Atrial natriuretic peptide receptors in guinea pig placentas

Natriuretic peptide receptors in rat brain were mapped by in vitro autoradiography using 125I-labeled [Tyr0]CNP-(1-22) to bind atrial natriuretic peptide receptor (ANPR)-B and ANPR-C receptors selectively, and 125I-labeled alpha-ANP to select ANPR-A and ANPR-C receptors. Des-[Gln18,Ser19,Gly20,Leu21,Gly22]ANP-(4- 23)-amide (C-ANP) was used for its selectivity for ANPR-C over ANPR-A. Specific binding of 125I-[Tyr0]CNP-(1-22) with a dissociation constant (Kd) approximately 1 nM occurred in olfactory bulb, cerebral cortex, lateral septal nucleus, choroid plexus, and arachnoid mater. This binding was abolished by C-type natriuretic peptide [CNP-(1-22)], alpha-ANP and C-ANP, and conformed to ANPR-C. 125I-alpha-ANP bound to all structures that bound 125I-[Tyr0]CNP-(1-22). This binding was also inhibited by both CNP-(1-22) and C-ANP, confirming the presence of ANPR-C-like binding sites. However, ANPR-C-like binding sites were heterogenous because only some had high affinities for 125I-[Tyr0]CNP-(1-22) and CNP-(1-22). 125I-alpha-ANP also bound sites without affinities for C-ANP or CNP-(1-22). These sites were consistent with ANPR-A. They occurred mainly on the olfactory bulb, the choroid plexus, and the subfornical organ. Guanosine 3',5'-cyclic monophosphate production was strongly stimulated by alpha-ANP but not by CNP-(1-22) in olfactory bulb. Neither ligand stimulated it in cortical tissue. Thus the natriuretic peptide binding sites of rat brain conformed to ANPR-A and to heterogenous ANPR-C-like sites. No ANPR-B were detected.

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Atrial natriuretic peptide receptors are present in brown adipose tissue

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(88)80943-4 ◽

1988 ◽

Vol 156 (2) ◽

pp. 1000-1006 ◽

Cited By ~ 24

Author(s):

H. Okamura ◽

P.A. Kelly ◽

J.G. Chabot ◽

G. Morel ◽

M. Belles-Isles ◽

...

Keyword(s):

Adipose Tissue ◽

Atrial Natriuretic Peptide ◽

Brown Adipose Tissue ◽

Natriuretic Peptide ◽

Peptide Receptors ◽

Natriuretic Peptide Receptors ◽

Brown Adipose ◽

Atrial Natriuretic

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Computerized approach using autoradiography to quantify atrial natriuretic peptide receptors in the DOCA-salt hypertensive rat kidney

Regulatory Peptides ◽

10.1016/0167-0115(91)90474-u ◽

1991 ◽

Vol 35 (2) ◽

pp. 115-125 ◽

Cited By ~ 4

Author(s):

Katsuhiko Takatori ◽

Toshio Ogura ◽

Zensuke Ota

Keyword(s):

Atrial Natriuretic Peptide ◽

Natriuretic Peptide ◽

Rat Kidney ◽

Peptide Receptors ◽

Natriuretic Peptide Receptors ◽

Hypertensive Rat ◽

Atrial Natriuretic

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The expression of atrial natriuretic peptide in the oviduct and its functions in pig spermatozoa

Journal of Endocrinology ◽

10.1677/joe.1.06483 ◽

2006 ◽

Vol 189 (3) ◽

pp. 493-507 ◽

Cited By ~ 17

Author(s):

Meijia Zhang ◽

Haiyan Hong ◽

Bo Zhou ◽

Shiying Jin ◽

Chao Wang ◽

...

Keyword(s):

Atrial Natriuretic Peptide ◽

Natriuretic Peptide ◽

Acrosome Reaction ◽

Formation Rate ◽

Maximal Response ◽

Peptide Receptors ◽

Cleavage Rate ◽

Natriuretic Peptide Receptors ◽

Selective Ligand ◽

Atrial Natriuretic

Locally synthesized atrial natriuretic peptide (ANP) and its receptors have been found in reproductive tissues of various mammals, and play an important role in the acrosome reaction of human sperm. The objective of the present study was to examine the expression of ANP and its receptors in pig spermatozoa and oviduct, and the effect of ANP on pig spermatozoa function. The expression of ANP and its receptors was analyzed by RT-PCR. Only natriuretic peptide receptors-A (NPRA) mRNA was detected in fresh sperm. While the levels of natriuretic peptide receptors-C (NPRC) mRNA were low with no obvious change among different oviductal phases, the levels of ANP mRNA were high in oviduct(OT)1 , OT3 and OT5, but were very low in OT2. On the other hand, the levels of NPRA mRNA were low in OT1 and OT2, increased in OT3 and reached a maximum in OT4 and OT5. Western blot analysis revealed that the level of ANP was high in OT1, decreased in OT2 and OT3, and arrived at the nadir in OT4 and OT5. The effect of ANP on spermatozoa function was studied by the acrosome reaction and IVF. Incubation with ANP for 1 h significantly induced acrosome reaction of preincubated spermatozoa, and maximal response of acrosome reaction (34.1 ± 2.3%) was achieved at 1 nM ANP treatment. Both C-ANP-(4–23), a selective ligand of NPRC, and caffeine had no effect on the acrosome reaction. The stimulatory effect of ANP on acrosome reaction could be mimicked by the permeable cGMP analog, 8-Br-cGMP. ANP and caffeine had a similar effect on improving the oocytes penetration rate, polyspermy rate and the average number of sperm per penetrated oocyte. Also, ANP treatment had a similar effect on cleavage rate, blastocyst formation rate and the number of cells per blastocyst as that of caffeine treatment. The effects of ANP on the acrosome reaction and the parameters of oocyte penetration could be blocked by cGMP-dependent protein kinase (PKG) inhibitors KT5823 and/or Rp-8-pCPT-cGMPS. These results suggest that the expression of ANP in the oviduct may be involved in the regulation of the acrosome reaction and the fertilising ability of pig spermatozoa, and the PKG pathway possibly participates in the process.

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