Neurophysins: Molecular and Cellular Aspects

Acher, Roger

doi:10.1002/anie.197908461

Cited by 22 publications

(7 citation statements)

References 78 publications

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“…The affinity constant of NPII for the immobilized peptide increased markedly with increasing amounts of applied protein and with the addition of small amounts of soluble ligand, the latter being more pronounced at higher protein concentrations. The affinity constant of the protein for the N e u r o p h ysins, a class of disulfide-rich acidic proteins, are synthesized in the hypothalamus and then transported via axons to the posterior pituitary, in neurosecretory granules, as parts of noncovalent complexes with the peptide hormones oxytocin (OXT)' and VP (Seif & Robinson, 1978;Acher, soluble ligand showed a smaller increase. The variation of l / ( V -V,) (where V = the NPII elution volume and V, = the elution volume of noninteracting control protein) with soluble ligand concentration was linear except near [ligand] = 0.…”

Section: Interdependence Of Neurophysin Self-association and Neuropepmentioning

confidence: 99%

Interdependence of neurophysin self-association and neuropeptide hormone binding as expressed by quantitative affinity chromatography

Angal¹,

Chaiken²

1982

Biochemistry

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The reciprocal modulation of neurophysin self-association and noncovalent peptide--protein interaction between neurophysin and the hormones oxytocin and vasopressin has been assessed by quantitative affinity chromatography. Competitive elutions of radiolabeled bovine neurophysin II (NPII) from the affinity matrices Met-Tyr-Phe-omega-(amino-hexyl)- [and (aminobutyl)-] agarose were performed with increasing concentrations of either of the soluble ligands oxytocin or lysine-vasopressin. Also, the dependence of NPII retardation by the same adsorbents on the concentration of applied protein was investigated in the absence of soluble ligand. The affinity constant of NPII for the immobilized peptide increased markedly with increasing amounts of applied protein and with the addition of small amounts of soluble ligand, the latter being more pronounced at higher protein concentrations. The affinity constant of the protein for the soluble ligand showed a smaller increase. The variation of l/(V - V0) (where V = the NPII elution volume and V0 = the elution volume of noninteracting control protein) with soluble ligand concentration was linear except near [ligand] = 0. The quantitative affinity chromatographic results on the tripeptidyl affinity columns are consistent with the view that NPII exists in a monomer in equilibrium dimer equilibrium, with the dimer exhibiting a stronger interaction with both neuropeptide and tripeptide analogues. The data also indicate that the self-associated protein dimer itself exhibits cooperativity, that is, stronger binding of the immobilized ligand at one site when a second site is occupied with a molecule of the soluble ligand than when no soluble ligand is bound. The deduction from the above of ligand-induced dimerization is evident also in the increased retardation of NPII on neurophysin--Sepharose when the eluting buffer contains soluble peptide hormone.

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Section: Interdependence Of Neurophysin Self-association and Neuropepmentioning

confidence: 99%

Interdependence of neurophysin self-association and neuropeptide hormone binding as expressed by quantitative affinity chromatography

Angal¹,

Chaiken²

1982

Biochemistry

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“…We have found that trypsin treatment of disulfide-intact neurophysins effects a rapid loss, complete within 3 h at 37"C, of interaction functions, measured as a loss of ability to stimulate retardation of [1251]neurophysin on Met-Tyr-Phe-aminohexylagarose. Reverse-phase HPLC analysis of tryptic digests of neurophysin I allows detection of two major protein products and the peptide fragment (1)(2)(3)(4)(5)(6)(7)(8). Release of the latter N-terminal piece occurs at about the same rate as loss of interaction function.…”

Section: Structural Characteristics Of Binding Surfacesmentioning

confidence: 99%

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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“…(1980) have given strong support to the hypothesis of common precursors for neurohypophyseal hormones and nemophysins. Furthermore, the cosecretion of argininevasopressin and MSELneurophysin in man (Chauvet et al, 1979) suggests specific tandems and two types of precursors (for recent reviews on neurophysins, see Acher, 1979. It seems therefore of great interest to check whether the three hormones of Macropodidae are accompanied by three distinct neurophysins and whether the duplication of vasopressin is associated with the duplication of MSELneurophysin.…”

Section: Neurohypoph Yseal Hormone Precursorsmentioning

confidence: 99%

PHYLOGENY OF NEUROHYPOPHYSEAL HORMONES. Vasopressin Polymorphism in Three Kangaroo Species

Chauvet

Hurpet

Chauvet

et al. 1981

International Journal of Peptide and Protein Research

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The neurohypophyseal hormones of three species of Australian marsupials belonging to the family Macropodidae (Macropus rufus, Macropus giganteus, Macropus robustus). have been investigated. In these species three active peptides have been disclosed, one with oxytocic activity and two with pressor activity. The three hormones are present in all the individual glands which have been examined. Purification has been undertaken by ion‐exchange chromatography and paper chromatoelectrophoresis. The more abundant of the pressor hormones (about 80% of the total pressor activity) has been identified as lysine‐vasopressin by its biological properties, its chromatographic behaviour and its amino acid composition. The second pressor principle, more basic, has not yet been chemically characterized but its pharmacological properties and its chromatographic behaviour suggest that it is closely related or identical to arginine‐vasopressin. Dimorphism of vasopressins seems peculiar to Metatheria since it has not been observed in Protheria and very rarely in Eutheria.

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Neurophysins: Molecular and Cellular Aspects

Cited by 22 publications

References 78 publications

Interdependence of neurophysin self-association and neuropeptide hormone binding as expressed by quantitative affinity chromatography

Interdependence of neurophysin self-association and neuropeptide hormone binding as expressed by quantitative affinity chromatography

Neurophysin–neuropeptide hormone complexes: Biosynthetic origin and noncovalent interactions

PHYLOGENY OF NEUROHYPOPHYSEAL HORMONES. Vasopressin Polymorphism in Three Kangaroo Species

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