scholarly journals Cholesterol-dependent partitioning of PtdIns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa)

2004 ◽  
Vol 379 (3) ◽  
pp. 527-532 ◽  
Author(s):  
Richard M. EPAND ◽  
Phan VUONG ◽  
Christopher M. YIP ◽  
Shohei MAEKAWA ◽  
Raquel F. EPAND
Keyword(s):  
Membrane Protein ◽  
Fluorescence Microscopy ◽  
Fluorescence Spectroscopy ◽  
Membrane Domains ◽  
Domain Formation ◽  
Membrane Domain ◽  
Terminal Fragment ◽  
N Terminus ◽  
Total Internal Reflectance ◽  
Internal Reflectance

A myristoylated peptide corresponding to the N-terminus of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa) causes the quenching of the fluorescence of BODIPY®-TMR-labelled PtdIns(4,5)P2 in bilayers of 1-palmitoyl-2-oleoyl phosphatidylcholine containing 40 mol% cholesterol and 0.1 mol% BODIPY®–PtdIns(4,5)2. Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy revealed the cholesterol-dependent nature of PtdIns(4,5)P2-enriched membrane-domain formation.

scholarly journals Elucidation of Perovskite Film Micro-Orientations Using Two-Photon Total Internal Reflectance Fluorescence Microscopy

2015 ◽  
Vol 6 (16) ◽  
pp. 3283-3288 ◽  
Author(s):  
Brianna R. Watson ◽  
Bin Yang ◽  
Kai Xiao ◽  
Ying-Zhong Ma ◽  
Benjamin Doughty ◽  
...  
Keyword(s):  
Fluorescence Microscopy ◽  
Two Photon ◽  
Total Internal Reflectance ◽  
Internal Reflectance

An integrated multi-wavelength SCATTIRSTORM microscope combining TIRFM and IRM modalities for imaging cellulases and other processive enzymes

2021 ◽  
Author(s):  
Daguan Nong ◽  
Zachary K. Haviland ◽  
Kate Vasquez Kuntz ◽  
Ming Tien ◽  
Charles T. Anderson ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Fluorescence Microscopy ◽  
Motor Proteins ◽  
Custom Software ◽  
Multi Wavelength ◽  
Degradative Enzymes ◽  
Total Internal Reflectance ◽  
Internal Reflectance

AbstractWe describe a multimodal SCATTIRSTORM microscope for visualizing processive enzymes moving on immobilized substrates. The instrument combines Interference Reflection Microscopy (IRM) with multi-wavelength Total Internal Reflectance Fluorescence Microscopy (TIRFM). The microscope can localize quantum dots with a precision of 2.8 nm at 100 frames/s, and was used to image the dynamics of the cellulase, Cel7a interacting surface-immobilized cellulose. The instrument, which was built with off-the-shelf components and controlled by custom software, is suitable for tracking other degradative enzymes such as collagenases, as well as motor proteins moving along immobilized tracks.

Compartmentalization, processing and redistribution of the plasma membrane protein CE9 on rodent spermatozoa. Relationship of the annulus to domain boundaries in the plasma membrane of the tail

1994 ◽  
Vol 107 (2) ◽  
pp. 561-570 ◽  
Author(s):  
M.M. Cesario ◽  
J.R. Bartles
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Domain Boundary ◽  
Immunogold Electron Microscopy ◽  
Membrane Domains ◽  
Tail Domain ◽  
Membrane Domain ◽  
Plasma Membrane Protein ◽  
Plasma Membrane Domain

Western blotting, immunofluorescence and immunogold electron microscopy were used to examine the compartmentalization, processing and redistribution of the integral plasma membrane protein CE9 on the spermatozoa of rats, mice and hamsters. In each species examined, spermatozoal CE9 was found to undergo endoproteolytic processing followed by a net redistribution from the posterior-tail domain into the anterior-tail domain of the plasma membrane during epididymal maturation. Compared to spermatozoa of the rat and mouse, those of the hamster were found to express a greater proportion of their CE9 within the anterior-tail plasma membrane domain at all stages of maturation. As a consequence, CE9 was judged to be a suitable marker for two different spermatozoal plasma membrane domains: the posterior-tail plasma membrane domain (spermatozoa from the testis and caput epididymidis of the rat and mouse) and the anterior-tail domain (spermatozoa from the cauda epididymidis of the hamster). Immunogold electron microscopy was used to pinpoint the positions of the boundaries of these CE9-containing plasma membrane domains at a high level of resolution. In each case, the position of the CE9 domain boundary was found to be strongly correlated with that of the subplasmalemmal electron-dense ring known as the annulus. The precise spatial relationship between the CE9 domain boundary and the annulus was, however, found to differ significantly among species and/or as a function of maturation.

FEATURES

2016 ◽  
Vol 20 (12) ◽  
pp. 12-22
Keyword(s):  
Medical Imaging ◽  
Fluorescence Microscopy ◽  
Fluorescence Spectroscopy ◽  
Medical Images ◽  
Light Sheet ◽  
The Future ◽  
Light Sheet Fluorescence Microscopy

Scanning the Future of Medical Imaging Putting Numbers into Biology: The Combination of Light Sheet Fluorescence Microscopy and Fluorescence Spectroscopy Abyss Processing – Exploring the Deep in Medical Images

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