Amyloid A (AA) amyloidosis is a lethal disease characterized by systemic AA amyloid deposition, and it reported in many animal species. Despite experiments have shown that AA amyloidosis can be transmitted orally, horizontal transmission and cross-species transmission are concerns, the transmission mechanism has been unknown. In this study, we examined the oral transmission efficiency of AA amyloidosis using oxazolone-induced gastrointestinal disorder mice. As a result, the upper or lower gastrointestinal disorder groups developed more severe amyloid deposition in systemic tissues than the group without gastrointestinal disorders. The results of this study suggest that gastrointestinal damage promotes the oral transmission of AA amyloidosis.

Medical sheets are useful in surgically repair vascular disease. To avoid long-term side effects, they are to be replaced with regenerated tissue after implantation. Silk fibroin is a fibrous protein secreted by silkworm. The advantage of silk fibroin is its biocompatibility and has been used as regenerative artificial materials. The problem of its biodegradability is that the effect is time consuming. In this study, SVVYGLR peptide was used to expect promoting cell migration and accelerating the biodegradation of silk fibroin. Silk fibroin and polyurethane-based medical sheets with or without SVVYGLR peptide were implanted in rat abdominal aorta (silk fibroin/polyurethane/SVVYGLR peptide versus silk fibroin/polyurethane). The result of histological evaluation indicated that the new cell layer created under both sheets was composed of endothelial cells, smooth muscle, and fibroin in both sheets and similar to a native vessel. Both sheets did not show any excessive inflammation or calcification, and moderate biodegradability was observed. The decrease of silk fibroin indicated the biodegradability of all sheets. Silk fibroin/polyurethane/SVVYGLR peptide had many small vessels in the regenerated tissue than silk fibroin/polyurethane. This appearance indicated that SVVYGLR peptide promoted the angiogenesis in the regenerative tissue. This study suggested that SVVYGLR peptide could give the angiogenic-promoting activity to silk fibroin-based vascular repairing sheet.

In AA amyloidosis, cross-species oral transmission has been demonstrated in several animal models. While it is known that the transmission efficiency of AA amyloidosis between different species is lower than that among the same species, the mechanism of this species-barrier is unclear. In this study, we found at first that mice orally given a large amount of bovine AA simultaneously with inflammatory stimulation did not develop AA amyloidosis. Therefore, we hypothesized that the low efficiency of the cross-species oral transmission of AA amyloidosis might be due to the low absorption rate in Peyer’s patches. To evaluate the hypothesis, we next investigated whether bovine AA was taken up by Peyer’s patches and translocated to other organs in vivo and ex vivo models. The direct absorption of bovine AA by Peyer’s patches was not observed. Besides, translocation of bovine AA to the mesenteric lymph nodes, spleen, liver, or kidney was not observed except the mesenteric lymph node of a single mouse. Thus, absorption of bovine AA by Peyer’s patches occurred much less efficiently in mouse models of cross-species oral transmission of AA amyloidosis. The present study suggests that the less efficient amyloid uptake by Peyer’s patches may be involved in the species-barrier of oral transmission of AA amyloidosis.

Amyloidosis is diagnosed by the histologic detection of amyloid deposits; however, this method has limitations such as a prolonged diagnosis time and the need for histologic proficiency. We aimed to develop a rapid and simple method for diagnosing amyloidosis by targeting amyloid-specific endogenous fluorescence, which has not been reported previously, to our knowledge. Fluorescence fingerprint analysis of amyloid extracts and tissue homogenates derived from amyloid A (AA) amyloidosis-affected cattle exhibited a specific intrinsic fluorescence pattern. Furthermore, principal component analysis using analytical data revealed that AA could be identified by peaks near λex 350 nm and λem 430 nm. Fluorescence spectrometry analysis using tissue homogenates, which does not require special histochemical staining, enables the rapid detection of bovine AA.