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

TY - JOUR

T1 - Co-deposition of basement membrane components during the induction of murine splenic AA amyloid.

AU - Lyon, A W

AU - Narindrasorasak, S

AU - Young, I D

AU - Anastassiades, T

AU - Couchman, J R

AU - McCarthy, K J

AU - Kisilevsky, R

N1 - Keywords: Animals; Basement Membrane; Collagen; Fibronectins; Heparan Sulfate Proteoglycans; Heparitin Sulfate; Immunohistochemistry; Laminin; Mice; Proteochondroitin Sulfates; Serum Amyloid A Protein; Spleen

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 2046330

SN - 0023-6837

VL - 64

SP - 785

EP - 790

JO - Laboratory Investigation

JF - Laboratory Investigation

IS - 6

ER -