Biosynthesis of Vasopressin and Neurophysins

North, William G.

doi:10.1007/978-1-4615-8129-1_4

Cited by 22 publications

(14 citation statements)

References 117 publications

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“…1) (3 ). Neurophysin II has a complex structure with many putative intramolecular disulfide bonds, and it may be associated with AVP during maturation and transport (4 ). Copeptin, the Cterminal portion of provasopressin, is a 39-amino acid glycopeptide of unknown function (5,6 ).…”

mentioning

confidence: 99%

Assay for the Measurement of Copeptin, a Stable Peptide Derived from the Precursor of Vasopressin

Morgenthaler¹,

Struck²,

Alonso³

et al. 2006

Clinical Chemistry

926

871

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Background: Arginine vasopressin (AVP) is a key regulator of water balance, but its instability makes reliable measurement difficult and precludes routine use. We present a method for quantifying AVP release by use of copeptin, a glycopeptide comprising the C-terminal part of the AVP prohormone. Methods: We measured copeptin in 50-L serum and plasma samples from healthy individuals and from critically ill patients with sepsis. Our sandwich immunoluminometric assay used 2 polyclonal antibodies to amino acids 132-164 of pre-provasopressin. Results: The assay yielded results within 3 h. The analytical detection limit was 1.7 pmol/L, and the interlaboratory CV was <20% for values >2.25 pmol/L. The assay was linear on dilution of the analyte. Ex vivo copeptin stability (<20% loss of analyte) for at least 7 days at room temperature and 14 days at 4°C was shown for serum and EDTA-, heparin-, and citrate plasma. Copeptin (median, 4.2 pmol/L; range, 1-13.8 pmol/L) was detectable in 97.5% of 359 healthy individuals and was not associated with age. Median concentrations were considerably higher in men than women, increased significantly after exercise, and were influenced by fasting and water load. Copeptin was significantly (P <0.001) increased in 60 critically ill patients with sepsis (median, 79.5 pmol/L; range, 10.6 -228.0 pmol/L). The correlation between copeptin and AVP for 110 samples was r ‫؍‬ 0.78 (P <0.0001). Conclusions: Copeptin is stable for days after blood withdrawal and can be quickly and easily measured.

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mentioning

confidence: 99%

Assay for the Measurement of Copeptin, a Stable Peptide Derived from the Precursor of Vasopressin

Morgenthaler¹,

Struck²,

Alonso³

et al. 2006

Clinical Chemistry

926

871

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“…Consistent with this possibility, VP and OT are known to be stored in vesicles along with cysteine-rich polypeptides, the neurophysins. Indeed, neurophysins and nonapeptide form crystalline complexes in vesicles [29]. This fact alone may make stored VP and OT relatively inaccessible to intracellular CSH.…”

Section: Discussionmentioning

confidence: 99%

“…This fact alone may make stored VP and OT relatively inaccessible to intracellular CSH. Additionally, because the storage vesicles sequester large quantities of the neurophysins, which contain six times more cysteine residues per molecule than VP or OT [29], their presence in the vesicles might conceivably 'buffer' VP and OT against the actions of CSH. In con trast, SRIF storage vesicles are not known to contain cys teine-rich storage proteins, or to form crystalline com plexes within storage granules.…”

Section: Discussionmentioning

confidence: 99%

Effect of Cysteamine Injection on Vasopressin and Oxytocin Biosynthesis in Rat Hypothalamus

1994

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Cysteamine (CSH), a sulfhydryl agent that promotes disulfide-exchange reactions, was studied for its effects on the immunoreactive (IR) levels and synthesis of oxytocin and vasopressin in the hypothalamus. CSH injection (300 mg/ kg s.c.) caused a rapid (1 h) suppression of ³⁵S-cysteine incorporation into hypothalamic arginine vasopressin (VP) and oxytocin (OT). The reduction in labeling persisted for about 8 h; label incorporation was normal within 10 h of CSH administration. The drug did not influence ³⁵S-cysteine incorporation into acid-precipitable protein, nor did it influence ³⁵S-cysteine specific activity in the hypothalamus. In addition, ³⁵S-VP and ³⁵S-OT molecules could not be recovered from hypothalami of CSH-treated rats by subjecting samples to denaturing, reducing and then reoxidizing conditions. Despite the reduction in peptide labeling, CSH treatment produced no alterations in the IR VP and OT contents of hypothalamus or posterior pituitary. These results indicate that CSH causes a true suppression of both VP and OT formation in hypothalamus, and suggest that the effect is either too transient to promote a reduction in endogenous stores of either peptide, or that the drug equally inhibits peptide production and removal (i.e., axonal transport, secretion).

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“…Each nonapeptide and its cor responding NP are synthesized from large molecular weight common precursors within distinct neuronal populations of the SON and PVN. The common precursor for VP and its NP is termed pro-pressophysin, and a similar common precursor for OT and its NP is called pro-oxyphysin [29].…”

Section: Discussionmentioning

confidence: 99%

Identification of Neurophysin Immunoreactivity in Hypothalamus by a Monoclonal Antibody to a Carcinoma Cell Surface Antigen

et al. 1990

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Mouse monoclonal antibody (mAb) L6 identifies an antigen expressed on the cell surface of many different human carcinomas. While studying the binding activity of mAb L6 to intracerebral tumor xenografts of human lung carcinoma LX-1 cells in nude rats using immunohistological techniques, we observed that L6 can also bind to a cytoplasmic antigen expressed in the magnocellular component of the hypothalamo-neurohypophysial system. Double-labeling experiments with antisera to vasopressin and oxytocin confirmed the localization of L6 immunoreactivity within both peptide-containing cell groups. L6 immunoreactivity in Brattleboro rats (with genetic deletion in the vasopressin gene) was exclusively localized within oxytocin neurons. Oxytocin and vasopressin failed to block L6 staining which suggested that its target epitope resides within the neurophysin sequence, and this explanation was supported by the finding that adsorption of L6 with porcine neurophysin completely eliminated hypothalamic immunoreactivity. Western blot analysis of bovine neurophysin and human pituitary extracts identified L6-immunoreactive bands which corresponded to the position of neurophysin and pro-pressophysin, confirming that L6 immunoreactivity in hypothalamus is related to neurophysin. Thus, monoclonal antibody L6, which is highly reactive with a membrane antigen of human lung cancer cell line LX-1 recognizes a cytoplasmic epitope in hypothalamic neurons identified as neurophysin by immunohistochemistry and Western analysis.

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Biosynthesis of Vasopressin and Neurophysins

Cited by 22 publications

References 117 publications

Assay for the Measurement of Copeptin, a Stable Peptide Derived from the Precursor of Vasopressin

Assay for the Measurement of Copeptin, a Stable Peptide Derived from the Precursor of Vasopressin

Effect of Cysteamine Injection on Vasopressin and Oxytocin Biosynthesis in Rat Hypothalamus

Identification of Neurophysin Immunoreactivity in Hypothalamus by a Monoclonal Antibody to a Carcinoma Cell Surface Antigen

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