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Identification of adenosine A1 and A3 receptor subtypes in rat pial and intracerebral arteries.

The expression and microanatomical localization of adenosine A1 and A3 receptor subtypes were investigated in rat pial and intracerebral arteries by immunoblotting, immunohistochemistry and in situ hybridization techniques. Pial artery membranes develop immune bands of approximately 79 and 52 kDa when exposed to anti-A1 and anti-A3 receptor protein antibodies respectively. Sympathectomy performed by bilateral superior cervical ganglionectomy did not change the pattern of adenosine A1 or A3 receptor immunochemistry. Sections of pial and intracerebral arteries processed for A1 or A3 receptor protein immunohistochemistry developed immune reaction in the tunica media, within arterial smooth muscle. A1 receptor immunoreactivity was more pronounced in large-sized compared to medium- and small-sized pial arteries and was stronger in small than in medium- or large-sized intracerebral arteries. A3 receptor immunoreactivity was more pronounced in smaller sized pial arteries compared to larger pial arteries, whereas no differences in the intensity of immune staining were noticeable between different sized intracerebral arteries. In situ hybridization histochemistry revealed a strong signal for A1 receptor and a moderate signal for A3 receptor in the tunica media of pial arteries, within smooth muscle. The present study indicates that rat pial and intracerebral arteries besides to the well characterized A2a and A2b receptors, express also A1 and A3 receptor subtypes. The identification of cerebrovascular A1 and A3 adenosine receptor subtypes may stimulate further research for detailing the mechanism(s) of regulation of cerebral circulation by adenosine.
Maria Antonietta Di Tullio, Seyed Khosrow Tayebati, Francesco Amenta

2417 related Products with: Identification of adenosine A1 and A3 receptor subtypes in rat pial and intracerebral arteries.

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Immunolocalization of A1 adenosine receptors in mammalian spermatozoa.

The presence of A1 adenosine receptors (A1AR) in mammalian spermatozoa was previously demonstrated by radiochemical and immunochemical detection. This study was performed to investigate the cellular location of the A1AR to determine whether these receptors were somehow connected with ecto-adenosine deaminase and to evaluate their function in calcium uptake. By immunofluorescence staining we showed that in mammalian spermatozoa A1AR were constantly localized in the acrosomal region. This finding was confirmed by immunogold detection. Confocal analyses with anti-A1 and anti-ADA antibodies showed a high degree of co-localization. Calcium loading assay showed that this association was functional and affected calcium accumulation in mammalian spermatozoa. Therefore, we concluded that the acrosomal localization of A1AR was a constant feature in mammalian sperm. Moreover, these A1 receptors were functionally coupled to ecto-ADA and were able to modulate calcium uptake into an IP3-gated store.(J Histochem Cytochem 48:1163-1171, 2000)
A Minelli, C Allegrucci, P Piomboni, R Mannucci, C Lluis, R Franco

2257 related Products with: Immunolocalization of A1 adenosine receptors in mammalian spermatozoa.

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Human mononuclear phagocytes express adenosine A1 receptors. A novel mechanism for differential regulation of Fc gamma receptor function.

Using monoclonal anti-adenosine A1 receptor antibodies that bind the A1 receptor ligand binding site, we demonstrate that A1 receptors are expressed on cultured monocytes and rheumatoid synovial fluid mononuclear phagocytes. This finding is associated with the acquisition of reactivity with selective adenosine A1 receptor agonists and is temporally coordinated with the induction of adenosine A2 receptors on cultured monocytes. In a rapid, concentration-dependent fashion, these two distinct adenosine receptors modulate Fc gamma receptor-mediated phagocytosis, a response critical to the pathogenesis of immune complex diseases. Occupancy of A1 receptors by N6-cyclopentyladenosine (an A1-specific adenosine analogue) or mAb AA1 (an anti-A1 mAb) results in a potent stimulation that is blocked by adenosine receptor antagonists. This A1 receptor-induced enhancement of Fc gamma receptor-mediated phagocytosis is a consequence of preferential augmentation of Fc gamma RI function, suggesting distinct mechanisms for receptor-effector coupling of Fc gamma receptor families. In contrast, ligation of A2 receptors by A2-specific agonists decreases Fc gamma receptor-mediated phagocytosis in cultured monocytes. The opposing effects of adenosine A1 and A2 receptors allow for a concentration-dependent feed-back loop that responds more rapidly than effects elicited by other endogenous modulators. Low concentrations of adenosine are proinflammatory providing enhanced Fc gamma receptor function via A1 receptors, whereas higher concentrations that can occur with tissue damage are anti-inflammatory providing inhibition via A2 receptors. This rapid and potent modulation of Fc gamma receptor-mediated function suggests that adenosine is an important local regulator of the inflammatory response.
J E Salmon, N Brogle, C Brownlie, J C Edberg, R P Kimberly, B X Chen, B F Erlanger

2082 related Products with: Human mononuclear phagocytes express adenosine A1 receptors. A novel mechanism for differential regulation of Fc gamma receptor function.

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