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David L. Vesely - One of the best experts on this subject based on the ideXlab platform.

  • Atrial Natriuretic Peptide prohormone gene expression: hormones and diseases that upregulate its expression.
    IUBMB life, 2002
    Co-Authors: David L. Vesely
    Abstract:

    Atrial Natriuretic Peptides consist of a family of Peptide hormones that are synthesized by three separate genes and then stored as three different prohormones (i.e., 126-amino acid [a.a.]) Atrial Natriuretic Peptide (ANP), 108-a.a. brain Natriuretic Peptide (BNP), and 126-a.a. C-Natriuretic Peptide (CNP) prohormones. The gene encoding for the synthesis of the Atrial Natriuretic Peptide prohormone (proANP) consists of three exons and two introns. Exon 1 encodes the signal Peptide and the first 16 a.a. of the ANP prohormone. These 16 a.a. form the N -terminus of a Peptide hormone named long-acting Natriuretic hormone (LANH). A valine-to-methionine substitution in LANH results in a 2-fold increased incidence of strokes in humans. Exon 2 of the proANP gene encodes for three Peptide hormones, i.e., vessel dilator, kaliuretic hormone, and ANP. Each of the proANP gene products have vasodilatory, diuretic, Natriuretic, and/or kaliuretic properties. Stretch, glucocorticoids, thyroid hormone(s), mineralocorticoids, and calcium enhance proANP gene expression. Enhanced proANP gene expression is found in congestive heart failure, hypertension, and cirrhosis with ascites. The proANP gene is present with invertebrates and plants as well as in humans and other vertebrates.

  • Atrial Natriuretic Peptide increases urodilatin in the circulation
    American Journal of Nephrology, 1998
    Co-Authors: David L. Vesely, Rose M. Overton, Mary S. Blankenship, Michael T. Mccormick, Douglas D. Schocken
    Abstract:

    Background: Urodilatin is a 32-amino-acid (AA) Peptide formed in the kidney. Methods: High-performance gel permeation chromatography and high-pressure liquid chromatography evaluation of plasma followed by sensitive urodilatin and Atrial Natriuretic Peptide (ANP) assays revealed that urodilatin does circulate distinctly from ANP. Results: Urodilatin circulates at very low levels (i.e 9–12 pg/ml). Infusion of ANP increased the circulating concentration of urodilatin 135-fold (p Conclusion: Urodilatin circulates and is increased by ANP in humans.

  • Atrial Natriuretic Peptide gene expression within invertebrate hearts
    General and Comparative Endocrinology, 1995
    Co-Authors: John E Poulos, William R Gower, Frank E Friedl, David L. Vesely
    Abstract:

    Abstract The present investigation was designed to (1) determine if Atrial Natriuretic factor gene expression occurs within invertebrates as well as within vertebrates; (2) determine whether the product of this gene expression is the 126-amino-acid Atrial Natriuretic factor prohormone or some other molecular species; and (3) evaluate within the same invertebrates if the products of Atrial Natriuretic factor gene expression are released into their circulation. Utilizing a very sensitive RNase protection assay it was found that Atrial Natriuretic Peptide gene expression occurs within the heart of the oyster, Crassostrea virginica , and within the heart of the blue crab, Callinectes sapidus , but was expressed sevenfold less than in a vertebrate heart (i.e. rat, Rattus norvegiucs ). High-performance gel-permeation chromatography followed by N-terminal and C-terminal Atrial Natriuretic factor prohormone radioimmunoassays indicated that the molecular species synthesized within the oyster and blue crab hearts was the Atrial Natriuretic factor prohormone. The product(s) of this Atrial Natriuretic factor gene expression (i.e., Atrial Natriuretic Peptides) was found to be released into the circulation, i.e., hemolymph, of both the oyster and the blue crab.

Masahiko Kinoshita - One of the best experts on this subject based on the ideXlab platform.

Lincoln R. Potter - One of the best experts on this subject based on the ideXlab platform.

