Neurophysine – molekulare und zelluläre Aspekte

Acher, Roger

doi:10.1002/ange.19790911107

Cited by 15 publications

(3 citation statements)

References 77 publications

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“…The chemical structure and pharmacological properties of AVT and MT from the chicken and other avian species suggest that these are similar to the equivalent hormones from lungfishes, amphibians and reptiles (2). The oxytocic and vasopressic families are probably derived from a common ancestral gene by gene duplication (3). During phylogeny vasopressin has most likely evolved from AVT and oxytocin from MT.…”

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confidence: 94%

Embryonal Development of Arginine Vasotocin/Mesotocin Gene Expression in the Chicken Brain

Milewski

Lvell²,

Großmann

et al. 1989

J Neuroendocrinology

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An ontogenic series of chick embryo brains (4,6,9,12,14,16 and 18 days of incubation, hatching day: 21) was coronally or saggitally sectioned and investigated for expression of the arginine vasotocin (AVT)/mesotocin (MT) gene. To this end a 39mer oligonucleotide recognizing the AVTlMT encoding sequence of their respective mRNAs was constructed employing optimized codon usage and was used for in situ hybridization. AVTlMT mRNA-expressing neurons were first detected on embryonal day (E) 6 adjacent to the third ventricle. By E9 the periventricular nucleus had expanded in size but the hybridization signal was weaker. These results suggest a migration of cells in all directions away from the third ventricle into the diencephalon; some perikarya were even observed at the lateral pial surface above the optic chiasm. By E12, brain differentiation had advanced to distinct hypothalamo-neurohypophyseal nuclei (supraoptic and paraventricular nuclei) as well as to accessory groups expressing AVTlMT mRNA. Two cell types were then distinguishable in the paraventricular nucleus; the specific mRNA was expressed either as a weak or a strong hybridization signal.Comparison with other studies suggested that differentiation had almost attained adult level though cell growth and differentiation of supraoptic and paraventricular nuclei still occurred. This was complete by El8 when individual cells were larger and the intensity of the hybridization signal became very strong.RNase pretreatment depressed the signal by 100%. Northern blot hybridization of RNA extracted from newly hatched chicks verified the specificity of the probe. A single band was evident, indicating an mRNA of approximately 700 bases, which is only found in hypothalamus and not in muscle, liver or extra-hypothalamic brain, and corresponds in size closely with mammalian vasopressin mRNA.The data demonstrate a very early development (E6) of neurohypophyseal hormone gene expression in the chick embryo brain with important differentiation around E9. At El2 magnocellular neuronal arrangement resembled adult neurons but the gene expression signal increased in intensity until E18.Once the egg is shelled inside the hen and once it is layed, the chick embryo develops independently of maternal support. Thus, the chick embryo offers a number of excellent advantages over mammalian systems to study hypothalamo-neurohypophyseal development and function (1). In addition, embryonic tissue is easily accessible and the embryology is well defined. The similarity in the structures, and in part, in the function of neurohypophyseal hormones between mammals and the chicken, suggests that the chicken model could provide very useful information to assess the ontogenetic regulation of these genes and may pertain for all homeotherms.Arginine vasotocin (AVT) and mesotocin (MT) are the avian analogues to the mammalian neuropeptide hormones vasopressin and oxytocin, respectively. Throughout the vertebrates, these neurohypophyseal nonapeptides can be classified into two types according to t...

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confidence: 94%

Embryonal Development of Arginine Vasotocin/Mesotocin Gene Expression in the Chicken Brain

Milewski

Lvell²,

Großmann

et al. 1989

J Neuroendocrinology

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“…Arginine vasopressin (AVP) and oxytocin (OT), two nonapeptide hormones, are produced together with their corresponding 'carrier' proteins, the neurophysins, as common precursors by different magnocellular neurones in both the supraoptic and paraventricular nuclei of the hypothalamus (Pickering and Swann, 1983;Brownstein et al, 1980;Breslow, 1979;Acher, 1979;North et al, 1978). The precursors are packaged into neurosecretory granules and transported axonally in the pituitary stalk to the posterior pituitary.…”

Section: Introductionmentioning

confidence: 99%

Structural organization of the rat gene for the arginine vasopressin-neurophysin precursor.

