High-performance liquid chromatographic mapping and structural characterization of neurophysin isoforms

Chaiken, Irwin M.; Miller, Ted H.; Sequeira, Reginald P.; Kanmera, Tatsuhiko

doi:10.1016/0003-2697(84)90656-0

Cited by 15 publications

(8 citation statements)

References 21 publications

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“…North et al (1 977) found that, in some strains of rat, OT-Np' in solution could give rise to another by-product, and also demonstrated the conversion of VP-Np to VP-Np'. The molecular nature of the aging events has been somewhat described and seems to correspond to the truncation of the NH2-terminus (Cohen et al, 1979;Chaiken et al, 1984; R. W. Newcomb and J. J. Nordmann, in preparation).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Newly Formed and Aged Granules in the Neurohypophysis

Nordmann

Cazalis

1986

Journal of Neurochemistry

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Neurosecretory granules from the rat and bovine neurohypophysis were isolated and some of their biochemical and biophysical properties studied. Neurosecretory granules (NSG) from rat neurohypophysis were labeled, in vivo, with [35S]cysteine and isolated on isoosmotic gradients. Whereas 1 day after labeling most of the radioactivity was found in the lower part of the gradient, 35 days later the isotope was also located in the lighter NSG-containing fraction. Different analytical procedures showed that the lighter fraction, both in bovine and rat NSG, contain more subpopulations of neurophysin-like material than the heavier fraction. The first material to be released during stimulation of secretion, in vivo or in vitro, is mobilized from the heavy NSG. Isolation of rat NSG, at different times during and after dehydration of the animals, reveals that the newly synthesized material is found in the heavy NSG-containing fraction. Furthermore, the results indicate that the newly synthesized NSG are more resistant to lysis than the lighter granules. The results are discussed in relation to the maturation and degradation processes of the granule content and to the functional state of the NSG.

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Section: Discussionmentioning

confidence: 99%

Characterization of Newly Formed and Aged Granules in the Neurohypophysis

Nordmann

Cazalis

1986

Journal of Neurochemistry

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“…In this context, it may be interesting to note the early reports of a third NP in the rat (125)(126)(127), pig (128,129), cow (130), and sheep (131) neurohypophysis, although it was suggested that this may represent an artifact of isolation/purification procedures, reflecting enzymatic breakdown of NPs. Chaiken et al (132), however, have recently shown multiple isoforms of bovine and human NPs some of which cannot be accounted for by isolation/purification artifacts.…”

Section: Overviewmentioning

confidence: 97%

Arginine Vasopressin (AVP) and AVP-Like Immunoreactivity in Peripheral Tissues

Clements

Funder

1986

Endocrine Reviews

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“…3). The semisynthetic precursor was observed as a doublet, presumably due to the presence of isoforms of BNPII (Chaiken et al, 1984). The identity of the chromatographic peak as semisynthetic precursor was confirmed by amino acid analysis (Table 1).…”

Section: Semisynthesis Of Proavp/npii Precursor and Avp Domain-redesimentioning

confidence: 70%

“…A chromatographic procedure was newly devised to separate BNPII isoforms (Chaiken et al, 1984) and glycopeptide in a single step. Crude extract of pituitary glands was obtained by acid extraction of freeze dried bovine posterior pituitaries, NaCl precipitation and gel filtration on Sephadex (3-75 in 1 M formic acid (Hollenberg and Hope, 1968).…”

Section: Purification Of Neurophysins and G P 1-39 From Bovine Pituitmentioning

confidence: 99%

“…Separation of BNPII and G P 1-39 from BNPI isoforms and other polypeptides was achieved by ion exchange chromatography on DEAE-Trisacryl (LKB, 2.4 x 70 cm) using a linear gradient from 0.1 M (1 L) to 0.5 M (1 L), ammonium acetate pH 6.0. Assignment of eluted peaks to NP's I and I1 was by comparison of chromatographic positions with those of authentic, previously isolated preparations (Chaiken et al, 1984). Fractions containing neurophysin I1 isoforms were pooled, lyophilized and further purified by biospecific adsorption on [Met-Tyr-Phel-Affigel 102 (1 x 7 cm) to remove inactive BNP's.…”

Section: Purification Of Neurophysins and G P 1-39 From Bovine Pituitmentioning

confidence: 99%

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Sequence simplification and the intra‐ and intermolecular self‐recognition properties of vasopressin/neurophysin biosynthetic precursor

Fassina

Chaiken

1989

J of Molecular Recognition

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The self-assembly properties of the arginine 8-vasopressin/bovine neurophysin II (AVP/BNPII) biosynthetic precursor were studied using glycopeptide-deleted and sequence-redesigned semisynthetic derivatives. Semisynthetic precursors were prepared by chemically coupling synthetic vasopressinyl sequence domains and native protein-derived neurophysin II domain. Measurement of precursor-protein association by the extent of affinity chromatographic retardation on agarose-immobilized BNPII verified that the semisynthetic precursor with native AVP sequence has an enhanced self-association propensity similar to that predicted for native precursor. Here, the stabilizing contacts between hormone and neurophysin domains, mainly the positively charged protonated alpha-amino group and tyrosyl 2 side chain of the hormone, are retained. Semisynthetic precursor variants in which the hormone domain is sequence-simplified by introducing alanyl residues in positions not considered important for neurophysin recognition show non-reduced association to BNPII. In contrast, removal of one of the main contact elements between hormone and neurophysin by acetylation of the hormone alpha-amino group abolishes potentiation of precursor self-association. The results show that the presence of the C-terminal glycopeptide sequence domain of native vasopressin precursor is not required to promote self-assembly of the precursor. The data verify the view proposed for the oxytocinyl precursor that intramolecular domain interaction is the triggering event which promotes the increase in affinity of precursor self-association (intermolecular self-recognition). The data also define some of the intramolecular self-recognition elements in the folded precursor required for the high affinity intermolecular self-recognition.

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High-performance liquid chromatographic mapping and structural characterization of neurophysin isoforms

Cited by 15 publications

References 21 publications

Characterization of Newly Formed and Aged Granules in the Neurohypophysis

Characterization of Newly Formed and Aged Granules in the Neurohypophysis

Arginine Vasopressin (AVP) and AVP-Like Immunoreactivity in Peripheral Tissues

Sequence simplification and the intra‐ and intermolecular self‐recognition properties of vasopressin/neurophysin biosynthetic precursor

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