T. Isobe et al., V-DOMAIN DEPOSITION OF LAMBDA-BENCE-JONES PROTEIN IN THE RENAL TUBULAR EPITHELIAL-CELLS IN A PATIENT WITH THE ADULT FANCONI-SYNDROME WITH MYELOMA, Amyloid (Carnforth), 5(2), 1998, pp. 117-120
Citations number
10
Categorie Soggetti
Medicine, General & Internal","Medicine, Research & Experimental",Biology
An extracted Bence Jones lambda protein from a Japanese patient with m
yeloma-associated Fanconi syndrome was found to contain 5 components,
including the dimer and the monomer of the entire light-chain, the dim
er and the monomer of the constant domain, and monomer of the variable
domain. The entire amino acid sequence of this lambda chain was compl
eted. The protein, containing 5 components, was injected intraperitone
ally in C3H mice, 20 mg for 13 days and 200 mg for 3 days. Both groups
pf C3H mice showed a renal proximal tubular deposition of variable do
main fragment of the Bence Jones protein by immunoperoxidase staining.
Other control Bence Jones proteins of the lambda type and serum album
in were negative in terms of deposition in the epithelial tubular cell
s. It is also shown that the proximal tubules of the biopsied kidney f
rom the patient had a deposition of variable domain fragment of Bence
Jones protein. Thus, the myeloma-associated Fanconi syndrome could be
included in the spectrum of light-chain associated disease or monoclon
al Ig deposition disease. This is the first case of lambda type Bence
Jones protein with a complete amino acid sequence analysis found in Fa
nconi syndrome with myeloma, demonstrating the deposition of the varia
ble domain in the proximal tubules of the kidney.