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.
Aruga
E
E
Department of Surgery, Tokyo Women's Medical College.
Ozasa
H
H
Teraoka
S
S
Ota
K
K
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