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

Sroga GE, Siddula A, Vashishth D - PLoS ONE (2015)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, United States of America.

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.

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Related in: MedlinePlus

Kinetics of fluorescent AGEs formation.The content of fAGEs was determined in human cortical (blue diamonds) and cancellous (red squares) bone after glycation using glucose (A and B) or ribose (C and D) for the male (61 M) and the female (59 F) donor.
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pone.0117240.g006: Kinetics of fluorescent AGEs formation.The content of fAGEs was determined in human cortical (blue diamonds) and cancellous (red squares) bone after glycation using glucose (A and B) or ribose (C and D) for the male (61 M) and the female (59 F) donor.

Mentions: Kinetics of the fAGEs formation was followed for cortical and cancellous bone tissues originating from the 61 year-old male and the 59 year-old female donor. The levels of fAGEs were measured for glucosylation (Fig. 6A and B) and ribosylation (Fig. 6C and D). We observed that after approx. one day of the induction period (a lag phase), the formation of fluorescent AGEs increased steadily in cortical as well as cancellous bone until beginning to approach the plateau around the 14th day of incubation (Fig. 6). The half-time of fluorescent AGEs formation in the bone matrix was 6 to 7 days for ribose and 20 to 22 days for glucose.


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

Sroga GE, Siddula A, Vashishth D - PLoS ONE (2015)

Kinetics of fluorescent AGEs formation.The content of fAGEs was determined in human cortical (blue diamonds) and cancellous (red squares) bone after glycation using glucose (A and B) or ribose (C and D) for the male (61 M) and the female (59 F) donor.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4334514&req=5

pone.0117240.g006: Kinetics of fluorescent AGEs formation.The content of fAGEs was determined in human cortical (blue diamonds) and cancellous (red squares) bone after glycation using glucose (A and B) or ribose (C and D) for the male (61 M) and the female (59 F) donor.
Mentions: Kinetics of the fAGEs formation was followed for cortical and cancellous bone tissues originating from the 61 year-old male and the 59 year-old female donor. The levels of fAGEs were measured for glucosylation (Fig. 6A and B) and ribosylation (Fig. 6C and D). We observed that after approx. one day of the induction period (a lag phase), the formation of fluorescent AGEs increased steadily in cortical as well as cancellous bone until beginning to approach the plateau around the 14th day of incubation (Fig. 6). The half-time of fluorescent AGEs formation in the bone matrix was 6 to 7 days for ribose and 20 to 22 days for glucose.

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, United States of America.

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.

Show MeSH
Related in: MedlinePlus