Evidence map›Paper›PMID 35368589›Full record

ArticleKidney3602020

Mannose Binding Lectin Is Hydroxylated by Collagen Prolyl-4-hydroxylase and Inhibited by Some PHD Inhibitors.

Vijesh J Bhute, James Harte, Jack W Houghton, Patrick H Maxwell

Open access · diamondAbstract read
In one paragraph

Article in Kidney360, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

8 citing papers in PubMed, 9 citations in OpenAlex.

  1. Trial
  2. Article
  3. Navigating Anemia Therapy in CKD With Hypoxia-Inducible Factor Activators: A Review.American journal of kidney diseases : the official journal of the National Kidney Foundation · 2026
    Review
  4. Review
  5. Review
  6. Roxadustat: Not just for anemia.Frontiers in pharmacology · 2022
    Review
  7. Applications of mannose-binding lectins and mannan glycoconjugates in nanomedicine.Journal of nanoparticle research : an interdisciplinary forum for nanoscale science and technology · 2022
    Review
  8. 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

4 authors at 2 institutions in 2 countries.

Vijesh J BhuteCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0001-9441-7963
James HarteDepartment of Biological Sciences, Cork Institute of Technology, Cork, Ireland.
Jack W HoughtonCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Patrick H MaxwellCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-0338-2679
University of Cambridge · GBUniversity College Cork · IE

Funding

Wellcome Trust 096956/Z
6 · The paper itself

Abstract

Background: Mannose-binding lectin (MBL) is an important component of innate immune defense. MBL undergoes oligomerization to generate high mol weight (HMW) forms which act as pattern recognition molecules to detect and opsonize various microorganisms. Several post-translational modifications including prolyl hydroxylation are known to affect the oligomerization of MBL. Yet, the enzyme(s) which hydroxylate proline in the collagen-like domain residues have not been identified and the significance of prolyl hydroxylation is incompletely understood. Methods: To investigate post-translational modifications of MBL, we stably expressed Myc-DDK tagged MBL in HEK293S cells. We used pharmacologic and genetic inhibition of 2-oxoglutarate-dependent dioxygenases (2OGDD) to identify the enzyme required for prolyl hydroxylation of MBL. We performed mass spectrometry to determine the effects of various inhibitors on MBL modifications. Results: Secretion of HMW MBL was impaired by inhibitors of the superfamily of 2OGDD, and was dependent on prolyl-4-hydroxylase subunit Conclusions: These data suggest that prolyl hydroxylation in the collagen-like domain of MBL is mediated by collagen prolyl-4-hydroxylase. Reduced MBL activity is likely to be an off-target effect of some, but not all, prolyl hydroxylase domain (PHD) inhibitors. There may be advantages in selective PHD inhibitors that would not interfere with MBL production.

Indexed as

Prolyl-Hydroxylase InhibitorsCollagenHypoxia-Inducible Factor-Proline DioxygenasesProcollagen-Proline DioxygenaseProlyl HydroxylasesCollagenHypoxia-Inducible Factor-Proline DioxygenasesProcollagen-Proline DioxygenaseProlyl-Hydroxylase InhibitorsProlyl Hydroxylaseschronic kidney diseasecollagen prolyl-4-hydroxylaseFG-4592HEK293 cellshypoxia inducible factormannose binding lectinPHD inhibitorspost-translationalprotein processingrenal anemiavadadustat; molidustat

Identifiers

PMID35368589
PMCPMC8809307
OpenAlexW3014611841

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.