In vitro biosynthesis and processing of composite common precursors containing amino acid sequences identified immunologically as neurophysin I/oxytocin and as neurophysin II/arginine vassopressin

Schmale, Hartwig; Richter, Dietmar

doi:10.1016/0014-5793(80)80381-4

Cited by 36 publications

(11 citation statements)

References 17 publications

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“…Incorporation studies with another radioactive amino acid, the initiator formylmethionine, indicated that the N-terminus was intact and thus that the 21k precursor represented the prepro-form [19]. Similarly, oxytocin-and bovine neurophysin I-specific antisera unambiguously selected a polypeptide of M, 16,500 (16.5k), prepro-oxytocin-neurophysin I [17].…”

Section: Cell-free Biosynthesismentioning

confidence: 98%

“…When bovine hypothalamic mRNA is microinjected into frog oocytes and these are incubated in the presence of (35S)cysteine, several AVP-neurophysin II and oxytocin-neurophysin I products can be identified. Neurophysin II antisera select principally products of 23,000 and 14,000 molecular weight, with lesser quantities of products in the range of 19,000-22,000 and at 25,000 M, [17]. All these products also react specifically with antisera to vasopressin.…”

Section: Further Processingmentioning

confidence: 99%

“…In contrast, preprooxytocin-neurophysin I is not glycosylated [17], but is re duced in size to an Mr 15,000 proform (15.5k).…”

Section: Cell-free Biosynthesismentioning

confidence: 99%

“…Experiments using antisera against AVP and bovine neurophysin 11 suggested that a polypeptide of 21,000 ap parent molecular weight (21k) was the common precursor to AVP and neurophysin II [17,19]. Incorporation studies with another radioactive amino acid, the initiator formylmethionine, indicated that the N-terminus was intact and thus that the 21k precursor represented the prepro-form [19].…”

Section: Cell-free Biosynthesismentioning

confidence: 99%

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Vasopressin and Oxytocin Precursors as Model Preprohormones

Ivell¹,

Schmale²,

Richter³

1983

Neuroendocrinology

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Using a combination of in vitro methodology, including cell-free translation, two-dimensional peptide mapping and recombinant DNA techniques, the structure of the precursors of the hypothalamic nonapeptide hormones vasopressin and oxytocin has been elucidated. Both hormone precursors are model cellular polyproteins in that they comprise several different entities within the same polypeptide molecule. In each precursor, the nonapeptide hormone follows immediately the signal peptide and is, in turn, attached to its respective carrier neurophysin. The vasopressin precursor also includes a pituitary glycoprotein at its C-terminus. The posttranslational processing of the precursors to set free the nonapeptide hormones is thus a critical regulatory step, which can in part be simulated in the quasi in vivo system of the Xenopus laevis oocyte. The preprohormones to vasopressin and oxytocin illustrate well the convenience of the in vitro experimental approach in understanding the function of the peptidergic neuron.

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Section: Cell-free Biosynthesismentioning

confidence: 98%

Section: Further Processingmentioning

confidence: 99%

“…In contrast, preprooxytocin-neurophysin I is not glycosylated [17], but is re duced in size to an Mr 15,000 proform (15.5k).…”

Section: Cell-free Biosynthesismentioning

confidence: 99%

Section: Cell-free Biosynthesismentioning

confidence: 99%

See 2 more Smart Citations

Vasopressin and Oxytocin Precursors as Model Preprohormones

Ivell¹,

Schmale²,

Richter³

1983

Neuroendocrinology

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“…The first step is biosynthesis in rough endoplasmic reticulum of a prohormone consisting of OT coupled with neurophysin and signal peptide (Schmale and Richter, 1980). The synthesis of prohormone lasts as long as OT-mRNA is available, ie until d 5-7 of the estrous cycle (Fehr et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Reduction of ovarian oxytocin content from early luteal phase does not affect the corpus luteum secretory function in cattle

Jaroszewski¹,

Kotwica²

1994

Reprod. Nutr. Dev.

