Evidence map›Paper›PMID 8615794›Full record

ArticleThe Biochemical journal1996

Cellular processing of the nerve growth factor precursor by the mammalian pro-protein convertases.

N G Seidah, S Benjannet, S Pareek, D Savaria, J Hamelin, B Goulet, J Laliberte, C Lazure, M Chrétien, R A Murphy

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

91 citing papers in PubMed, 288 citations in OpenAlex.

  1. Nerve growth factor receptor (NGFR): A key player in glioblastoma progression.Biochimica et biophysica acta. Reviews on cancer · 2026
    Review
  2. Monoclonal antibodies against nitrated nerve growth factor reveal an oxidation-dependent pathogenic hallmark in ALS.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. NGF and Its Role in Immunoendocrine Communication during Metabolic Syndrome.International journal of molecular sciences · 2023
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Role of NGF and its receptors in wound healing (Review).Experimental and therapeutic medicine · 2021
    Review
  19. Review
  20. Article

31 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 1 country.

N G SeidahJ. A. DeSève Laboratories of Biochemical and Molecular Neuroendocrinology, Clinical Research Institute of Montreal, University of Montreal, Canada.
S Benjannet
S Pareek
D Savaria
J Hamelin
B Goulet
J Laliberte
C Lazure
M Chrétien
R A Murphy
Montreal Neurological Institute and Hospital · CAMcGill University · CAMontreal Clinical Research Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to define the enzymes responsible for the maturation of the precursor of nerve growth factor (proNGF), its biosynthesis and intracellular processing by the pro-protein convertases furin, PC1, PC2, PACE4, PC5 and the PC5 isoform PC5/6-B were analysed using the vaccinia virus expression system in cells containing a regulated and/or a constitutive secretory pathway. Results demonstrate that in both cell types furin, and to a lesser extent PACE4 and PC5/6-B, are the best candidate proNGF convertases. Furthermore, two processed NGF forms of 16.5 and 13.5 kDa were evident in constitutively secreting cell lines such as LoVo and BSC40 cells, whereas only the 13.5 kDa form was observed in AtT20 cells, which contain secretory granules. Both forms display the same N-terminal sequence as mature NGF, and were also produced following site-directed mutagenesis of the C-terminal Arg-Arg sequence of NGF into Ala-Ala, suggesting that the difference between them is not at the C-terminus. Co-expression of proNGF with furin and either chromogranin B or secretogranin II (but not chromogranin A) in BSC40 cells eliminated the 16.5 kDa form. Data also show that N-glycosylation of the pro-segment of proNGF and trimming of the oligosaccharide chains are necessary for the exit of this precursor from the endoplasmic reticulum and its eventual processing and secretion. Sulphate labelling experiments demonstrated that proNGF is processed into mature NGF following the arrival of the precursor in the trans-Golgi network. This comparative study shows that the three candidate mammalian subtilisin/kexin-like convertases identified process proNGF into NGF and that the nature of the final processed products is dependent on the intracellular environment.

Indexed as

Nerve Growth FactorProtein Processing, Post-TranslationalAmino Acid SequenceAnimalsBase SequenceCell LineFurinGlycoside HydrolasesHumansMammalsMiceMolecular Sequence DataMutagenesis, Site-DirectedNerve Growth FactorsOligodeoxyribonucleotidesPlasmidsFurinGlycoside HydrolasesNerve Growth FactorNerve Growth FactorsOligodeoxyribonucleotidesPCSK6 protein, humanPcsk6 protein, mousepro-nerve growth factor, humanpro-nerve growth factor, mouseProprotein ConvertasesProtein PrecursorsRecombinant ProteinsSerine EndopeptidasesSubtilisins

Identifiers

PMID8615794
PMCPMC1217149
OpenAlexW1880716631

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.