Covalent attachment of soluble proteins by nonenzymatically glycosylated collagen. Role in the in situ formation of immune complexes

doi:10.1084/jem.158.5.1739

This Article

	Full Text (PDF, 459K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JEM
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Brownlee, M.
	Articles by Cerami, A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Brownlee, M.
	Articles by Cerami, A.


Social Bookmarking

	What's this?

ARTICLES

Covalent attachment of soluble proteins by nonenzymatically glycosylated collagen. Role in the in situ formation of immune complexes

M Brownlee, S Pongor and A Cerami

The chronic tissue damage associated with long-term diabetes mellitus may arise in part from in situ immune complex formation by accumulated immunoglobulins and/or antigens bound to long-lived structural proteins that have undergone excessive nonenzymatic glycosylation. In this report, we have tested this hypothesis using nonenzymatically glycosylated collagen. Binding of both albumin and IgG averaged four times the amount bound to unmodified collagen. Both albumin and IgG (anti-BSA) bound to nonenzymatically glycosylated collagen retained their ability to form immune complexes in situ with free antibody and antigen.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Sell, D. R., Monnier, V. M. (2004). Conversion of Arginine into Ornithine by Advanced Glycation in Senescent Human Collagen and Lens Crystallins. J. Biol. Chem. 279: 54173-54184 [Abstract] [Full Text]
Bierhaus, A., Hofmann, M. A, Ziegler, R., Nawroth, P. P (1998). AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus. I. The AGE concept. Cardiovasc Res 37: 586-600 [Abstract] [Full Text]
Takahashi, M., Pischetsrieder, M., Monnier, V. M. (1997). Isolation, Purification, and Characterization of Amadoriase Isoenzymes (Fructosyl Amine-oxygen Oxidoreductase EC 1.5.3) from Aspergillus sp.. J. Biol. Chem. 272: 3437-3443 [Abstract] [Full Text]
Elgawish, A., Glomb, M., Friedlander, M., Monnier, V. M. (1996). Involvement of Hydrogen Peroxide in Collagen Cross-linking by High Glucose in Vitro and in Vivo. J. Biol. Chem. 271: 12964-12971 [Abstract] [Full Text]
Palinski, W., Koschinsky, T., Butler, S. W., Miller, E., Vlassara, H., Cerami, A., Witztum, J. L. (1995). Immunological Evidence for the Presence of Advanced Glycosylation End Products in Atherosclerotic Lesions of Euglycemic Rabbits. Arterioscler. Thromb. Vasc. Bio. 15: 571-582 [Abstract] [Full Text]
Brownlee, M, Vlassara, H, Kooney, A, Ulrich, P, Cerami, A (1986). Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 232: 1629-1632 [Abstract]
BROWNLEE, M., VLASSARA, H., CERAMI, A. (1984). Nonenzymatic Glycosylation and the Pathogenesis of Diabetic Complications. ANN INTERN MED 101: 527-537 [Abstract]