Identification of a unique membrane receptor for adenosine 5‘,5“‘-P1,P4-tetraphosphate.

Hilderman, Richard H.; Martín, M; Zimmerman, James K.; Pivorun, Edward B.

doi:10.1016/s0021-9258(20)89589-1

Cited by 86 publications

(31 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Isolation of Membrane Extracts from Mouse Hearts. All membrane fractions were prepared as previously described (Hilderman et al, 1991). These membranes were isolated by centrifugation at 40000g for 10 min and contain a mixture of plasma membranes, nuclear membranes, mitochrondrial membranes, and other membranes.…”

Section: Methodsmentioning

confidence: 99%

“…The pellets were resuspended in 0.3 mL of binding buffer plus 0.033 mM [3H]-Ap<A (15 000-20 000 cpm/pmol), and the samples were assayed after incubation for an additional 20 min at 20 °C. All membranes samples were collected on glass fiber discs and counted as described (Hilderman et al, 1991).…”

Section: Methodsmentioning

confidence: 99%

“…The samples were then reincubated at 29 °C for the corresponding amount of time so that all samples were incubated at 29 °C for a total of 60 min, centrifuged at 16000g for 10 min, resuspended in binding buffer with 0.033 mM [3H]Ap4A (15 000-20 000 cpm/pmol), and the samples were assayed after incubation for an additional 20 min at 20 °C. All membranes samples were collected on glass fiber discs and counted as described (Hilderman et al, 1991). Detection of TL4 Binding to Its Membrane Receptor by ELISA.…”

Section: Methodsmentioning

confidence: 99%

“…0006-2960/93/0432-3119S04.00/0 as an extracellular modulator by altering tissues in the presence of stress conditions. We have demonstrated the presence of specific, saturable membrane receptors for Ap4A in brain, cardiac, liver, kidney, spleen, and adipose tissue (Hilderman et al, 1991). Recently, we have identified the Ap4A receptor as a 30-kDa polypeptide using a covalent radiolabeled derivative of Ap4A.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Identification of a serine protease which activates the mouse heart adenosine 5',5''',P1,P4-tetraphosphate receptor

Walker¹,

Hilderman²

1993

Biochemistry

View full text Add to dashboard Cite

We have previously demonstrated that a serine protease dependent processing step is required for activation of the 30-kDa adenosine 5',5"',P1,P4-tetraphosphate (Ap4A) receptor. However, monoclonal antibodies (Mabs) against a 212-kDa polypeptide inhibit Ap4A binding to its receptor [Walker et al. (1993) Biochemistry 32, 1264-1269]. SDS-PAGE followed by autoradiography of [3H]diisopropylfluorophosphate (DIPF) covalently attached to membrane fractions reveals that the serine protease is the 212-kDa polypeptide or a proenzyme. Mabs against the 30-kDa Ap4A receptor are identified that inhibit Ap4A binding to its membrane receptor. These Mabs do not recognize the 212-kDa membrane protein but recognize four membrane proteins with molecular masses of 67, 55, 42, and 30 kDa. These data suggest that the precursor for the Ap4A receptor is a 67-kDa polypeptide which undergoes multiple cleavage events, at least one by the 212-kDa protein.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Identification of a serine protease which activates the mouse heart adenosine 5',5''',P1,P4-tetraphosphate receptor

Walker¹,

Hilderman²

1993

Biochemistry

View full text Add to dashboard Cite

show abstract

“…In 1991, the P2U purinoceptor was proposed to be activated by both ATP and UTP [32]. Finally, adenine dinucleotides were proposed to produce some of their pharmacological effects by stimulating the P2D purinoceptor [33,34].…”

Section: More P 2 Purinoceptor Subtypesmentioning

confidence: 99%

The P2Y/P2X divide: How it began

Kennedy

2021

Biochemical Pharmacology

View full text Add to dashboard Cite

Brain synaptosomes display a diadenosine tetraphosphate (Ap4A)-mediated Ca2+ influx distinct from ATP-mediated influx

Pivorun

Nordone

1996

J. Neurosci. Res.

View full text Add to dashboard Cite

Studies undertaken to compare the effects of Ap4A and ATP on altering intrasynaptosomal Ca2+ levels from deermouse brain reveal that both ligands induce a rapid influx of extracellular Ca2+. The Ca2+ profile elicited by 167 μM Ap4A is “spike‐like” (half‐time for decline to baseline, 19.1 ± 1.2 sec), in contrast to the gradual decline observed with ATP (104.0 ± 7.4 sec). DIDS (4‐4′‐diisothiocyano‐2,2′‐disulfonic acid stilbene) and suramin preincubation alter only the ATP‐induced Ca2+ profile. Cross‐desensitization studies indicate that prior application of ATP does not significantly affect the Ca2+ influx elicited by Ap4A, and that prior application of Ap4A does not affect the Ca2+ influx elicited by ATP. These results demonstrate that extracellular Ap4A and ATP elicit distinct intrasynaptosomal Ca2+ influx profiles, and suggest that these two nucleotides may be interacting with distinct purinoceptor subclasses or purinoceptor‐effector complexes. Subjecting the synaptosomes simultaneously to depolarization and Ap4A, or to depolarization and ATP, induces an additive effect on Ca2+ influx. Preincubation with verapamil negates the effects of depolarization without modifying the ligand‐elicited Ca2+ fluxes. These results indicate the presence of Ap4A and ATP ligand‐gated channels that may function as modulators of neuronal activity. © 1996 Wiley‐Liss, Inc.

show abstract

Identification of a unique membrane receptor for adenosine 5‘,5“‘-P1,P4-tetraphosphate.

Cited by 86 publications

References 25 publications

Identification of a serine protease which activates the mouse heart adenosine 5',5''',P1,P4-tetraphosphate receptor

Identification of a serine protease which activates the mouse heart adenosine 5',5''',P1,P4-tetraphosphate receptor

The P2Y/P2X divide: How it began

Brain synaptosomes display a diadenosine tetraphosphate (Ap4A)-mediated Ca2+ influx distinct from ATP-mediated influx

Contact Info

Product

Resources

About