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DOI: 10.1055/s-0028-1105868
© Georg Thieme Verlag KG Stuttgart · New York
Einfluss proteolytischer Enzyme auf Advanced Glycation Endproducts (AGEs) – Mögliche klinische Implikationen?
Effects of proteolytic enzymes on advanced glycation end-products (AGE): possible clinical applicationsPublikationsverlauf
eingereicht: 11.12.2007
akzeptiert: 6.11.2008
Publikationsdatum:
11. Dezember 2008 (online)

Unter den Risikofaktoren kardiovaskulärer, metabolischer und onkologischer Erkrankungen gewinnen die Advanced Glycation Endproducts (AGEs) zunehmendes Interesse. Die Bildung dieser Verzuckerungsprodukte erfolgt einerseits durch die nichtenzymatische Reaktion zwischen reduzierenden Zuckern und freien Aminogruppen von Proteinen, Lipiden und Aminosäuren, andererseits durch oxidativen Stress. Da AGEs als heterogene Substanzgruppe, methodisch nicht leicht zu bestimmen sind, hat ihre Analytik noch keinen Eingang in die Routinediagnostik gefunden. Dies könnte sich durch die neuen AGE-Reader ändern, mit denen sich der AGE-Gehalt der Haut, der die AGE-Last des Körpers reflektiert, nicht-invasiv innerhalb von Minuten bestimmen lässt.
Literatur
- 1
Uribarri J, Cai W, Sandu O, Peppa M, Goldberg T, Vlassara H.
Diet-derived advanced
glycation end products are major contributors to the body’s
AGE pool and induce inflammation in healthy subjects.
Ann
N Y Acad Sci.
2005;
1043
461-466
Reference Ris Wihthout Link
- 2
Bierhaus A, Humpert P, Stern D, Arnold B, Nawroth P P.
Advanced glycation end product receptor-mediated cellular dysfunction.
Ann NY Acad Sci.
2005;
1043
676-680
Reference Ris Wihthout Link
- 3
Heidland A, Sebekova K, Schinzel R.
Advanced glycation end products and the progressive course of
renal disease.
Am J Kidney Dis.
2001;
38
S100-S106
Reference Ris Wihthout Link
- 4
Sebeková K, Wagner Z, Schupp N, Boor P.
Genomic damage and malignancy
in end-stage renal failure: do advanced glycation end products contribute?.
Kidney Blood Press Res.
2007;
30
56-66
Reference Ris Wihthout Link
- 5
Takeuchi M, Yamagishi S.
Possible involvement
of advanced glycation end-products (AGEs) in the pathogenesis of
Alzheimer’s disease.
Curr Pharm Des.
2008;
14
973-978
Reference Ris Wihthout Link
- 6
Foell D, Wittkowski H, Roth J.
Mechanisms of disease: a „DAMP” view of inflammatory
arthritis.
Nat Clin Pract Rheumatol.
2007;
3
382-390
Reference Ris Wihthout Link
- 7
Xiang G, Schinzel R, Simm A, Münch G, Sebekova K. et al .
Advanced glycation end products (AGEs)-induced
expression of TGFß1 is suppressed by a protease in the
tubule cell line LLC-PK1.
Nephrol Dial Transplant.
2001;
16
1562-1569
Reference Ris Wihthout Link
- 8
Ling H, Vamvakas S, Busch G, Dämmrich J, Schramm L, Lang F, Heidland A.
Suppressing role of transforming growth factorbeta 1 on cathepsin
activity in cultured kidney tubule cells.
Am J Physiol.
1995;
269
F911-917
Reference Ris Wihthout Link
- 9
Sebeková K, Schinzel R, Ling H, Simm A, Xiang G, Gekle M, Münch G, Vamvakas S, Heidland A.
Advanced glycated albumin impairs protein degradation in the
kidney proximal tubules cell line LLC-PK1.
Cell Mol Biol
(Noisy-le-grand).
1998;
44
1051-1060
Reference Ris Wihthout Link
- 10
Stopper H, Schinzel R, Sebeková K, Heidland A.
Genotoxicity of advanced
glycation end products in mammalian cells.
Cancer Letters.
2003;
190
151-156
Reference Ris Wihthout Link
- 11
Stopper H, Schupp N, Bahner U, Sebekova K, Klassen A, Heidland A.
Genomic damage in end-stage
renal failure: potential involvement of advanced glycation end products and
carbonyl stress.
Semin Nephrol.
2004;
24
474-478
Reference Ris Wihthout Link
- 12
Schupp N, Schinzel R, Heidland A, Stopper H.
Genotoxicity of advanced
glycation end products – potential involvement of AT 1
receptors.
Ann NY Acad Sci.
2005;
1043
685-695
Reference Ris Wihthout Link
- 13
Park L, Raman K G, Lee K J. et al .
Suppression of accelerated
diabetic atherosclerosis by the soluble receptor for advanced glycation
endproducts.
Nat Med.
1998;
4
1025-1031
Reference Ris Wihthout Link
- 14
Taguchi A, Blood D C, del Toro G. et al .
Blockade of RAGE-amphoterin signalling
suppresses tumour growth and metastases.
Nature.
2000;
405
354-360
Reference Ris Wihthout Link
- 15
Yan S D, Chen X, Fu J, Chen M, Zhu H. et al .
RAGE
and amyloid-b; peptide neurotoxicity in Alzheimer’s disease.
Nature.
1996;
382
685-691
Reference Ris Wihthout Link
- 16
Paczek L, Soin J, Bartolomiejczyk I, Krolak R, Lao M, Heidland A.
Impairment of proteolytic activity
in isolated glomeruli and tubules in experimental diabetic nephropathy.
Clin Nephrol.
1996;
46
258-260
Reference Ris Wihthout Link
- 17
Sebeková K, Dämmrich J, Fierlbeck W, Krivosiková Z, Paczek L, Heidland A.
Effect
of chronic therapy with proteolytic enzymes on hypertension-induced
renal injury in the rat model of Goldblatt hypertension.
Am
J Nephrol.
1998;
18
570-576
Reference Ris Wihthout Link
- 18
Sebeková K, Dämmrich J, Krivosíková Z, Heidland A.
The
effect of oral protease administration in the rat remnant kidney model.
Res Exp Med (Berl).
1999;
199
177-188
Reference Ris Wihthout Link
Prof. Dr. August Heidland
Med. Univ.-Klinik Würzburg und Kuratorium
für Dialyse und Nierentransplantation
Hans-Brandmann-Weg
1
97080 Würzburg
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