Evidence map›Paper›PMID 25679213›Full record

ArticlePloS one2015

Glycation of human cortical and cancellous bone captures differences in the formation of Maillard reaction products between glucose and ribose.

Grażyna E Sroga, Alankrita Siddula, Deepak Vashishth

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Identification of water compartment in bone using ATR-FTIR spectroscopy.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2026
    Article
  2. Glycoxidation of the bone matrix modulates mineralization.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025
    Article
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  10. Effect of non-enzymatic glycation on collagen nanoscale mechanisms in diabetic and age-related bone fragility.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2023
    Article
  11. Article
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  15. Degradation of Bone Quality in a Transgenic Mouse Model of Alzheimer's Disease.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2022
    Article
  16. Review
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  19. Circadian rhythm disruption with high-fat diet impairs glycemic control and bone quality.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  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

3 authors at 1 institution in 1 country.

Grażyna E SrogaDepartment of Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, United States of America.
Alankrita SiddulaDepartment of Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, United States of America.
Deepak VashishthDepartment of Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, United States of America.
Rensselaer Polytechnic Institute · US

Funding

TISSUE DISTRIBUTION FOR RARE DISEASE RESEARCHU42RR006042 · NCRR · NATIONAL DISEASE RESEARCH INTERCHANGE · PI LONSDALE, JOHN T · 1991 to 2011
$16.5M
Effects of Osteocalcin and Osteopontin on Damage Morphology and Bone FragilityR01AR049635 · NIAMS · RENSSELAER POLYTECHNIC INSTITUTE · PI VASHISHTH, DEEPAK · 2002 to 2014
$3.3M
Collagen Crosslinking Effects on Bone FragilityR01AG020618 · NIA · RENSSELAER POLYTECHNIC INSTITUTE · PI VASHISHTH, DEEPAK · 2005 to 2009
$1.1M
Effects of non-enzymatic glycation and collagen crosslinks on bone fragilityR56AG020618 · NIA · RENSSELAER POLYTECHNIC INSTITUTE · PI VASHISHTH, DEEPAK · 2017 to 2017
$386k
NCRR NIH HHS 5 U42 RR006042NCRR NIH HHS U42 RR006042NIAMS NIH HHS AR49635NIAMS NIH HHS R01 AR049635NIA NIH HHS AG20618NIA NIH HHS R01 AG020618NIA NIH HHS R56 AG020618
6 · The paper itself

Abstract

To better understand some aspects of bone matrix glycation, we used an in vitro glycation approach. Within two weeks, our glycation procedures led to the formation of advanced glycation end products (AGEs) at the levels that corresponded to approx. 25-30 years of the natural in vivo glycation. Cortical and cancellous bones from human tibias were glycated in vitro using either glucose (glucosylation) or ribose (ribosylation). Both glucosylation and ribosylation led to the formation of higher levels of AGEs and pentosidine (PEN) in cancellous than cortical bone dissected from all tested donors (young, middle-age and elderly men and women). More efficient glycation of bone matrix proteins in cancellous bone most likely depended on the higher porosity of this tissue, which facilitated better accessibility of the sugars to the matrix proteins. Notably, glycation of cortical bone from older donors led to much higher AGEs levels as compared to young donors. Such efficient in vitro glycation of older cortical bone could result from aging-related increase in porosity caused by the loss of mineral content. In addition, more pronounced glycation in vivo would be driven by elevated oxidation processes. Interestingly, the levels of PEN formation differed pronouncedly between glucosylation and ribosylation. Ribosylation generated very high levels of PEN (approx. 6- vs. 2.5-fold higher PEN level than in glucosylated samples). Kinetic studies of AGEs and PEN formation in human cortical and cancellous bone matrix confirmed higher accumulation of fluorescent crosslinks for ribosylation. Our results suggest that in vitro glycation of bone using glucose leads to the formation of lower levels of AGEs including PEN, whereas ribosylation appears to support a pathway toward PEN formation. Our studies may help to understand differences in the progression of bone pathologies related to protein glycation by different sugars, and raise awareness for excessive sugar supplementation in food and drinks.

Indexed as

Maillard ReactionAdultAgedAged, 80 and overArginineDisease ProgressionFemaleGlucoseGlycation End Products, AdvancedGlycosylationHumansKineticsLysineMaleMiddle AgedModels, MolecularArginineGlucoseGlycation End Products, AdvancedLysineOsteocalcinpentosidineRibose

Identifiers

PMID25679213
PMCPMC4334514
OpenAlexW2329659082

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.