-transparent.png){kind=logo}
Advanced protein glycation has been proposed as a major factor in the development of diabetic nephropathy. Advanced glycation end products (AGEs) have altered the structure of extracellular matrix component and impaired self association in vitro. To elucidate the role of AGEs in the progression of diabetic nephropathy, the present study was undertaken to localize glomerular AGEs immunohistochemically. Ultrastructural changes of the mesangial matrix were analyzed with high resolution scanning electron microscopy. No glomerular AGEs staining was noted in normal control kidney specimens, or in tissue from glomerulonephritis patients without diabetes mellitus. The mesangium showed a positive AGEs staining in advanced stages of diabetic nephropathy, and the most characteristic finding was the strong AGEs staining in nodular lesions. By high resolution scanning electron microscopy, control and diabetic mesangial matrices revealed a meshwork structure composed of fine fibrils (10 nm in width) and numerous pores (12 to 13 nm in diameter). In the nodular lesions, however, loosening of the meshwork was significant, and the diameter of the pores was enlarged (approximately 24 nm). This study provides the first immunohistochemical evidence that AGEs are localized in diabetic glomeruli, most notably to nodular lesions. Advanced glycation might play a role in the progression of diabetic nephropathy through impairment of the assembly of matrix proteins in vivo.
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
February 1996,
Journal of the American Society of Nephrology : JASN,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
April 1995,
The Western journal of medicine,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
August 1993,
Molecular and cellular biochemistry,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
April 2008,
Annals of the New York Academy of Sciences,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
August 1988,
FEBS letters,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
August 1987,
Experimental and clinical endocrinology,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
April 2006,
Laboratory investigation; a journal of technical methods and pathology,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
August 1986,
Clinica chimica acta; international journal of clinical chemistry,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
July 2010,
American journal of physiology. Renal physiology,
H Makino, and
K Shikata, and
K Hironaka, and
M Kushiro, and
Y Yamasaki, and
H Sugimoto, and
Z Ota, and
N Araki, and
S Horiuchi
February 1999,
Cellular and molecular biology (Noisy-le-Grand, France),
