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A brief history of how microscopic studies led to the elucidation of the 3D architecture and macromolecular organization of higher plant thylakoids.
Photosynth Res
September 2020
Plant Biology Section, School of Integrative Plant Science, Cornell University, Ithaca, NY, 14853, USA.
Microscopic studies of chloroplasts can be traced back to the year 1678 when Antonie van Leeuwenhoek reported to the Royal Society in London that he saw green globules in grass leaf cells with his single-lens microscope. Since then, microscopic studies have continued to contribute critical insights into the complex architecture of chloroplast membranes and how their structure relates to function. This review is organized into three chronological sections: During the classic light microscope period (1678-1940), the development of improved microscopes led to the identification of green grana, a colorless stroma, and a membrane envelope.
View Article and Find Full Text PDFRole of the clathrin adaptor PICALM in normal hematopoiesis and polycythemia vera pathophysiology.
Haematologica
April 2015
Division of Hematopoietic Stem Cell and Leukemia Research, Beckman Research Institute of the City of Hope, Duarte, CA, USA Division of Hematology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA
Clathrin-dependent endocytosis is an essential cellular process shared by all cell types. Despite this, precisely how endocytosis is regulated in a cell-type-specific manner and how this key pathway functions physiologically or pathophysiologically remain largely unknown. PICALM, which encodes the clathrin adaptor protein PICALM, was originally identified as a component of the CALM/AF10 leukemia oncogene.
View Article and Find Full Text PDFFundamental technical elements of freeze-fracture/freeze-etch in biological electron microscopy.
J Vis Exp
September 2014
Department of Pediatrics, Center for Environmental Medicine, Asthma, and Lung Biology, The University of North Carolina at Chapel Hill;
Freeze-fracture/freeze-etch describes a process whereby specimens, typically biological or nanomaterial in nature, are frozen, fractured, and replicated to generate a carbon/platinum "cast" intended for examination by transmission electron microscopy. Specimens are subjected to ultrarapid freezing rates, often in the presence of cryoprotective agents to limit ice crystal formation, with subsequent fracturing of the specimen at liquid nitrogen cooled temperatures under high vacuum. The resultant fractured surface is replicated and stabilized by evaporation of carbon and platinum from an angle that confers surface three-dimensional detail to the cast.
View Article and Find Full Text PDFThe origins and evolution of freeze-etch electron microscopy.
J Electron Microsc (Tokyo)
December 2011
Department of Cell Biology, Washington University School of Medicine, St. Louis, MO, USA.
The introduction of the Balzers freeze-fracture machine by Moor in 1961 had a much greater impact on the advancement of electron microscopy than he could have imagined. Devised originally to circumvent the dangers of classical thin-section techniques, as well as to provide unique en face views of cell membranes, freeze-fracturing proved to be crucial for developing modern concepts of how biological membranes are organized and proved that membranes are bilayers of lipids within which proteins float and self-assemble. Later, when freeze-fracturing was combined with methods for freezing cells that avoided the fixation and cryoprotection steps that Moor still had to use to prepare the samples for his original invention, it became a means for capturing membrane dynamics on the millisecond time-scale, thus allowing a deeper understanding of the functions of biological membranes in living cells as well as their static ultrastructure.
View Article and Find Full Text PDFFreeze-etch electron tomography for the plasma membrane interface.
Methods Mol Biol
November 2010
National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan.
To visualize the basal or apical cytoplasmic surface just beneath the plasma membrane, we developed two different methods ("unroof" and "rip-off"). The immunoreplica technique for "unroof" and "rip-off" sample preparation that will be presented in this chapter can determine the distributions of actin, actin-binding proteins, transmembrane proteins, and membrane lipids at the interface of the plasma membrane. We have currently developed freeze-etch electron tomography, which could visualize the 3D molecular architecture of membrane-associated structures (membrane skeleton, clathrin-coated pits, and caveolae) on the cytoplasmic surface of the plasma membrane with 0.
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