Evidence map›Paper›PMID 22573318›Full record

ArticleThe Journal of biological chemistry2012

Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance.

Marnisa Sricholpech, Irina Perdivara, Megumi Yokoyama, Hideaki Nagaoka, Masahiko Terajima, Kenneth B Tomer, Mitsuo Yamauchi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
6.5field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 96 citations in OpenAlex.

  1. Type VIII collagen: advances in matrix biology and translational promise.Frontiers in bioengineering and biotechnology · 2025
    Pooled it
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  14. Collagen fibril formationMaterials today. Bio · 2022
    Review
  15. Article
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  18. Article
  19. The roles of collagen in chronic kidney disease and vascular calcification.Journal of molecular medicine (Berlin, Germany) · 2021
    Review
  20. 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

7 authors at 3 institutions in 1 country.

Marnisa SricholpechNorth Carolina Oral Health Institute, School of Dentistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Irina Perdivara
Megumi Yokoyama
Hideaki Nagaoka
Masahiko Terajima
Kenneth B Tomer
Mitsuo Yamauchi
University of North Carolina at Chapel Hill · USNational Institute of Environmental Health Sciences · USNational Institutes of Health · US

Funding

Protein Characterization By Mass SpectrometryZIAES050171 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI TOMER, KENNETH · 2009 to 2013
$2.9M
Protein Characterization By Mass SpectrometryZ01ES050171 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI TOMER, KENNETH · 2000 to 2008
$1.1M
Lysyl Oxidase Control of TGF-? in BoneR21DE019569 · NIDCR · UNIV OF NORTH CAROLINA CHAPEL HILL · PI YAMAUCHI, MITSUO · 2009 to 2010
$407k
Matrix-assisted Craniofacial Bone RegenerationR21DE020909 · NIDCR · UNIV OF NORTH CAROLINA CHAPEL HILL · PI YAMAUCHI, MITSUO · 2011 to 2012
$406k
Collagen Glycosylation, Maturation and MineralizationR21AR060978 · NIAMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI YAMAUCHI, MITSUO · 2012 to 2013
$352k
Intramural NIH HHS Z01 ES050171NIAMS NIH HHS AR060978NIAMS NIH HHS R21 AR060978NIDCR NIH HHS DE020909NIDCR NIH HHS R21 DE019569NIDCR NIH HHS R21 DE020909
6 · The paper itself

Abstract

Recently, by employing the short hairpin RNA technology, we have generated MC3T3-E1 (MC)-derived clones stably suppressing lysyl hydroxylase 3 (LH3) (short hairpin (Sh) clones) and demonstrated the LH3 function as glucosyltransferase in type I collagen (Sricholpech, M., Perdivara, I., Nagaoka, H., Yokoyama, M., Tomer, K. B., and Yamauchi, M. (2011) Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture. J. Biol. Chem. 286, 8846-8856). To further elucidate the biological significance of this modification, we characterized and compared type I collagen phenotypes produced by Sh clones and two control groups, MC and those transfected with empty vector. Mass spectrometric analysis identified five glycosylation sites in type I collagen (i.e. α1,2-87, α1,2-174, and α2-219. Of these, the predominant glycosylation site was α1-87, one of the major helical cross-linking sites. In Sh collagen, the abundance of glucosylgalactosylhydroxylysine was significantly decreased at all of the five sites with a concomitant increase in galactosylhydroxylysine at four of these sites. The collagen cross-links were significantly diminished in Sh clones, and, for the major cross-link, dihydroxylysinonorleucine (DHLNL), glucosylgalactosyl-DHLNL was diminished with a concomitant increase in galactosyl-DHLNL. When subjected to in vitro incubation, in Sh clones, the rate of decrease in DHLNL was lower, whereas the rate of increase in its maturational cross-link, pyridinoline, was comparable with controls. Furthermore, in Sh clones, the mean diameters of collagen fibrils were significantly larger, and the onset of mineralized nodule formation was delayed when compared with those of controls. These results indicate that the LH3-mediated glucosylation occurs at the specific molecular loci in the type I collagen molecule and plays critical roles in controlling collagen cross-linking, fibrillogenesis, and mineralization.

Indexed as

AnimalsCalcification, PhysiologicCells, CulturedCollagen Type ICross-Linking ReagentsGlucaric AcidGlycosylationHydroxylysineIsoenzymesMass SpectrometryMiceMicroscopy, Electron, TransmissionOsteoblastsProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseProtein-Lysine 6-OxidaseRNA, Small InterferingCollagen Type ICross-Linking ReagentsGlucaric AcidHydroxylysineIsoenzymeslysyl hydroxylase 3, mouseProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseProtein-Lysine 6-OxidaseRNA, Small Interfering

Identifiers

PMID22573318
PMCPMC3391079
OpenAlexW2009402410

What OpenQuestion holds

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Registered trials

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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.