Evidence map›Paper›PMID 20717923›Full record

ArticleJournal of cellular biochemistry2010

Role of lysyl oxidase propeptide in secretion and enzyme activity.

Jessica L Grimsby, Hector A Lucero, Philip C Trackman, Katya Ravid, Herbert M Kagan

Abstract read
In one paragraph

Article in Journal of cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

27 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Sex differences and role of lysyl oxidase-like 2 in angiotensin II-induced hypertension in mice.American journal of physiology. Heart and circulatory physiology · 2024
    Article
  3. IGF-II regulates lysyl oxidase propeptide and mediates its effects in part via basic helix-loop-helix E40.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Bioreactors for Vocal Fold Tissue Engineering.Tissue engineering. Part B, Reviews · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Functional importance of lysyl oxidase family propeptide regions.Journal of cell communication and signaling · 2018
    Review
  19. Article
  20. Lysyl Oxidase: Its Diversity in Health and Diseases.Indian journal of clinical biochemistry : IJCB · 2017
    Review
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

5 authors at 1 institution in 1 country.

Jessica L GrimsbyDivision of Oral Biology, Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118, USA.
Hector A Lucero
Philip C Trackman
Katya Ravid
Herbert M Kagan
Boston University · US

Funding

TISSUE CULTURE FACILITY (MAMMALS) --COREP01HL013262 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SMITH, BARBARA A · 1985 to 2007
$12.5M
Mechanisms Regulating Megakaryocyte EndomitosisR01HL080442 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAVID, KATYA · 2006 to 2015
$3.6M
Inhibited Intramembranous Bone Healing in DiabetesR01DE014066 · NIDCR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI TRACKMAN, PHILIP C · 2003 to 2013
$3.0M
NHLBI NIH HHS HL13262-31NHLBI NIH HHS HL80442NHLBI NIH HHS P01 HL013262NHLBI NIH HHS R01 HL080442NIDCR NIH HHS R01 DE014066
6 · The paper itself

Abstract

Lysyl oxidase (LOX) is secreted as a proenzyme (proLOX) that is proteolytically processed in the extracellular milieu to release the propeptide and mature, active LOX. LOX oxidizes lysyl residues of a number of protein substrates in the extracellular matrix and on the cell surface, which impacts several physiological and disease states. Although the LOX propeptide (LOX-PP) is glycosylated, little is known about the role of this modification in LOX secretion and activity. To gain insight into this issue, cells were transfected with native, full-length LOX cDNA (pre-pro-LOX), the N-glycosylation null pre-[N/Q]pro-LOX cDNA and the deletion mutant pre-LOX cDNA, referred to as secretory LOX, in which mature LOX is targeted to the secretory pathway without its N-terminal propeptide sequence. The results show that glycosylation of the LOX-PP is not required for secretion and extracellular processing of pro-LOX but it is required for optimal enzyme activity of the resulting mature LOX. Complete deletion of the propeptide sequence prevents mature LOX from exiting the endoplasmic reticulum (ER). Taken together, our study points out the requirement of the LOX-PP for pro-LOX exit from the ER and is the first to highlight the influence of LOX-PP glycosylation on LOX enzyme activity.

Indexed as

Sequence DeletionAnimalsCHO CellsCricetinaeCricetulusDNA, ComplementaryEndoplasmic ReticulumEnzyme PrecursorsGlycosylationHumansProtein-Lysine 6-OxidaseProtein TransportTransfectionDNA, ComplementaryEnzyme PrecursorsProtein-Lysine 6-Oxidase

Identifiers

PMID20717923
PMCPMC3858906
OpenAlexW2129788789

What OpenQuestion holds

Textmetadata
LicenceTDM
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.