Co-deposition of basement membrane components during the induction of murine splenic AA amyloid

Lab Invest. 1991 Jun;64(6):785-90.


Past studies have demonstrated that during murine AA amyloid induction there is co-deposition of the AA amyloid peptide and the basement membrane form of heparan sulfate proteoglycan. The synthesis and accumulation of heparan sulfate proteoglycan does not usually occur in the absence of other basement membrane components, such as type IV collagen, laminin, and fibronectin. Using immunohistochemical techniques, the present experiments have demonstrated that in addition to the heparan sulfate proteoglycan, there are other basement membrane components present in splenic AA amyloid deposits and these are present as soon as AA amyloid deposits are detectable. The results indicate that within the time constraints imposed by the experiments, the basement membrane components, fibronectin, laminin, type IV collagen, and heparan sulfate proteoglycan are co-deposited 36 to 48 hours after the AgNO3 and amyloid enhancing factor induction of amyloid, the period when amyloid is first detected. These observations raise the possibility that an abnormality in basement membrane metabolism is a very early event, and potentially plays an integral part in the process of AA amyloidogenesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Basement Membrane / metabolism*
  • Chondroitin Sulfate Proteoglycans / metabolism
  • Collagen / metabolism
  • Fibronectins / metabolism
  • Heparan Sulfate Proteoglycans
  • Heparitin Sulfate / metabolism
  • Immunohistochemistry
  • Laminin / metabolism
  • Mice
  • Serum Amyloid A Protein / metabolism*
  • Spleen / metabolism*


  • Chondroitin Sulfate Proteoglycans
  • Fibronectins
  • Heparan Sulfate Proteoglycans
  • Laminin
  • Serum Amyloid A Protein
  • Collagen
  • Heparitin Sulfate