Detection of osteopontin as matrix protein in calcium-containing urinary stones.
Osteopontin (OPN) has been identified as a matrix protein of calcium oxalate urinary stones by sequencing c-DNA for urinary stone protein. OPN, a phosphoprotein, is susceptible to thrombin digestion and specifically stainable with Stains-All. We examined the matrix in 4 kinds of urinary stones, calcium oxalate dihydrate, calcium phosphate, magnesium ammonium phosphate and uric acid; for the presence of OPN by staining thrombin-digestion and undigested matrix with Stains-All. Matrix was extracted with a 0.1 M ethylenediamine tetraacetic acid (EDTA) solution. Furthermore, the amino acid sequence was determined for the NH2-terminal 20 amino acid residues. OPN was identified in calcium oxalate dihydrate and calcium phosphate stones, but was absent in magnesium ammonium phosphate and uric acid stones. Our findings suggest that OPN, which binds tightly to hydroxyapatite and is related to bone formation as bone matrix, also participates in the formation of calcium-containing urinary stones.
Yamate
T
T
Department of Urology, Kinki University School of Medicine.
Umekawa
T
T
Iguchi
M
M
Kurita
T
T
Kohri
K
K
D002129:Calcium Oxalate / Q000032:analysis*; D016326:Extracellular Matrix Proteins / Q000032:analysis; D006801:Humans; D053495:Osteopontin; D012795:Sialoglycoproteins / Q000032:analysis*; D014545:Urinary Calculi / Q000737:chemistry*
D016326:Extracellular Matrix Proteins; C506895:SPP1 protein, human; D012795:Sialoglycoproteins; D053495:Osteopontin; D002129:Calcium Oxalate