Adenylated Dinucleotide Binding to the Adenosine 5′,5′′′-P1,P4-Tetraphosphate Mouse Heart Receptor

Hilderman, Richard H.; Lilien, Jack; Zimmerman, James K.; Tate, D.H.; Dimmick, M.A.; Jones, Graham B.

doi:10.1006/bbrc.1994.1514

Cited by 21 publications

(14 citation statements)

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“…Molecular modeling of Ap 4A reveals a looped hairpin-like structure with two distinct cavities and three hydrophilic regions (baseϪphosphasteϪbase) in a parallel orientation. Modeling of Ap 5A also reveals a looped orientation [21]. The structural similarities of Ap 4 A and Ap 5 A are consistent with their affinities for the receptor, clone A phage amino acid insert, and RGS.…”

Section: Discussionsupporting

confidence: 52%

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A peptide isolated from a random phage peptide library is a structural mimic to the P¹, P⁴‐diadenosine 5′‐tetraphosphate binding site on its receptor

Hilderman

Liu

Zimmerman

1998

European Journal of Biochemistry

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Section: Discussionsupporting

confidence: 52%

“…We have demonstrated in cardiac tissue that Ap 4 A appears to act on a unique dipurinoceptor which is highly specific for Ap 4 A, Ap 5 A, and Ap 6 A (P 2D ) [20]. This receptor undergoes an activation step which enhances only Ap 4 A binding [21]. Other investigators have demonstrated the presence on rat brain synaptosomes of a P 2D purinoceptor [18].…”

mentioning

confidence: 80%

A peptide isolated from a random phage peptide library is a structural mimic to the P¹, P⁴‐diadenosine 5′‐tetraphosphate binding site on its receptor

Hilderman

Liu

Zimmerman

1998

European Journal of Biochemistry

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“…A receptor that specifically binds adenine dinucleotides rather than ATP has been isolated from Swiss CDl mice cardiac muscle membranes (Walker et al, 1993b;Hilderman et al, 1994). Unfortunately, no functional study has been carried out to determine what action this receptor mediates.…”

Section: Degradation Of Nucleotides By Atrial Tissuementioning

confidence: 99%

“…Unfortunately, no functional study has been carried out to determine what action this receptor mediates. This receptor, isolated from membrane fractions, has a molecular weight of 30 kDa, and is derived from a protein whose post-translational processing, involving a serine protease, yields precursors of 67, 55 and 42 kDa (Walker & Hilderman, 1993;Walker et al, 1993b;Hilderman et al, 1994). However, in intact cardiac myocytes the 42 kDa form of the receptor predominates, and it has been suggested that the conversion of the 42 kDa to the 30 kDa form is an artefact (Walker et al, 1993a).…”

Section: Degradation Of Nucleotides By Atrial Tissuementioning

confidence: 99%

The activation of P₁‐ and P₂‐purinoceptors in the guinea‐pig left atrium by diadenosine polyphosphates

Hoyle

Зиганшин

Pintor

et al. 1996

British J Pharmacology

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1 The effects of P', P2-di(adenosine) pyrophosphate (AP2A), P',P3-di(adenosine) triphosphate (AP3A), P',P"-di(adenosine) tetraphosphate (AP4A), P',P5-di(adenosine) pentaphosphate (AP5A), ATP, a,,Bmethylene ADP and 2-chloroadenosine (2-ClAd) were examined in the guinea-pig driven left atrium.2 All these purine compounds except a,#-methylene ADP produced a negative inotropic response with a rank order of potency of: 2-ClAd > > AP2A > ATP > AP4A = AP3A = AP5A. The ECs, value for 2-ClAd was approximately 1 guM, while those for the remaining compounds were in the range 10 guM-100 MM, a,f,-Methylene ADP (10-300 gM), a selective P2Y-purinoceptor agonist, produced a small positive inotropism.3 The P1-purinoceptor antagonist, 8-para-sulphophenyltheophylline 20 gM) caused a rightward shift in the concentration-response curves for 2-ClAd, ATP and AP2A, but converted the responses of AP3A, AP4A, and AP5A into positive inotropisms.4 The non-selective P2-purinoceptor antagonist, suramin (300 gM), had no significant effect on the concentration-response curves for 2-ClAd, ATP or AP2A, but significantly antagonized inhibitory responses to AP3A, AP4A and AP5A, and excitatory responses to a,,B-methylene ADP.5 In the presence of 8-pSPT (20 gM), suramin (300 gM) abolished the positive inotropic responses evoked by the dinucleotides. 6 ATP was degraded far more rapidly than any of the dinucleotides, and AP3A was the least stable of the diadenosine compounds. The relative order of stability was AP2A > AP4A = AP5A > AP3A > > ATP.Suramin (300 gM) reduced the rate of degradation of ATP and AP3A by approximately 30%. Suramin had no significant effect on the degradation of AP2A, AP4A or AP5A.7 It is concluded that the diadenosine polyphosphates cause negative inotropic responses via PIpurinoceptors and a hitherto undefined suramin-sensitive P2-purinoceptor, and that they appear to have positive inotropic effects mediated via another suramin-sensitive P2-purinoceptor.

