Structure of a guinea pig common precursor to a MSEL-type neurophysin and copeptin

Chauvet, M.T.; Chauvet, Jacqueline; Acher, Roger; Sunde, David; Thorn, Anders

doi:10.1016/0303-7207(86)90130-9

Cited by 23 publications

(7 citation statements)

References 19 publications

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“…The sequence was unusual in containing a Met at position 22 instead of Val in an otherwise highly conserved region of the glycopeptide. This has subsequently been confirmed and extended by the work of Acher and his colleagues who determined the full sequence and showed that guinea-pig CPP is also unusual in being one residue shorter than the other mammalian CPPs analysed to date (14). The Val/Met substitution at position 22 has not been found in other mammalian CPP sequences but has recently been found in the corresponding glycopeptide sequences in amphibia (16).…”

Section: Discussionsupporting

confidence: 61%

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The Carboxy‐Terminal Glycopeptide of the Vasopressin Precursor in the Guinea‐Pig: Release Studies Using a Specific and Sensitive Homologous Radioimmunoassay

Fairhall¹,

Robinson²

1989

J Neuroendocrinology

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The glycopeptide corresponding to the C-terminal portion of the vasopressin precursor (CPP) h a s been isolated from guinea-pig posterior pituitary glands and used to generate a specific and sensitive radioimmunoassay. The antiserum is directed to the peptide rather than sugar moieties, and detects two components in pituitary extracts: CPP itself, and a biosynthetic intermediate (NP-CPP) containing both neurophysin and CPP sequences. Release of CPP from neurointermediate lobes incubated in vitro w a s stimulated five-fold by high K + in a C a 2 + dependent manner: in vivo studies suggest that CPP is released under conditions stimulating vasopressin release. Chronic dehydration depleted neural lobe stores of CPP in parallel with other vasopressin-related components, and plasma levels of CPP were raised from 68+18 to 320k89 fmol/ml (SEM, n=6). In anaesthetized guinea-pigs, intraperitoneal injections of increasing amounts of hypertonic saline increased plasma levels of CPP in a graded manner compared with isotonic saline injections. Acute haemorrhage also stimulated CPP release into plasma, and the half-time of clearance of CPP after infusion to steady state levels in guinea-pig plasma was 24 min. Cerebrospinal fluid withdrawn from the cisterna magna also contained detectable amounts of CPP (390 k 2 5 fmol/ml) suggesting that CPP is released from both hypophysial and extrahypophysial projections. This assay may now be used to study the biosynthesis, processing and release of endogenous CPP under different physiological conditions. The presence of glycosylated substances in the neurohypophysial systcm of a number of species has been demonstrated by a variety of techniques including in vivo incorporation of radiolabelled sugars, chemical and biochemical analysis of pituitary extracts (1)(2)(3)(4)(5). Although closely related amino-acid sequences of a 39-residue pituitary glycopeptide had been deduced for a number of species (4, 5), it was not until the structure of the vasopressin (AVP) precursor was elucidated from its cDNA sequence (6) that this pituitary glycopeptide was recognised as the C-terminal domain of the AVP precursor. linked to the C-terminus of neurophysin (NP) by a single basic residue. Since similar studies of the oxytocin (OT) precursor failed to show an equivalent glycopeptide moiety (7, it appeared that this glycopeptide is only Produced in conjunction with AVP, and immunohistochemical studies confirmed that glycopeptide immunoreactivity was indeed expressed in the AVP, but not OT, neurons in the hypothalamus Although these biochemical and immunocytochemical studies suggest that the glycopeptide is co-localized with AVP, to date there is little direct evidence to show that this glycopeptide is actually released under physiological conditions. Such studies would require a highly sensitive and specific RIA, and whilst antisera have been raised against sheep and human material, sequence comparisons reveal a much higher degree of homology between the glycopeptides from the larger animal species...

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Section: Discussionsupporting

confidence: 61%

“…CPP, C-terminus of propressophysin (8, lo), copeptin (14)). For the sake of uniformity, and because the term 'glycopeptide' is too non-specific, we will adopt the abbreviation CPP in this study.…”

mentioning

confidence: 99%

The Carboxy‐Terminal Glycopeptide of the Vasopressin Precursor in the Guinea‐Pig: Release Studies Using a Specific and Sensitive Homologous Radioimmunoassay

Fairhall¹,

Robinson²

1989

J Neuroendocrinology

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“…Chen et al (74) determined that the crystal structure of vasopressin-associated bovine NPII complex is an asymmetric unit, a pseudotetramer consisting of 2 dimers. The fucosylated glycopeptide portion of the propressophysin molecule was described by Brownstein et al (75) and later named "copeptin" by Acher and Chauvet's group (76).…”

