Evidence map›Paper›PMID 8300415›Full record

ArticleJournal of anatomy1993

Novel peptides from adrenomedullary chromaffin vesicles.

J Sigafoos, W G Chestnut, B M Merrill, L C Taylor, E J Diliberto, O H Viveros

Abstract read
In one paragraph

Article in Journal of anatomy, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Exploring the Sea Urchin Neuropeptide Landscape by Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Identification of peptides from brain and pituitary of Cpe(fat)/Cpe(fat) mice.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  10. Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  11. Article
  12. Article
  13. Accumulation of Hg(II) Ions in Mouse Adrenal Gland.Pathology oncology research : POR · 1996
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

J SigafoosDivision of Pharmacology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.
W G Chestnut
B M Merrill
L C Taylor
E J Diliberto
O H Viveros
Burroughs Wellcome Fund · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The adrenal medulla chromaffin vesicle (CV) contains, on a weight basis, as much soluble protein and peptide as catecholamine. The bulk of the protein is accounted for by chromogranins (Cgr) A, B and C. Additionally, a large variety of neuropeptides and their precursor proteins have been found recently within these vesicles. Nevertheless, fractionation of CV lysates indicates the presence of many more peptides than previously reported. In the hope of finding novel bioactive peptides, we initiated a systematic isolation and characterisation of CV peptides. Bovine CV pellets were prepared by sucrose gradient centrifugation and immediately boiled in water to avoid degradation of native proteins and peptides. The water lysates were fractionated through a battery of reversed-phase and ion-exchange high-performance chromatographic steps. We fully or partially characterised a substantial number of novel peptides derived from CgrA and CgrB. A tetradecapeptide and a 13 kDa extended peptide were derived from the bovine homologue of rat secretogranin III. Peptides corresponding to C-terminal fragments of 7B2 and proteoglycan II were also found. Additionally, several sequences had no known precursors. Of the sequences derived from known precursors some corresponded to fragments bracketed by pairs of basic amino acids, but others were preceded or followed by single basic residues or by unusual putative cleavage sites. Some of these peptides were postranslationally modified (pyroglutamylation, glycosylation, phosphorylation, amidation). A significant degree of structural conservation of some of these peptides across species suggests that they may exert biological effects when cosecreted with catecholamines during splanchnic stimulation.

Indexed as

Adrenal MedullaAmino Acid SequenceAnimalsCattleChromaffin GranulesChromogranin AChromograninsDecorinExtracellular Matrix ProteinsMolecular Sequence DataPeptidesProteinsProteoglycansRatsSequence AlignmentSwineChromogranin AChromograninsDcn protein, ratDecorinExtracellular Matrix ProteinsPeptidesProteinsProteoglycans

Identifiers

PMID8300415
PMCPMC1259906
OpenAlexW1568712429

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.