Enzymatic Cleavage of Glycinamide From Vasopressin and a Proposed Structure for This Pressor-Antidiuretic Hormone of the Posterior Pituitary

Vigneaud, Vincent du; Lawler, H. Claire; Popenoe, Edwin A.

doi:10.1021/ja01115a554

Cited by 274 publications

(64 citation statements)

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“…In contrast, tryptic digestion destroys nearly all of the classical endocrine activities of LVP. This Doepfner, Sturmer & Berde, 1963. is in accord with findings of du Vigneaud et al (1953) with respect to the oxytocic and pressor activity. The recent isolation of DG-LVP from hog pituitaries (Lande et al, 1971) and its ability to restore the behavioural competence of hypophysectomized rats again reveals the importance of neurohypophysial and related hormones in the formation and maintenance of new behavioural patterns.…”

Section: Discussionsupporting

confidence: 81%

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Dissociation of the behavioural and endocrine effects of lysine vasopressin by tryptic digestion

Wied

Greven

Lande

et al. 1972

British J Pharmacology

170

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Section: Discussionsupporting

confidence: 81%

“…12865) by tryptic digestion, since it is well known that this results in a specific cleavage of the c-terminal glycinamide residue (Lawler & du , du Vigneaud, Lawler & Popenoe, 1953. Paper chromatography of this synthetic LVP preparation demonstrated the presence of an immobile spot (RJ=O), together with LVP (RJ=041).…”

Section: Methodsmentioning

confidence: 99%

Dissociation of the behavioural and endocrine effects of lysine vasopressin by tryptic digestion

Wied

Greven

Lande

et al. 1972

British J Pharmacology

170

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“…However, it was not until du Vigneaud and colleagues (1952) isolated the peptide that specific activities could be ascribed. Following this finding, the nine amino acid sequence and structures of Avp (Turner et al, 1951;Archer and du Vigneaud, 1953;du Vigneaud et al, 1953a) and the related hormone oxytocin (Oxt) (Tuppy, 1953;du Vigneaud et al, 1953b) were elucidated, followed shortly by their synthesis (du Vigneaud et al, 1954a;du Vigneaud et al, 1954b). In 1955, du Vigneaud won the Nobel Prize in Chemistry due, in part, to his early descriptions and syntheses of Avp and Oxt.…”

Section: Introductionmentioning

confidence: 99%

Vasopressin: Behavioral roles of an “original” neuropeptide

Caldwell

Lee

Macbeth

et al. 2008

Progress in Neurobiology

427

416

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Vasopressin (Avp) is mainly synthesized in the magnocellular cells of the hypothalamic supraoptic (SON) and paraventricular nuclei (PVN) whose axons project to the posterior pituitary. Avp is then released into the blood stream upon appropriate stimulation (e.g., hemorrhage or dehydration) to act at the kidneys and blood vessels. The brain also contains several populations of smaller, parvocellular neurons whose projections remain within the brain. These populations are located within the PVN, bed nucleus of the stria terminalis (BNST), medial amygdala (MeA) and suprachiasmatic nucleus (SCN).Since the 1950's, research examining the roles of Avp in the brain and periphery has intensified. The development of specific agonists and antagonists for Avp receptors has allowed for a better elucidation of its contributions to physiology and behavior. Anatomical, pharmacological and transgenic, including "knockout," animal studies, have implicated Avp in the regulation of various social behaviors across species.Avp plays a prominent role in the regulation of aggression, generally of facilitating or promoting it. Affiliation and certain aspects of pair-bonding are also influenced by Avp. Memory, one of the first brain functions of Avp that was investigated, has been implicated especially strongly in social recognition. The roles of Avp in stress, anxiety, and depressive states are areas of active exploration. In this review, we concentrate on the scientific progress that has been made on understanding the role of Avp in regulating of these and other behaviors across species, as well as discuss the implications for human behavior.

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“…Found: C, 17.75; H, 3.66; Br, 39.53. Epi-di-thio sarcosine anhydride was a gift from Dr. Ivan Bernal of Brookhaven National Laboratory, and the 4-substituted 1,2-dithiolane (namely, 2-oxa-6,7-dithiaspiro- [3,4] …”

mentioning

confidence: 99%

Disulfide Bond Dihedral Angles from Raman Spectroscopy

Wart

Lewis

Scheraga

et al. 1973

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

169

103

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Raman spectra of several compounds containing the CS-SC moiety were obtained (in the solid phase) from 450-800 cm-' to investigate the S-S and C-S stretching behavior. The S-S stretching frequency varied linearly with the CS-SC dihedral angle (obtained from either x-ray or neutron diffraction or ultraviolet absorption) for compounds whose CC-SS dihedral angles were not very different. The ratio of the intensities of the S-S and C-S stretching bands exhibited no recognizable correlation with either the CS-SC dihedral angle or the CSS bond angle, probably because this ratio is sesisitive to the crystalline environment. The linear dependence of the S-S stretching frequency on dihedral angle leads to a dihedral angle for the plant hormone, malformin A, that is in excellent agreement with that estimated from the longest wavelength CS-SC ultraviolet absorption band.The disulfide bond is an important structural feature of many important biological molecules. The CS-SC moiety occurs in antibiotics such as gliotoxin, sporidesmin, and acetylaranotin in the form of an S-S bridged piperazinedione system in which the CS-SC dihedral angle is severely restricted by ring closure (1, 2). Hormones, such as oxytocin (3), vasopressin (4), and malformin (5), contain disulfide bonds (cystine) that can assume conformations with widely varying dihedral angle, depending upon ring size and other structural constraints. In globular proteins, such as ribonuclease, chymotrypsin, lysozyme, carboxypeptidase, etc., packing requirements may result in dihedral angles that vary substantially from the widely accepted value (6) of about 900 for L-cystine in aqueous solution. In chymotrypsin, for example, this angle varies from 87°-126°(7). It is, therefore, of considerable importance to have a method that can provide information about this dihedral angle both in solid state and in aqueous solution. Raman spectroscopy appears to be a suitable technique for this purpose, since the Raman spectra of compounds containing disulfide bonds usually show welldefined bands that arise from C-S and S-S stretching modes (8,9), and these vibrations might be sensitive to the CS-SC dihedral angle.Absorption spectra can also be used to obtain information about CS-SC dihedral angles, since the relationship between this dihedral angle and the longest-wavelength CS-SC absorption frequency in the ultraviolet is well established both theoretically (10) and experimentally (see references cited in ref. 10). However, this method for determining CS-SC dihedral angles is limited to simple systems in which the UV absorption spectrum is free from nondisulfide-related transitions from about 250 to 380 nm. Many systems (proteins for example, which contain aromatic residues) have nondisulfide chromophores that absorb in this region, and thus prevent study of the CS-SC absorption bands. On the other hand, as t To whom requests for reprints should be addressed. 2619has been pointed out (8, 9), these compounds (including proteins) exhibit S-S and C-S stretching bands in a reg...

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Enzymatic Cleavage of Glycinamide From Vasopressin and a Proposed Structure for This Pressor-Antidiuretic Hormone of the Posterior Pituitary

Cited by 274 publications

References 2 publications

Dissociation of the behavioural and endocrine effects of lysine vasopressin by tryptic digestion

Dissociation of the behavioural and endocrine effects of lysine vasopressin by tryptic digestion

Vasopressin: Behavioral roles of an “original” neuropeptide

Disulfide Bond Dihedral Angles from Raman Spectroscopy

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