Macromolecules that are colocalized with deposits of beta 2-microglobulin in hemodialysis-associated amyloidosis.
BACKGROUND
Common elements in many different types of amyloid may have important roles in amyloidogenesis. The proteinaceous tissue deposits have a common appearance in polarized light and other similar features. The present investigation describes for the first time the relation between beta 2-microglobulin (beta 2-M)-type amyloidosis and colocalized materials, as demonstrated using specific antibodies and hyaluronan-binding protein.


METHODS
Amyloid-rich carpal tunnel synovium was obtained surgically from 28 patients who were being treated by maintenance hemodialysis. Serial sections were examined using a hyaluronan (hyaluronic acid)-binding protein and antibodies against heparan sulfate-glycosaminoglycan, chondroitin sulfate-proteoglycan, dermatan sulfate-proteoglycan, alpha 1-antichymotrypsin, alpha 1-antitrypsin, inter-alpha-trypsin inhibitor, haptoglobin, and ubiquitin.


RESULTS
Accumulation of hyaluronan was of three types, namely, localization around beta 2-M deposits, colocalization with deposition of beta 2-M itself and localization at a small distance from beta 2-M deposits. Immunostaining for heparan sulfate glycosaminoglycan was demonstrated at the sites of beta 2-M plaques. Chondroitin sulfate-proteoglycan did not show specific patterns of immunostaining, resembling hyaluronan rather than heparan sulfate. The other materials tested, alpha 1-antichymotrypsin, alpha 1-antitrypsin, inter-alpha-trypsin, haptoglobin and ubiquitin, were not immunostained at sites of beta 2-M plaques. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting revealed that the molecular weight of heparan sulfate-glycosaminoglycan was 16,000.


CONCLUSIONS
These results suggest that HS has an important role in hemodialysis-associated amyloidosis as it does in other types of amyloidosis. Moreover, accumulation of hyaluronan may be an indication of inflammation of the carpal synovium.
Department of Surgery, Tokyo Women's Medical College.
E
E
Aruga
H
H
Ozasa
S
S
Teraoka
K
K
Ota
D000686:Amyloidosis / Q000209:etiology* / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000378:metabolism; D006242:Haptoglobins / Q000378:metabolism; D006497:Heparan Sulfate / Q000378:metabolism; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism; D046911:Macromolecular Substances; D011480:Protease Inhibitors / Q000378:metabolism; D006435:Renal Dialysis / Q000009:adverse effects*; D014018:Tissue Distribution; D014452:Ubiquitins / Q000378:metabolism; D001613:beta 2-Microglobulin / Q000378:metabolism*
D006025:Glycosaminoglycans; D006242:Haptoglobins; D006497:Heparan Sulfate; D006820:Hyaluronic Acid; D046911:Macromolecular Substances; D011480:Protease Inhibitors; D014452:Ubiquitins; D001613:beta 2-Microglobulin