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“…Finally the involvement of specific diadenosine polyphosphate receptors must be considered. Such a receptor for diadenosine polyphosphates was identified in membrane extracts of different mouse tissues including brain, heart, liver, spleen, kidney, muscle and fat [24,25].…”

Section: Systemic Hemodynamicsmentioning

confidence: 99%

Effects of Diadenosine Polyphosphates on Systemic and Regional Hemodynamics in Anesthetized Rats

Khattab

Hohage²,

Hollah³

et al. 1998

Kidney Blood Press Res

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Diadenosine polyphoshates (Ap4A, Ap5A, Ap6A) induce vasodilatation or vasoconstriction in various isolated vessels and influence central and peripheral hemodynamics. The influence of diadenosine polyphoshates on hemodynamics was studied in anesthetized rats in vivo. Mean arterial blood pressure (MABP) and heart rate (HR) measured in the carotid artery decreased with Ap4A, Ap5A and Ap6A. Renal blood flow (RBF), femoral blood flow (FBF) and cardiac output (CO) were evaluated by an ultrasonic transit-time method. Renal superficial blood flow (RSBF) was measured by laser Doppler flowmetry. CO, RBF and RSBF were decreased initially by all three diadenosine polyphosphates. FBF was also slightly decreased. Total peripheral (TPR), renal (RVR) and femoral (FVR) vascular resistances were calculated. TPR was transiently increased by the dinucleotides following by a decrease. RVR and, to a lesser extent, FVR were also increased. These data show that diadenosine polyphosphates have effects on both the heart and the peripheral blood vessels. The effects on the heart and MABP were dominated by bradycardia and hypotension. In the kidney, diadenosine polyphosphates induced a predominant vascoconstriction. The effects on skeletal muscle blood flow were much smaller. Thus, the three diadenosine polyphosphates studied differ in the effects on heart and peripheral vessels.

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Adenylated Dinucleotide Binding to the Adenosine 5′,5′′′-P1,P4-Tetraphosphate Mouse Heart Receptor

Cited by 21 publications

References 0 publications

A peptide isolated from a random phage peptide library is a structural mimic to the P¹, P⁴‐diadenosine 5′‐tetraphosphate binding site on its receptor

A peptide isolated from a random phage peptide library is a structural mimic to the P¹, P⁴‐diadenosine 5′‐tetraphosphate binding site on its receptor

The activation of P₁‐ and P₂‐purinoceptors in the guinea‐pig left atrium by diadenosine polyphosphates

Effects of Diadenosine Polyphosphates on Systemic and Regional Hemodynamics in Anesthetized Rats

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Adenylated Dinucleotide Binding to the Adenosine 5′,5′′′-P1,P4-Tetraphosphate Mouse Heart Receptor

Cited by 21 publications

References 0 publications

A peptide isolated from a random phage peptide library is a structural mimic to the P1, P4‐diadenosine 5′‐tetraphosphate binding site on its receptor

A peptide isolated from a random phage peptide library is a structural mimic to the P1, P4‐diadenosine 5′‐tetraphosphate binding site on its receptor

The activation of P1‐ and P2‐purinoceptors in the guinea‐pig left atrium by diadenosine polyphosphates

Effects of Diadenosine Polyphosphates on Systemic and Regional Hemodynamics in Anesthetized Rats

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A peptide isolated from a random phage peptide library is a structural mimic to the P¹, P⁴‐diadenosine 5′‐tetraphosphate binding site on its receptor

A peptide isolated from a random phage peptide library is a structural mimic to the P¹, P⁴‐diadenosine 5′‐tetraphosphate binding site on its receptor

The activation of P₁‐ and P₂‐purinoceptors in the guinea‐pig left atrium by diadenosine polyphosphates