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Glycation of nail proteins: from basic biochemical findings to a representative marker for diabetic glycation-associated target organ damage

Antoine Sadiki Kishabongo, Philippe Katchunga, Elisabeth Van Aken UGent, Reinhart Speeckaert, Sabrina Lagniau, Renaat Coopman, Marijn Speeckaert UGent and Joris Delanghe UGent (2015) PLOS ONE. 10(3).
abstract
Background : Although assessment of glycated nail proteins may be a useful marker for monitoring of diabetes, their nature and formation are still poorly understood. Besides a detailed anatomical analysis of keratin glycation, the usefulness of glycated nail protein assessment for monitoring diabetic complications was investigated. Methods : 216 patients (94 males, 122 females; mean age +/- standard deviation: 75.0 +/- 8.7 years) were enrolled. Glycation of nail and eye lens proteins was assessed using a photometric nitroblue tetrazolium-based assay. Following chromatographic separation of extracted nail proteins, binding and nonbinding fractions were analyzed using one-dimensional gel electrophoresis. Using a hand piece containing a latch-type-bur, a meticulous cutting of the nail plate into superficial and deep layers was performed, followed by a differential analysis of fructosamine. Results : Using SDS PAGE, four and two bands were identified among the nonglycated and glycated nail fraction respectively. Significantly lower fructosamine concentrations were found in the superficial nail layer (mean: 2.16 +/- 1.37 mu mol/g nails) in comparison with the deep layer (mean: 4.36 +/- 2.55 mu mol/g nails) (P<0.05). A significant higher amount of glycated eye lens proteins was found in diabetes mellitus patients (mean: 3.80 +/- 1.57 mu mol/g eye lens) in comparison with nondiabetics (mean: 3.35 +/- 1.34 mu mol/g eye lens) (P<0.05). A marked correlation was found between glycated nail and glycated eye lens proteins [y (glycated nail proteins) = 0.39 + 0.99 x (eye lens glycated proteins); r(2) = 0.58, P<0.001]. The concentration of glycated eye lens proteins and the HbA1c level were found to be predictors of the concentration of glycated nail proteins. Conclusions : Glycation of nail proteins takes place in the deep layer of finger nails, which is in close contact with blood vessels and interstitial fluid. Glycation of nail proteins can be regarded as a representative marker for diabetic glycation-associated target organ damage.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
NONENZYMATIC GLYCATION, DISSOCIATION MASS-SPECTROMETRY, AFFINITY-CHROMATOGRAPHY, MAILLARD REACTION, STRATUM-CORNEUM, HAIR FOLLICLE, HUMAN PLASMA, EYE LENS, PEPTIDES, COMPLICATIONS
journal title
PLOS ONE
PLoS One
volume
10
issue
3
article number
e0120112
pages
13 pages
Web of Science type
Article
Web of Science id
000351284600129
JCR category
MULTIDISCIPLINARY SCIENCES
JCR impact factor
3.057 (2015)
JCR rank
11/63 (2015)
JCR quartile
1 (2015)
ISSN
1932-6203
DOI
10.1371/journal.pone.0120112
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
6714276
handle
http://hdl.handle.net/1854/LU-6714276
date created
2015-06-15 15:15:29
date last changed
2016-12-21 15:41:20
@article{6714276,
  abstract     = {Background : Although assessment of glycated nail proteins may be a useful marker for monitoring of diabetes, their nature and formation are still poorly understood. Besides a detailed anatomical analysis of keratin glycation, the usefulness of glycated nail protein assessment for monitoring diabetic complications was investigated. 
Methods : 216 patients (94 males, 122 females; mean age +/- standard deviation: 75.0 +/- 8.7 years) were enrolled. Glycation of nail and eye lens proteins was assessed using a photometric nitroblue tetrazolium-based assay. Following chromatographic separation of extracted nail proteins, binding and nonbinding fractions were analyzed using one-dimensional gel electrophoresis. Using a hand piece containing a latch-type-bur, a meticulous cutting of the nail plate into superficial and deep layers was performed, followed by a differential analysis of fructosamine. 
Results : Using SDS PAGE, four and two bands were identified among the nonglycated and glycated nail fraction respectively. Significantly lower fructosamine concentrations were found in the superficial nail layer (mean: 2.16 +/- 1.37 mu mol/g nails) in comparison with the deep layer (mean: 4.36 +/- 2.55 mu mol/g nails) (P{\textlangle}0.05). A significant higher amount of glycated eye lens proteins was found in diabetes mellitus patients (mean: 3.80 +/- 1.57 mu mol/g eye lens) in comparison with nondiabetics (mean: 3.35 +/- 1.34 mu mol/g eye lens) (P{\textlangle}0.05). A marked correlation was found between glycated nail and glycated eye lens proteins [y (glycated nail proteins) = 0.39 + 0.99 x (eye lens glycated proteins); r(2) = 0.58, P{\textlangle}0.001]. The concentration of glycated eye lens proteins and the HbA1c level were found to be predictors of the concentration of glycated nail proteins. 
Conclusions : Glycation of nail proteins takes place in the deep layer of finger nails, which is in close contact with blood vessels and interstitial fluid. Glycation of nail proteins can be regarded as a representative marker for diabetic glycation-associated target organ damage.},
  articleno    = {e0120112},
  author       = {Sadiki Kishabongo, Antoine and Katchunga, Philippe and Van Aken, Elisabeth and Speeckaert, Reinhart and Lagniau, Sabrina and Coopman, Renaat and Speeckaert, Marijn and Delanghe, Joris},
  issn         = {1932-6203},
  journal      = {PLOS ONE},
  keyword      = {NONENZYMATIC GLYCATION,DISSOCIATION MASS-SPECTROMETRY,AFFINITY-CHROMATOGRAPHY,MAILLARD REACTION,STRATUM-CORNEUM,HAIR FOLLICLE,HUMAN PLASMA,EYE LENS,PEPTIDES,COMPLICATIONS},
  language     = {eng},
  number       = {3},
  pages        = {13},
  title        = {Glycation of nail proteins: from basic biochemical findings to a representative marker for diabetic glycation-associated target organ damage},
  url          = {http://dx.doi.org/10.1371/journal.pone.0120112},
  volume       = {10},
  year         = {2015},
}

Chicago
Sadiki Kishabongo, Antoine, Philippe Katchunga, Elisabeth Van Aken, Reinhart Speeckaert, Sabrina Lagniau, Renaat Coopman, Marijn Speeckaert, and Joris Delanghe. 2015. “Glycation of Nail Proteins: From Basic Biochemical Findings to a Representative Marker for Diabetic Glycation-associated Target Organ Damage.” Plos One 10 (3).
APA
Sadiki Kishabongo, A., Katchunga, P., Van Aken, E., Speeckaert, R., Lagniau, S., Coopman, R., Speeckaert, M., et al. (2015). Glycation of nail proteins: from basic biochemical findings to a representative marker for diabetic glycation-associated target organ damage. PLOS ONE, 10(3).
Vancouver
1.
Sadiki Kishabongo A, Katchunga P, Van Aken E, Speeckaert R, Lagniau S, Coopman R, et al. Glycation of nail proteins: from basic biochemical findings to a representative marker for diabetic glycation-associated target organ damage. PLOS ONE. 2015;10(3).
MLA
Sadiki Kishabongo, Antoine, Philippe Katchunga, Elisabeth Van Aken, et al. “Glycation of Nail Proteins: From Basic Biochemical Findings to a Representative Marker for Diabetic Glycation-associated Target Organ Damage.” PLOS ONE 10.3 (2015): n. pag. Print.