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1.
J Neurochem ; 168(7): 1317-1339, 2024 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-38361142

RESUMO

Glycoprotein non-metastatic melanoma protein B (GPNMB) is up-regulated in one subtype of microglia (MG) surrounding senile plaque depositions of amyloid-beta (Aß) peptides. However, whether the microglial GPNMB can recognize the fibrous Aß peptides as ligands remains unknown. In this study, we report that the truncated form of GPNMB, the antigen for 9F5, serves as a scavenger receptor for oligomeric Aß1-42 (o-Aß1-42) in rat primary type 1 MG. 125I-labeled o-Aß1-42 exhibited specific and saturable endosomal/lysosomal degradation in primary-cultured type 1 MG from GPNMB-expressing wild-type mice, whereas the degradation activity was markedly reduced in cells from Gpnmb-knockout mice. The Gpnmb-siRNA significantly inhibits the degradation of 125I-o-Aß1-42 by murine microglial MG5 cells. Therefore, GPNMB contributes to mouse MG's o-Aß1-42 clearance. In rat primary type 1 MG, the cell surface expression of truncated GPNMB was confirmed by a flow cytometric analysis using a previously established 9F5 antibody. 125I-labeled o-Aß1-42 underwent endosomal/lysosomal degradation by rat primary type 1 MG in a dose-dependent fashion, while the 9F5 antibody inhibited the degradation. The binding of 125I-o-Aß1-42 to the rat primary type 1 MG was inhibited by 42% by excess unlabeled o-Aß1-42, and by 52% by the 9F5 antibody. Interestingly, the 125I-o-Aß1-42 degradations by MG-like cells from human-induced pluripotent stem cells was inhibited by the 9F5 antibody, suggesting that truncated GPNMB also serve as a scavenger receptor for o-Aß1-42 in human MG. Our study demonstrates that the truncated GPNMB (the antigen for 9F5) binds to oligomeric form of Aß1-42 and functions as a scavenger receptor on MG, and 9F5 antibody can act as a blocking antibody for the truncated GPNMB.


Assuntos
Peptídeos beta-Amiloides , Glicoproteínas de Membrana , Camundongos Knockout , Microglia , Fragmentos de Peptídeos , Animais , Peptídeos beta-Amiloides/metabolismo , Microglia/metabolismo , Fragmentos de Peptídeos/metabolismo , Glicoproteínas de Membrana/metabolismo , Ratos , Camundongos , Receptores Depuradores/metabolismo , Células Cultivadas , Camundongos Endogâmicos C57BL , Humanos , Ratos Sprague-Dawley , Masculino , Proteínas do Olho
2.
Materials (Basel) ; 13(19)2020 Oct 01.
Artigo em Inglês | MEDLINE | ID: mdl-33019783

RESUMO

In this study, the exothermic temperature performance of various Al/Ni multilayer powders with particle sizes ranging from under 75 to over 850 µm, which generate enormous heat during self-propagating exothermic reactions, was determined using a high-speed sampling pyrometer. The Al/Ni multilayer powders were prepared by a cold-rolling and pulverizing method. The multilayer constitution of the Al/Ni multilayer powders was examined by observing the cross-section of the powders using scanning electron microscopy; the results indicate that the powders had similar lamellar structures regardless of the particle size. Exothermic reactions were carried out to measure the temperature changes during the experiment using a pyrometer. We found that the maximum temperature and the duration of the exothermic reaction increased with an increase in the particle size caused by the heat dissipation of the surface area of the Al/Ni multilayer powder. This indicates that the thermal characteristics of the exothermic reaction of the Al/Ni multilayer powder can be controlled by adjusting the particle size of the Al/Ni multilayer powder. Finally, we concluded that this controllability of the exothermic phenomenon can be applied as a local heating source in a wide range of fields.

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