Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2006 Jan;65(1):101-4.
doi: 10.1136/ard.2004.034348.

Advanced glycation end product modification of bone proteins and bone remodelling: hypothesis and preliminary immunohistochemical findings

G Hein  1 , C Weiss, G Lehmann, T Niwa, G Stein, S Franke
Affiliations

Advanced glycation end product modification of bone proteins and bone remodelling: hypothesis and preliminary immunohistochemical findings

G Hein et al. Ann Rheum Dis. 2006 Jan.

Abstract

Background: The process of bone remodelling is disturbed in the development of osteoporosis.

Objective: To investigate if proteins in osteoporotic bone are modified by advanced glycation end products (AGEs), and whether these alterations are related to measures of bone remodelling based on histomorphometric findings.

Methods: Bone specimens taken from the iliac crest by bone biopsy of eight osteoporotic patients were investigated by histomorphometry and by immunohistochemical staining with the AGEs imidazolone and N(epsilon)-carboxymethyllysine.

Results: Both AGEs were found in all bone specimens. The intensity of staining correlated with patient age. The percentage of bone surface covered with osteoblasts showed a significantly negative correlation with the staining intensity of both AGEs.

Conclusions: It is known that AGEs can regulate proliferation and differentiation of osteoblastic cells and that AGE-specific binding sites are present in cultured osteoblast-like cells. Moreover, AGE induced biological effects in these cells might be mediated by RAGE (receptor of AGE) or by other AGE receptors in different stages of osteoblast development. The inverse relation between AGE staining intensity and the percentage of bone surface covered with osteoblasts in the trabecular bone may provide evidence that AGE modification of bone proteins disturbs bone remodelling.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Parfitt A M. Quantum concept of bone remodeling and turnover: implications for the pathogenesis of osteoporosis. Calcif Tissue Int 1979281–5. - PubMed
    1. Teitelbaum S L, Ross P F. Genetic regulation of osteoclast development and function. Nat Rev Genet 20034638–649. - PubMed
    1. Ulrich P, Cerami A. Protein glycation, diabetes, and aging. Recent Prog Horm Res 2001561–21. - PubMed
    1. Thornalley P J. Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs. Cell Mol Biol (Noisy‐le‐grand) 1998441013–1023. - PubMed
    1. Vlassara H, Palace M R. Diabetes and advanced glycation endproducts. J Intern Med 200225187–101. - PubMed

MeSH terms