Are advanced glycation end-product-modified proteins of pathogenetic
importance in fibromyalgia?

Rheumatology (Oxford) 2002 Oct;41(10):1163-1167

Hein G, Franke S.

Department of Internal Medicine IV, Rheumatology and Osteology,
Friedrich-Schiller-University of Jena, 07740 Jena, Germany.


OBJECTIVE:To quantify the serum levels of the advanced glycation end-product
(AGE) pentosidine in 41 patients with fibromyalgia (FM) and 46 healthy
controls. The formation of pentosidine is closely related to oxidative
stress.

METHODS:Pentosidine was measured by reverse-phased high-performance liquid
chromatography with gradient separation on a RP-18 column.

RESULTS:Patients with FM have significantly higher pentosidine serum levels
than healthy subjects.

CONCLUSION:AGE modification of proteins leads to reduced solubility and high
resistance to proteolytic digestion of such altered proteins (e.g.
AGE-modified collagens). AGEs are also able to stimulate different kinds of
cells via activation of the NFkappaB, mediated by specific receptors of AGEs
(e.g. RAGE) on the cell surface. Both mechanisms may contribute to the
development, perpetuation and spreading of pain phenomena in FM patients.

PMID: 12364637