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Occurrence of prostaglandin D synthase in urine of patients with immunoglobulin light chain amyloidosis (Al amyloidosis)
htemationd
Colloquium on Beta-Truce: Huyuishi
OCCURRENCE OF PROSTAGLANDIN D SYNTHAS E IN URINE OF PATIENTS WITH IXMUNOGICBULIN LIGHT CHAIN AMYM)IDOSIS (AL AM!fLOIDOSIS) C. Murphy, T. Niewold and A. Solomon Human Immunology and Cancer Program: University of Tennessee Medical Center Knoxville Tennessee 37828, USA Light chain amyloidosis (AL amyloidosis) is a plasma cell dyscrasia, characterized by the urinary excretion of monoclonal light chains i. e. Bence often in Jones proteins that are deposited, fragmented form in various organs as amyloid fibrils. This material may be found in kidney, spleen, liver, heart, small intestine, nerve, tongue or other tissue and is responsible for progressive organ dysfunction and eventual death. During the course of isolation by zone electrophoresis and gel filtration of urinary Bence Jones proteins, from patients with AL amyloidos,is, we found an additional component that had the apparent electrophoretic mobility and molecular weight of a light chain. The n-terminal 33 residues were determined by automated sequence analysis and the remaining amino acid sequence was established through'analysis of trypsin and chymotrypsin derived peptides. These analyses revealed the complete primary structure of this molecule to be identical to glutathione independent prostaglandin D synthase. The enzymatic activity was identical to that of the human cerebrospinal fluid prostaglandin D syntha$e. Our finding of a urinary prostaglandin D synthase presumably resulted from amyloid-associated renal disease. However the relationship of this component to amyloidosis remains to be established.
ProstagZundins
1996:51,April
291
Colloquium on Beta-Truce: Huyuishi
OCCURRENCE OF PROSTAGLANDIN D SYNTHAS E IN URINE OF PATIENTS WITH IXMUNOGICBULIN LIGHT CHAIN AMYM)IDOSIS (AL AM!fLOIDOSIS) C. Murphy, T. Niewold and A. Solomon Human Immunology and Cancer Program: University of Tennessee Medical Center Knoxville Tennessee 37828, USA Light chain amyloidosis (AL amyloidosis) is a plasma cell dyscrasia, characterized by the urinary excretion of monoclonal light chains i. e. Bence often in Jones proteins that are deposited, fragmented form in various organs as amyloid fibrils. This material may be found in kidney, spleen, liver, heart, small intestine, nerve, tongue or other tissue and is responsible for progressive organ dysfunction and eventual death. During the course of isolation by zone electrophoresis and gel filtration of urinary Bence Jones proteins, from patients with AL amyloidos,is, we found an additional component that had the apparent electrophoretic mobility and molecular weight of a light chain. The n-terminal 33 residues were determined by automated sequence analysis and the remaining amino acid sequence was established through'analysis of trypsin and chymotrypsin derived peptides. These analyses revealed the complete primary structure of this molecule to be identical to glutathione independent prostaglandin D synthase. The enzymatic activity was identical to that of the human cerebrospinal fluid prostaglandin D syntha$e. Our finding of a urinary prostaglandin D synthase presumably resulted from amyloid-associated renal disease. However the relationship of this component to amyloidosis remains to be established.
ProstagZundins
1996:51,April
291