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Summary ― It was found previously that the reduction of ovarian oxytocin (OT) content by up to 80% on d 12 and 16 of the cycle affects neither luteolysis nor estrous cycle duration in cattle. Because ovarian OT is suggested to be involved in progesterone synthesis/secretion, in the present study we wanted to investigate whether ovary depletion of OT in the early stages of the estrous cycle will influence the corpus luteum (CL) secretory function. In experiment 1, heifers (n = 15) had cannulae inserted into the aorta abdominalis through the coccygeal artery. The tip of each cannula was placed cranial to the origin of the ovarian artery. Noradrenaline (NA; 4 mg) was infused on d 5-10 for 30 min daily, evoking release of OT and lower, but evident, increases in the progesterone levels. This did not affect the length of the estrous cycle compared with control heifers infused with saline only. Because ovarian OT cannot be restored once discharged, NA served as a tool to deplete the CL of OT in experiment 2. The same dose of NA was given on d 5-10 to 4 heifers. The corpora lutea used to determine OT tissue concentrations were obtained by surgery under local anaesthesia 10-15 min after the last NA infusion. This dose of NA, depleted CL of OT by about 51 % compared with control heifers. We conclude that significant reduction of ovarian OT content on d 5-10 does not affect the CL function. Thus, if ovarian OT is involved in ovarian steroidogeneis, it plays a modulatory rather than a mandatory role. corpus luteum / oxytocin / noradrenaline / estrous cycle / cattle Résumé ― La réduction de la concentration de l'ocytocine ovarienne au début de la phase lutéale n'influe pas sur la fonction du corps jaune chez la vache. Des recherches antérieures ont démontré que la diminution du taux d'oxytocine (OT) de 80 % entre le 12e et le 16e jour du cycle cestral n'influe pas sur la durée du cycle chez la vache. Pour tester un rôle possible de l'OT ovarienne sur la synthèselsecrétion de la progestérone, nous avons vérifié si la déplétion de l'OT contenue dans l'ovaire au début de la phase lutéale influençait la fonction sécrétoire du corps jaune (CL). Chez les génisses (n = 15) des canules ont été introduites dans l'artère abdominale à partir de l'artère caudale de façon à ce que les terminaisons de chaque canule soient placées frontalement à l'origine de l'artère ovarienne. L'infusion de noradrénaline (NA; 4

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Neurophysin–neuropeptide hormone complexes: Biosynthetic origin and noncovalent interactions

Chaiken

1983

Biopolymers

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SynopsisRecent studies of the neurophysins and associated neuropeptide hormones have addressed both the biosynthetic pathways by which these noncovalent protein-peptide complexes are derived in neurosecretory neurons and the nature of the noncovalent interactions likely to occur during transport and storage in neurosecretory granules within the neurons. In uitro translation of hypothalamic mRNA and sequencing of cDNA obtained from this mRNA have yielded chemical evidence that each complex of hormone and major neurophysin is made through a common precursor molecule. The mature complexes obtained upon proteolytic processing of precursors exhibit interdependent hormone binding and self-association interactions. Photoaffinity labeling and quantitative affinity chromatography have helped detect and define the binding surfaces involved. Further study of the structural nature of these surfaces is being carried out using large neurophysin fragments obtained by limited tryptic proteolysis.

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In vitro biosynthesis and processing of composite common precursors containing amino acid sequences identified immunologically as neurophysin I/oxytocin and as neurophysin II/arginine vassopressin

Cited by 36 publications

References 17 publications

Vasopressin and Oxytocin Precursors as Model Preprohormones

Vasopressin and Oxytocin Precursors as Model Preprohormones

Reduction of ovarian oxytocin content from early luteal phase does not affect the corpus luteum secretory function in cattle

Neurophysin–neuropeptide hormone complexes: Biosynthetic origin and noncovalent interactions

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