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Abstract
Previously, the role of the serum amyloid P component (SAP) in the deposition of murine AA amyloid has been examined in SAP-deficient mice in which the deposition was significantly retarded. In this study, AA amyloid fibrillogenesis in SAP-deficient mice was examined ultrastructurally. The fibrils of wild type mice were made up of a microfibril-like main body composed of SAP, chondroitin sulfate proteoglycan (CSPG), and outermost heparan sulfate proteoglycan (HSPG), and associated on its surface were 3 nm wide AA protein ‘helical rods’, a possible suitable form for Congo red staining. In SAP-deficient mice, fibrils of a similar appearance were also noted among an overwhelming amount of amorphous material, but the AP-containing main body of the fibril was replaced by elongated irregular aggregates of CSPG. The mechanism of retardation of AA amyloid induction in SAP-deficient mice has not yet been clear. It may be caused by possible slower formation of a ‘substitute’ core. Also, slower formation of AA helical rods may be possible due to the difference in the core material to which AA protein is attached. If it is so, it may limit the extent of Congo red staining, resulting in underestimation of the actual amount of AA protein.
| Abbreviations | ||
| AEF | = | amyloid enhancing factor |
| CSPG | = | chondroitin sulfate proteoglycan |
| SAP | = | serum amyloid P component |
| Abbreviations | ||
| AEF | = | amyloid enhancing factor |
| CSPG | = | chondroitin sulfate proteoglycan |
| SAP | = | serum amyloid P component |