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In vivo processing and release into the circulation of GFP fusion protein in arginine vasopressin enhanced GFP transgenic rats: response to osmotic stimulation.

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In vivo processing and release into the circulation of GFP fusion protein in arginine vasopressin enhanced GFP transgenic rats: response to osmotic stimulation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Satoh, Keita Oti, Takumi Katoh, Akiko Ueta, Yoichi Morris, John F. Sakamoto, Tatsuya Sakamoto, Hirotaka
Description	Country affiliation: Japan Author Affiliation: Satoh K ( Ushimado Marine Institute, Graduate School of Natural Science and Technology, Okayama University, Japan.); Oti T ( Ushimado Marine Institute, Graduate School of Natural Science and Technology, Okayama University, Japan.); Katoh A ( Department of Physiology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan.); Ueta Y ( Department of Physiology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan.); Morris JF ( Department of Physiology, Anatomy and Genetics, Le Gros Clark Building, University of Oxford, UK.); Sakamoto T ( Ushimado Marine Institute, Graduate School of Natural Science and Technology, Okayama University, Japan.); Sakamoto H ( Ushimado Marine Institute, Graduate School of Natural Science and Technology, Okayama University, Japan.)
Abstract	Arginine vasopressin (AVP) is a neurohypophysial hormone synthesized as a part of a prepropeptide precursor containing the signal peptide, AVP hormone, AVP-associated neurophysin II and copeptin in the hypothalamic neurosecretory neurons. A transgenic (Tg) rat line expressing the AVP-eGFP fusion gene has been generated. To establish the AVP-eGFP Tg rat as a unique model for an analysis of AVP dynamics in vivo, we first examined the in vivo molecular dynamics of the AVP-eGFP fusion gene, and then the release of GFP in response to physiological stimuli. Double immunoelectron microscopy demonstrated that GFP was specifically localized in neurosecretory vesicles of AVP neurons in this Tg rat. After stimulation of the posterior pituitary with high potassium we demonstrated the exocytosis of AVP neurosecretory vesicles containing GFP at the ultrastructural level. Biochemical analyses indicated that the AVP-eGFP fusion gene is subjected to in vivo post-translational modifications like the native AVP gene, and is packaged into neurosecretory vesicles as a fusion protein: copeptin1-14 -GFP. Moreover, GFP release into the circulating blood appeared to be augmented after osmotic stimulation, like native AVP. Thus, here we show for the first time the in vivo molecular processing of the AVP-eGFP fusion gene and stimulated secretion after osmotic stimulation in rats. Because GFP behaved like native AVP in the hypothalamo-pituitary axis, and in particular was released into the circulation in response to a physiological stimulus, the AVP-eGFP Tg rat model appears to be a powerful tool for analyzing neuroendocrine systems at the organismal level.
File Format	HTM / HTML
ISSN	1742464X
Issue Number	13
Volume Number	282
e-ISSN	17424658
Journal	FEBS Journal
Language	English
Publisher	Wiley (on behalf of the Federation of European Biochemical Societies)
Publisher Date	2015-07-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Arginine Vasopressin Metabolism Green Fluorescent Proteins Recombinant Fusion Proteins Animals Exocytosis Genetics Male Microscopy, Immunoelectron Osmolar Concentration Protein Processing, Post-translational Rats Rats, Transgenic Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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