Neuroendocrinology of Atrial Natriuretic Polypeptide in the Brain

Y, L; Zhang, M L; Yang, Xiao; Tian, Demin; Qi, Jinwen; Zhang, D M

doi:10.1159/000125789

Cited by 15 publications

(6 citation statements)

References 38 publications

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“…In contrast to other circumventricular organs, such as the subfornical organ and area postrema (which are characterized by relatively high levels of ANP receptors) (28), there is only a poor expression of GC-A in the pineal gland. It is to be noted, however, that this organ is characterized by exceptionally high levels of the CNP receptor, GC-B (17).…”

Section: Expression Of Anp Receptors In Different Tissuesmentioning

confidence: 85%

Central Nervous System-Specific Glycosylation of the Type A Natriuretic Peptide Receptor

Müller¹,

Middendorff

Olcese³

et al. 2002

Endocrinology

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Physiological effects of atrial natriuretic peptide (ANP) are thought to be mediated by binding to and activation of a widely expressed membrane receptor, termed guanylyl cyclase (GC)-A. During comparative analyses of ANP receptor expression in various rat and bovine tissues, by UV light-induced affinity cross-linking to (125)I-ANP, we uncovered a size heterogeneity of GC-A, detectable as a 130-kDa protein in peripheral and as a 122-kDa protein in central nervous system tissues. This heterogeneity could be explained by differences in N-linked glycosylation, because treatments with N-glycosidase F reduced the apparent molecular weights of both receptor variants to the same value of 116,000. As judged by displacement experiments, the two receptor glycoforms did not differ in their binding affinities for natriuretic peptides. Assessments of GC activities did not reveal any difference in ANP-induced generation of the second messenger, cyclic GMP. The examination of GC-A expression in brain during ontogeny revealed an alteration of the apparent molecular mass during early postnatal development from the 130-kDa to the 122-kDa form, suggesting a change in oligosaccharide processing. This study provides a reliable method for characterizing GC-A expression and identifies, for the first time, a differential glycosylation of this receptor in vivo.

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Section: Expression Of Anp Receptors In Different Tissuesmentioning

confidence: 85%

Central Nervous System-Specific Glycosylation of the Type A Natriuretic Peptide Receptor

Müller¹,

Middendorff

Olcese³

et al. 2002

Endocrinology

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“…In brain it exists as amino-terminally truncated form. Two systems are involved in the secretion of ANP: peripheral ANP (heart and plasma) and central ANP (paraventricular, periventricular, arcuate, and pre-optical-medial nuclei and other sites) (6). Despite the blood-brain barrier, these systems communicate through the circumventricular organs, the organum vasculosum lamina terminalis and the organum subfornicalis (7)(8)(9).…”

Section: Mha Oliveira Et Almentioning

confidence: 99%

Atrial natriuretic peptide and feeding activity patterns in rats

Oliveira¹,

Antunes‐Rodrigues²,

Gutkowska³

et al. 1997

Braz J Med Biol Res

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This review presents historical data about atrial natriuretic peptide (ANP) from its discovery as an atrial natriuretic factor (ANF) to its role as an atrial natriuretic hormone (ANH). As a hormone, ANP can interact with the hypothalamic-pituitary-adrenal axis (HPA-A) and is related to feeding activity patterns in the rat. Food restriction proved to be an interesting model to investigate this relationship. The role of ANP must be understood within a context of peripheral and central interactions involving different peptides and pathways.

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“…Key raords: atrial natriuretic peptide, ANP mRNA, Brattleboro rats, fluid balance Cardiac and hypothalamic cells have been shown to synthesize atrial natriuretic peptide (ANP) and these locations are suggested to be involved in the peripheral and central regulation of the natriuresis and diuresis (de Bold 1985, Ma et a / . 1991).…”

mentioning

confidence: 99%

Atrial natriuretic peptide and its mRNA in heart and brain of vasopressin‐deficient Brattleboro rats

Arjamaa

Taskinen

Kanervo

et al. 1995

Acta Physiologica Scandinavica

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To understand the secretion and synthesis of atrial natriuretic peptide we measured immunoreactive atrial natriuretic peptide from plasma, heart tissues and brain areas, and ANP mRNA was determined from heart auricles and ventricles of vasopressin-deficient Brattleboro rats (DI) and from desmopressin treated Brattleboro rats (DI+DDAVP). Long-Evans rats (LE) served as controls. DI+DDAVP rats were given for 3 days sc. injections of 0.5 micrograms 1-desamino-8-D-arginine vasopressin in 1 mL saline twice a day. The rats were housed in single metabolic cages and urinary output and water intake were measured daily. All the body and organ weight parameters were similar in the three groups when the rats were killed. No change was seen in the plasma ANP level between the groups. The right ventricle of DI+DDAVP rats had significantly (P < 0.05) higher concentration of ANP than LE rats (15.8 +/- 4.4 vs. 3.4 +/- 0.6 ng mg-1 tissue). The left ventricle of DI and DI+DDAVP had significantly (P < 0.05) lower amounts of ANP mRNA than LE rats (0.5 +/- 0.2 vs. 1.3 +/- 0.2 and 0.5 +/- 0.1 vs. 1.3 +/- 0.2 arbitrary units). In the hypothalamus, the ANP concentration was significantly (P < 0.05) lower both in DI and in DI+DDAVP rats than in LE rats (9.3 +/- 1.3 vs. 14.5 +/- 1.6 and 6.1 +/- 0.6 vs. 14.5 +/- 1.6 pg mg-1 tissue). To conclude, although the water intake and urinary output of DI rats were changed towards normal with desmopressin treatment, the heart ventricular and hypothalamic ANP did not parallel the change.(ABSTRACT TRUNCATED AT 250 WORDS)

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Neuroendocrinology of Atrial Natriuretic Polypeptide in the Brain

Cited by 15 publications

References 38 publications

Central Nervous System-Specific Glycosylation of the Type A Natriuretic Peptide Receptor

Central Nervous System-Specific Glycosylation of the Type A Natriuretic Peptide Receptor

Atrial natriuretic peptide and feeding activity patterns in rats

Atrial natriuretic peptide and its mRNA in heart and brain of vasopressin‐deficient Brattleboro rats

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