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Volume 272, Number 7, Issue of February 14, 1997 pp. 4037-4042
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Accumulation of Pyrraline-modified Albumin in Phagocytes due to Reduced Degradation by Lysosomal Enzymes

(Received for publication, July 9, 1996, and in revised form, October 28, 1996)

From the The Second Department of Internal Medicine, Kobe University School of Medicine, 7-5-1, Kusunoki-cho, Chuo-ku, Kobe 650, Japan

Previous studies suggested that the interaction between proteins modified by advanced glycation end products (AGEs) and cells, such as macrophages, may be involved in diabetic angiopathy. Pyrraline is one of the AGEs and known to be elevated in plasma of diabetic rats and humans, and is present in vascular lesions of diabetic and elderly subjects. We examined whether modification of albumin by pyrraline influences its degradation by macrophage-like cell line, P388D₁ cells. Degradation of pyrraline-modified albumin by these cells was diminished, causing accumulation of the albumin in these cells. The susceptibility of pyrraline-modified albumin to lysosomal proteolytic enzymes was reduced by approximately 40% in vitro, while lysosomal activity in the cells per se was not affected. This phenomenon was also observed when human monocytes were used instead of P388D₁ cells. Our results suggest that accumulation of pyrraline-modified albumin in P388D₁ cells is due to the reduced susceptibility of the protein to lysosomal enzymatic degradation. Such alterations in the interaction between AGEs-modified protein and phagocytes may contribute to angiopathy in elderly subjects and patients with diabetes.

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