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Are advanced glycation end-product-modified proteins of pathogenetic importance in fibromyalgia?
Rheumatology (Oxford) 2002; 41(10):1163-7R

Abstract

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.

Authors+Show Affiliations

Department of Internal Medicine IV, Rheumatology and Osteology, Friedrich-Schiller-University of Jena, 07740 Jena, Germany.No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12364637

Citation

Hein, G, and S Franke. "Are Advanced Glycation End-product-modified Proteins of Pathogenetic Importance in Fibromyalgia?" Rheumatology (Oxford, England), vol. 41, no. 10, 2002, pp. 1163-7.
Hein G, Franke S. Are advanced glycation end-product-modified proteins of pathogenetic importance in fibromyalgia? Rheumatology (Oxford). 2002;41(10):1163-7.
Hein, G., & Franke, S. (2002). Are advanced glycation end-product-modified proteins of pathogenetic importance in fibromyalgia? Rheumatology (Oxford, England), 41(10), pp. 1163-7.
Hein G, Franke S. Are Advanced Glycation End-product-modified Proteins of Pathogenetic Importance in Fibromyalgia. Rheumatology (Oxford). 2002;41(10):1163-7. PubMed PMID: 12364637.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Are advanced glycation end-product-modified proteins of pathogenetic importance in fibromyalgia? AU - Hein,G, AU - Franke,S, PY - 2002/10/5/pubmed PY - 2002/11/26/medline PY - 2002/10/5/entrez SP - 1163 EP - 7 JF - Rheumatology (Oxford, England) JO - Rheumatology (Oxford) VL - 41 IS - 10 N2 - 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. SN - 1462-0324 UR - https://www.unboundmedicine.com/medline/citation/12364637/full_citation L2 - https://academic.oup.com/rheumatology/article-lookup/doi/10.1093/rheumatology/41.10.1163 DB - PRIME DP - Unbound Medicine ER -