  • renal hyporesponsiveness to Atrial Natriuretic Peptide in congestive heart failure results from reduced Atrial Natriuretic Peptide receptor concentrations
    American Journal of Physiology-renal Physiology, 2007
    Co-Authors: Paula M Bryan, Deborah M Dickey, Yingjie Chen, Lincoln R. Potter
    Abstract:

    Atrial Natriuretic Peptide (ANP) and B-type Natriuretic Peptide decrease blood pressure and cardiac hypertrophy by activating Natriuretic Peptide receptor A (NPR-A), a transmembrane guanylyl cyclase also known as guanylyl cyclase A. Inactivation of NPR-A is a potential mechanism for the renal hyporesponsiveness observed in congestive heart failure (CHF) but direct data supporting this hypothesis are lacking. We examined whether NPR-A activity was reduced in CHF, and if so, by what mechanism. In two separate trials, CHF was induced in mice by 8-wk transverse aortic constriction. Sham controls underwent surgery without constriction. The constricted animals developed severe heart failure as indicated by increased heart weight, increased left ventricular end diastolic and systolic diameters, and decreased left ventricular ejection fractions. Kidney membranes were assayed for guanylyl cyclase activity or used to purify NPR-A by sequential immunoprecipitation/SDS-PAGE. Maximal ANP-dependent guanylyl cyclase activities were reduced by 44 or 43% in kidney membranes from CHF animals in two independent trials. Basal cyclase activities were also reduced by 31% in the second trial. The amount of phosphorylated NPR-A was reduced by 25 or 24% in kidney membranes from CHF animals as well. SYPRO Ruby staining suggested that NPR-A protein levels were similar between treatments in the first trial. However, more accurate estimates of NPR-A protein levels by immunoprecipitation/Western analysis in the second trial indicated that NPR-A protein was reduced by 30%. We conclude that reduced NPR-A protein levels, not receptor dephosphorylation, explain the renal hyporesponsiveness to Natriuretic Peptides in CHF.

  • spatiotemporal regulation of the two Atrial Natriuretic Peptide receptors in testis
    Endocrinology, 2004
    Co-Authors: Dieter Muller, Lincoln R. Potter, Amal K Mukhopadhyay, Robert C Speth, Gabriela Guidone, Regine Potthast, Ralf Middendorff
    Abstract:

    By interacting with a guanylyl cyclase (GC) activity-containing receptor, termed GC-A, Atrial Natriuretic Peptide (ANP) acts as a regulator of blood pressure and fluid volume homeostasis. High expression levels of GC-A in the testis and reported effects of ANP on testosterone secretion by Leydig cells are indicative of important local functions in this organ. Here we show, based on radioligand receptor labeling and immunological approaches, that seminiferous tubules rather than Leydig cells are the predominant GC-A expression sites in the rat testis. Functional activity was proved by ANP- induced cGMP accumulation in isolated seminiferous tubules. Although ontogenetic studies revealed a massive increase in GC-A levels during sexual maturation, the so-called Natriuretic Peptide clearance receptor, another type of ANP receptor proposed to locally control the availability of Natriuretic Peptides, was found to be expressed predominantly before puberty, exceeding the level of GC-A expression at this time. Natr...

Jens P Goetze - One of the best experts on this subject based on the ideXlab platform.

  • effect of pancreatic hormones on pro Atrial Natriuretic Peptide in humans
    EBioMedicine, 2017
    Co-Authors: N E Zois, Dijana Terzic, Kristine Faerch, Peter Plomgaard, Jakob S Hansen, Peter Rossing, Jens P Goetze
    Abstract:

    Abstract Plasma concentrations of pro-Atrial Natriuretic Peptide, proANP, are decreased in obesity and diabetes. Decreased proANP concentrations have also been noted after meal intake, and recently, a glucose-mediated regulation of ANP gene expression was reported. Hence, we evaluated the effects of insulin, glucagon and glucose on plasma proANP in a series of observational and experimental studies. Six healthy men underwent seven days of bed rest. Before and after the bed rest, hyperinsulinemic euglycemic clamps with serial plasma measurements of proANP were performed. Moreover, plasma proANP was quantified in 65 individuals with normal or impaired glucose regulation. Finally, the effects of infusion-induced hyperglucagonemia were examined in ten healthy men. Bed rest decreased insulin sensitivity and plasma proANP. The decrease in proANP was not associated with insulin sensitivity and the Peptide concentrations remained constant during euglycemic hyperinsulinemia and hyperglycemic hyperglucagonemia. Impaired glucose regulation was not associated with decreased proANP concentrations. Bed rest per se induces a marked decrease in plasma proANP concentrations whereas insulin resistance and impaired glucose regulation was not associated with lower proANP concentrations. Neither acute hyperinsulinemia nor hyperglucagonemia seems to affect plasma proANP. Our findings thus suggest that decreased plasma proANP concentrations occur late in the development of insulin resistance.

Juan M. Saavedra - One of the best experts on this subject based on the ideXlab platform.