage looper, Trichoplusia ni, showed that the JHE mRNA levels are maximal on days 2 and 4 of the final stadium. Nuclear run-on analyses demonstrated that changes in JHE mRNA levels are primarily due to changes in the transcription rate of the gene, which may be a single copy in the genome. Treatment with a JH analog resulted in induction of JHE gene transcription, which could be detected within three hours after treatment. Salient features present in the 5′ flanking region of this JH-sensitive gene are presented, including the presence of sequences closely resembling binding sites for members of the family of nuclear receptors. This report is the first direct demonstration, by nuclear run-on analysis, of JH induction of gene transcription. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020150502
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