Renal amyloidosis revisited

TY - JOUR

T1 - Renal amyloidosis revisited

T2 - amyloid distribution, dynamics and biochemical type

AU - Hopfer, Helmut

AU - Wiech, Thorsten

AU - Mihatsch, Michael J

PY - 2011/9/1

Y1 - 2011/9/1

N2 - BACKGROUND: Renal amyloidosis results from protein misfolding and leads to progressive renal insufficiency. Few data are available concerning the relevance of the histomorphological patterns and the dynamics of the disease process.METHODS: Cases of renal amyloidosis in native kidney biopsies (n = 203) were retrospectively evaluated for the pattern of amyloid distribution, the extent of glomerular amyloid deposition and the amount of interstitial fibrosis and tubular atrophy. One hundred and fifty-eight cases were characterized by immunohistochemistry to determine the biochemical amyloid type. Morphological findings were correlated with available clinical data.RESULTS: According to the predominant site of amyloid deposition, 84.6% showed a glomerular, 9.4% a vascular and 6% a tubulointerstitial distribution pattern. Within the glomeruli, amyloid was initially deposited in a focal segmental fashion that became diffuse and global in later stages. Most cases were identified as AL lambda (84/158) or AA (68/158). There was no correlation between the biochemical type and the distribution pattern. Serum creatinine correlated well with interstitial fibrosis and tubular atrophy and proteinuria with the glomerular amyloid load.CONCLUSIONS: The relevance of the different distribution patterns is unclear at the moment, but they may be due to the physicochemical properties of the amyloid fibrils in a given patient. This may become important in future anti-fibrillar therapies.

AB - BACKGROUND: Renal amyloidosis results from protein misfolding and leads to progressive renal insufficiency. Few data are available concerning the relevance of the histomorphological patterns and the dynamics of the disease process.METHODS: Cases of renal amyloidosis in native kidney biopsies (n = 203) were retrospectively evaluated for the pattern of amyloid distribution, the extent of glomerular amyloid deposition and the amount of interstitial fibrosis and tubular atrophy. One hundred and fifty-eight cases were characterized by immunohistochemistry to determine the biochemical amyloid type. Morphological findings were correlated with available clinical data.RESULTS: According to the predominant site of amyloid deposition, 84.6% showed a glomerular, 9.4% a vascular and 6% a tubulointerstitial distribution pattern. Within the glomeruli, amyloid was initially deposited in a focal segmental fashion that became diffuse and global in later stages. Most cases were identified as AL lambda (84/158) or AA (68/158). There was no correlation between the biochemical type and the distribution pattern. Serum creatinine correlated well with interstitial fibrosis and tubular atrophy and proteinuria with the glomerular amyloid load.CONCLUSIONS: The relevance of the different distribution patterns is unclear at the moment, but they may be due to the physicochemical properties of the amyloid fibrils in a given patient. This may become important in future anti-fibrillar therapies.

KW - Adolescent

KW - Adult

KW - Aged

KW - Aged, 80 and over

KW - Amyloidosis

KW - Child

KW - Creatinine

KW - Female

KW - Follow-Up Studies

KW - Glomerular Filtration Rate

KW - Humans

KW - Immunoenzyme Techniques

KW - Kidney Diseases

KW - Kidney Glomerulus

KW - Male

KW - Middle Aged

KW - Prognosis

KW - Retrospective Studies

KW - Young Adult

U2 - 10.1093/ndt/gfq831

DO - 10.1093/ndt/gfq831

M3 - SCORING: Journal article

C2 - 21427073

VL - 26

SP - 2877

EP - 2884

JO - NEPHROL DIAL TRANSPL

JF - NEPHROL DIAL TRANSPL

SN - 0931-0509

IS - 9

ER -