Binding, coupling, and mRNA subtype heterogeneity of α1-adrenergic receptors in cultured human RPE

Moroi, Sayoko E.; Earley, O; Hirakata, Akito; Caron, Marc G.; Jaffe, Glenn J.

doi:10.1016/s0014-4835(05)80067-3

Cited by 8 publications

(5 citation statements)

References 20 publications

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“…There is evidence for both pertussis toxin-sensitive and -insensitive coupling to the PLC signal transduction pathway in human RPE cells. Epinephrine-stimulated phosphoinositide hydrolysis in RPE cells is inhibited completely by pertussis toxin pretreatment (Moroi-Fetters et al, 1995), whereas the response to carbachol is unaffected (Osborne et al, 1991). In light of the evidence for P2Y 2 receptor coupling to both pertussis toxin-sensitive and -insensitive G proteins in other systems, P2Y 2 receptor coupling to more than one type of G protein in RPE cells seems likely.…”

Section: Discussionmentioning

confidence: 95%

Identification and characterization of P2Y2 nucleotide receptors in human retinal pigment epithelial cells

et al. 1997

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P2 nucleotide receptor expression in cultured human retinal pigment epithelial (RPE) cells was investigated using the photoaffinity ATP analog BzATP, polymerase chain reaction of reverse-transcribed RNA (RT-PCR) and fura-2 fluorescence measurement of changes in intracellular free calcium concentration ([Ca2+]i). In experiments carried out in RPE cells at passage 10-15, addition of micromolar concentrations of ATP, UTP, and ATPgammaS to RPE cells resulted in a rapid, transient 3.5-fold increase in [Ca2+]i followed by a prolonged elevation that was twofold above the original baseline. Similar results were obtained from cells at passage 2. Characteristics of nucleotide-stimulated calcium mobilization in RPE cells, including partial inhibition by pertussis toxin, suggest that a G protein-coupled receptor mediates this response. Consistent with the expression of a P2Y2 nucleotide receptor subtype in RPE cells, [alpha-32P]BzATP labeled a 53-kDa protein in plasma membranes, and RT-PCR revealed the presence of P2Y2 receptor RNA. Adenosine had no effect on [Ca2+]i in RPE cells, indicating that the A2 subtype of P1 receptor described previously in human RPE is not involved in the response to nucleotides. Together the results indicate that human RPE cells express functional P2Y2 nucleotide receptors.

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Section: Discussionmentioning

confidence: 95%

Identification and characterization of P2Y2 nucleotide receptors in human retinal pigment epithelial cells

et al. 1997

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“…In vivo studies have revealed that alpha‐1 ARs are involved in the regulation of intraocular pressure (IOP) in rabbits and monkeys (Kiuchi et al ., 1992; Nishimura et al ., 1993; Wang et al ., 1997; Zhan et al ., 1998; Okada & Gregory, 2001). Moreover, alpha‐1 ARs have been found to regulate cellular functions in cultured endothelial cells from various ocular regions in several species (Walkenbach et al ., 1992; Moroi‐Fetters et al ., 1995; Ryan et al ., 1998). However, which subtype(s) of alpha‐1 AR is involved in the ocular functions remains to be clarified.…”

Section: Introductionmentioning

confidence: 99%

Distribution of alpha‐1 adrenoceptor subtypes in RNA and protein in rabbit eyes

Suzuki

Taniguchi

Nakamura

et al. 2002

British J Pharmacology

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1 We investigated subtypes of alpha-1 adrenoceptor (AR) in rabbit ocular tissues using reverse transcription-polymerase chain reaction (RT ± PCR), in situ hybridization (ISH) and binding studies. 2 Competitive RT ± PCR assays speci®c for the subtypes of alpha-1 AR revealed that the mRNA expression of alpha-1a AR was dominant, and that of each alpha-1b and alpha-1d was less than 10% and 0.5% of total alpha-1 ARs mRNA, respectively, in the iris, ciliary body, choroid and retina. 3 In alpha-1a AR splice isoform-speci®c RT ± PCR assays, we found a distinct proportion of each isoform mRNA in the iris, ciliary body and choroid. 4 The results of the ISH assays for alpha-1a AR subtype showed that hybridization signals were clearly observed in the iris dilator muscle and in the epithelium of the ciliary processes. 5 In binding studies, alpha-1A AR was a dominant subtype in the iris, choroid and retina in contrast to the ciliary body that had more alpha-1B than alpha-1A AR subtype at protein level.

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“…[Please note that after revision of the nomenclature, the α "c -adrenoceptor is currently denoted the α "a -adrenoceptor (Bylund et al, 1994 ;Ford et al, 1994 ;Hieble et al, 1995)]. However, in cultured human retinal pigment epithelial cells mRNA's encoding only the α "b -and α "d -adrenoceptors were detected (Moroi-Fetters et al, 1995).…”

Section: Introductionmentioning

confidence: 99%