Schmale¹,

Heinsohn²,

Richter³

1983

The EMBO Journal

183

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The rat arginine vasopressin-neurophysin precursor gene has been isolated from a genomic library cloned in X phage Charon 4A. Restriction mapping and nucleotide sequence analysis demonstrated that the gene is 1.85 kilobase pairs long and contains two intervening sequences located in the protein coding region. Exon A encodes a putative signal peptide, the hormone arginine vasopressin and the variable N terminus of the carrier protein neurophysin, exon B encodes the highly conserved middle part of neurophysin and exon C its variable C terminus together with glycoprotein. Thus, the three functional domains of the precursor -argiline vasopressin, neurophysin, glycoprotein -are encoded on three distinct exons.

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“…This precursor gave rise to a vasopressin-like peptide after trypsinization (7). In addition the precursor crossreacted with antibodies raised against one of the hypothalamic cysteine-rich neurophysins (8,9) which is known to transport vasopressin to its storage site in the posterior pituitary (10).…”

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Immunological identification of a common precursor to arginine vasopressin and neurophysin II synthesized by in vitro translation of bovine hypothalamic mRNA.

Schmale¹,

Richter²

1981

Proc. Natl. Acad. Sci. U.S.A.

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mRNA from membrane-bound polysomes of bovine hypothalamus was translated in an mRNA-dependent cellfree system from reticulocyte lysate or wheat germ. The translation products were identified by immunoprecipitation with antibodies to either neurophysin H or arginine vasopressin followed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. An immunoreactive polypeptide was obtained with an apparent Mr of 21,000. Sequential immunoprecipitation studies indicated that the Mr 21,000 product is a common precursor to neurophysin II and arginine vasopressin. The specificity of the immunoprecipitation was demonstrated by competition with excess amounts of unlabeled neurophysin H or arginine vasopressin; little or no competition was observed with unlabeled neurophysin I or oxytocin. Processing experiments with microsomal membranes from dog pancreas or tunicamycin-treated ascites tumor cells showed that the Mr 21,000 polypeptide is the prepro form. It was converted to a pro form with Mr 19,000 suggesting a pre sequence of approximately 15 amino acids. The Mr 19,000 polypeptide was coreglycosylated to an apparent Mr of 23,000, indicating that the neurophysin II-arginine vasopressin precursor is a glycopolypeptide.Oligopeptides such as the bacterial antibiotics gramicidin and tyrocidin are synthesized in a nonribosomal fashion on polyenzyme templates (1, 2). Reports that oligopeptides of hypothalamus from mammals also might be synthesized by a nonribosomal mechanism are still controversial (3-5). In vitro biosynthesis of the hypothalamic nonapeptide hormones vasopressin and oxytocin has not yet been resolved. Although Sachs (6) suggested more than a decade ago that vasopressin may be synthesized by a ribosome-dependent mechanism via a precursor polypeptide, only recently a tentative glycopolypeptide precursor with an apparent M, of 20,000 has been isolated from the hypothalamus of rats and mice (7-9). This precursor gave rise to a vasopressin-like peptide after trypsinization (7). In addition the precursor crossreacted with antibodies raised against one of the hypothalamic cysteine-rich neurophysins (8,9) which is known to transport vasopressin to its storage site in the posterior pituitary (10).If the precursor hypothesis is valid it should be possible to demonstrate biosynthesis of a vasopressin-neurophysin precursor directly by translation of hypothalamic mRNA in cellfree systems. Although a number of groups have reported the synthesis of neurophysin precursors in cell-free systems (11-13), identification of vasopressin-like sequences within the reported precursors has been lacking. The present communication reports mRNA-directed synthesis of a common precursor to arginine vasopressin (AVP) and neurophysin II and its processing and core glycosylation; specific antibodies were used for identification. MATERIALS AND METHODSBovine neurophysin I (Np I) and neurophysin II (Np II) and rabbit antisera to Np I and Np II were purchased from Bioproducts (Brussels); according to the supplier the antisera against Np ...

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Neurophysine – molekulare und zelluläre Aspekte

Cited by 15 publications

References 77 publications

Embryonal Development of Arginine Vasotocin/Mesotocin Gene Expression in the Chicken Brain

Embryonal Development of Arginine Vasotocin/Mesotocin Gene Expression in the Chicken Brain

Structural organization of the rat gene for the arginine vasopressin-neurophysin precursor.

Immunological identification of a common precursor to arginine vasopressin and neurophysin II synthesized by in vitro translation of bovine hypothalamic mRNA.

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