Real-Space Imaging of the Tailored Plasmons in Twisted Bilayer Graphene.

We report a systematic plasmonic study of twisted bilayer graphene (TBLG)-two graphene layers stacked with a twist angle. Through real-space nanoimaging of TBLG single crystals with a wide distribution of twist angles, we find that TBLG supports confined infrared plasmons that are sensitively dependent on the twist angle. At small twist angles, TBLG has a plasmon wavelength comparable to that of single-layer graphene. At larger twist angles, the plasmon wavelength of TBLG increases significantly with apparently lower damping. Further analysis and modeling indicate that the observed twist-angle dependence of TBLG plasmons in the Dirac linear regime is mainly due to the Fermi-velocity renormalization, a direct consequence of interlayer electronic coupling. Our work unveils the tailored plasmonic characteristics of TBLG and deepens our understanding of the intriguing nano-optical physics in novel van der Waals coupled two-dimensional materials.

Serum amyloid A in Alzheimer's disease brain is predominantly localized to myelin sheaths and axonal membrane.

Immunohistochemical localization of the injury specific apolipoprotein, acute phase serum amyloid A (A-apoSAA), was compared in brains of patients with neuropathologically confirmed Alzheimer's disease (AD), multiple sclerosis (MS), Parkinson's disease (PD); Pick's disease (Pick's), dementia with Lewy bodies (DLB), coronary artery disease (CAD), and schizophrenia. Affected regions of both AD and MS brains showed intense staining for A-apoSAA in comparison to an unaffected region and non-AD/MS brains. The major site of A-apoSAA staining in both diseases was the myelin sheaths of axons in layers V and VI of affected cortex. A-apoSAA contains a cholesterol binding site near its amino terminus and is likely to have a high affinity for cholesterol-rich myelin. These findings, along with our recent evidence that A-apoSAA can inhibit lipid synthesis in vascular smooth muscle cells suggest that A-apoSAA plays a role in the neuronal loss and white matter damage occurring in AD and MS.

Calreticulin is transported to the surface of NG108-15 cells where it forms surface patches and is partially degraded in an acidic compartment.

Although calreticulin (Crt) is primarily localized to the endoplasmic reticulum (ER), our results using biotinylation and immunocytochemical methods indicate that a small but significant amount of Crt is present and forms large patches on the surface of NG108-15 cells (a mouse neuroblastoma-rat glioma hybrid cell line). (35)S-labelled Crt molecules begin to reach the cell surface after only 10 min of labelling and disappear slowly from the cell surface. After 4 hr of labelling, approximately half of the newly synthesized Crt molecules are on the cell surface. We believe that some Crt molecules may escape from the KDEL receptor-mediated salvage pathway as they are synthesized and proceed through the secretory pathway to the cell surface. Immunoprecipitation from the culture medium shows that Crt is not released from the cell surface to the medium, suggesting tight binding to surface molecules. NH(4)Cl can block the degradation of Crt; therefore, Crt is presumably degraded in the lysosome pathway. However, blockage of the disappearance of surface Crt is less efficient than that of internal Crt. This suggests that the disappearance of Crt from the cell surface may not be due solely to its degradation, but may reflect transport into another cell compartment such as the ER.

KDEL proteins are found on the surface of NG108-15 cells.

Although KDEL proteins are primarily localized to the endoplasmic reticulum (ER), we have employed surface biotinylation method to demonstrate that the KDEL proteins calreticulin (Crt), protein disulfide isomerase (PDI) and the 78-kDa glucose regulated protein (GRP78) are found on the surface of the NG108-15 cell line. In contrast, the 94-kDa glucose regulated protein (GRP94), another KDEL protein, is not found on the cell surface. Calnexin (Cnx), a type-1 integral transmembrane ER protein which is partially homologous to Crt but lacks the KDEL sequence, is not detected on the cell surface either. While only small amounts of the total GRP78, PDI and Crt molecules exist on the cell surface at steady state, a significant fraction of the newly synthesized molecules are transported to the cell surface and transport of these proteins is inhibited by treatment with brefeldin A. The surface GRP78 contains the KDEL sequence. On the cell surface, GRP78, PDI and Crt associate with other proteins and form complexes of different sizes. Surface Crt is found to be essential for the neurite formation when NG108-15 cells are induced to differentiate using dibutyryl cAMP.