mentioning

confidence: 98%

Diabetes Insipidus: Celebrating a Century of Vasopressin Therapy

et al. 2014

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Diabetes mellitus, widely known to the ancients for polyuria and glycosuria, budded off diabetes insipidus (DI) about 200 years ago, based on the glucose-free polyuria that characterized a subset of patients. In the late 19th century, clinicians identified the posterior pituitary as the site of pathology, and pharmacologists found multiple bioactivities there. Early in the 20th century, the amelioration of the polyuria with extracts of the posterior pituitary inaugurated a new era in therapy and advanced the hypothesis that DI was due to a hormone deficiency. Decades later, a subset of patients with polyuria unresponsive to therapy were recognized, leading to the distinction between central DI and nephrogenic DI, an early example of a hormone-resistant condition. Recognition that the posterior pituitary had 2 hormones was followed by du Vigneaud's Nobel Prize winning isolation, sequencing, and chemical synthesis of oxytocin and vasopressin. The pure hormones accelerated the development of bioassays and immunoassays that confirmed the hormone deficiency in vasopressin-sensitive DI and abundant levels of hormone in patients with the nephrogenic disorder. With both forms of the disease, acquired and inborn defects were recognized. Emerging concepts of receptors and of genetic analysis led to the recognition of patients with mutations in the genes for 1) arginine vasopressin (AVP), 2) the AVP receptor 2 (AVPR2), and 3) the aquaporin 2 water channel (AQP2). We recount here the multiple skeins of clinical and laboratory research that intersected frequently over the centuries since the first recognition of DI.

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“…Processing is generally complete at the level of neurohypophysis because granules isolated from posterior pituitaries contain only mature products (25,26). However, incomplete processing has been detected in guinea pig neurohypophysis, with about 20%o of the vasopressin precursor remaining as a two-domain MSEL-neurophysin-copeptin fragment (27).…”

Section: Resultsmentioning

confidence: 99%

Hydrins, hydroosmotic neurohypophysial peptides: osmoregulatory adaptation in amphibians through vasotocin precursor processing.

Rouillé

Michel

Chauvet

et al. 1989

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

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From neurointermediate pituitary glands of Xenopus laevis and Rana escuknta, previously unreported peptides termed hydrins, active on water permeability of frog urinary bladder and frog skin (Brunn or "water-balance" effect), have been isolated and sequenced. These peptides seem to be derived from the pro-vasotocin-neurophysin precursor. Hydrin 1, found in Xenopus, has been identified as vasotocin C-terminally extended with the Gly-Lys-Arg sequence; hydrin 2, found in Rana, has been identified as vasotocin C-terminally extended with glycine. Hydrin 2 has been detected in several Ranidae (R. esculenta, Rana temporaria, Rana pipiens) and Bufonidae (Bufo bufo, Bufo ictercus) and appears to have a large distribution in terrestrial or semiaquatic anurans. Hydrins, in contrast to vasotocin, are not active on rat uterus or rat blood pressure. They are absent from other vasotocinbearers such as birds and could be involved specifically in water-electrolyte regulation of amphibians.Water-electrolyte regulation in amphibians raised peculiar developmental and evolutionary problems because of the transition from aquatic life to terrestrial conditions. Among order Anura, three families, toads (Bufonidae), frogs (Ranidae), and Xenopus (Pipidae), are mostly terrestrial, semiaquatic, and aquatic, respectively, and could have experienced different molecular adaptations. In nonmammalian tetrapods, the neurohypophysial peptide vasotocin (1-3) is known to play on kidney the antidiuretic role attributed to vasopressin in mammals (4). Furthermore, in frogs and toads, this hormone is also active on urinary bladder, determining water reabsorption across the wall, and on skin, increasing water uptake from hypotonic bathing solutions (Brunn or "water-balance" effect) (5). In these species, aside from vasotocin and mesotocin, which have been chemically characterized in Rana esculenta (1, 6), Rana pipiens (7), and Bufo bufo (2), occurrence of an additional peptide stimulating active sodium transport through the skin ("natriferic effect") has been suggested (8). In Xenopus, however, vasotocin, detected in the posterior pituitary gland (3), is active neither on the bladder nor on the skin ofthis permanently freshwaterdwelling animal in contrast to frogs and toads (5). Therefore, it was of interest to investigate comparatively the maturation of the vasotocin precursor in Rana and Xenopus genera and to look for previously unreported active peptides.In nonmammalian tetrapods, vasotocin is linked to a MSEL-type neurophysin (neurophysin containing methionine-2, serine-3, glutamic acid-6, and leucine-7) in a common precursor (9, 10). This precursor, homologous to the mammalian vasopressin precursor, is processed into two pieces rather than three as is the mammalian one. As a result, along with vasotocin, a "big" neurophysin encompassing two domains homologous to mammalian MSEL-neurophysin and copeptin, respectively, is produced (9, 11). Neurohypophysial peptides of R. esculenta and Xenopus laevis have been examined to specify the vasotocin ...

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Structure of a guinea pig common precursor to a MSEL-type neurophysin and copeptin

Cited by 23 publications

References 19 publications

The Carboxy‐Terminal Glycopeptide of the Vasopressin Precursor in the Guinea‐Pig: Release Studies Using a Specific and Sensitive Homologous Radioimmunoassay

The Carboxy‐Terminal Glycopeptide of the Vasopressin Precursor in the Guinea‐Pig: Release Studies Using a Specific and Sensitive Homologous Radioimmunoassay

Diabetes Insipidus: Celebrating a Century of Vasopressin Therapy

Hydrins, hydroosmotic neurohypophysial peptides: osmoregulatory adaptation in amphibians through vasotocin precursor processing.

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