scholarly journals Epidermal Cell Surface Structure and Chitin–Protein Co-assembly Determine Fiber Architecture in the Locust Cuticle

2020 ◽  
Vol 12 (23) ◽  
pp. 25581-25590
Author(s):  
Sanja Sviben ◽  
Oliver Spaeker ◽  
Mathieu Bennet ◽  
Marie Albéric ◽  
Jan-Henning Dirks ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Epidermal Cell ◽  
Fiber Architecture ◽  
Cell Surface Structure

Surface Structure of Nucleated Animal Cells: Carbon Replicas

1967 ◽  
Vol 25 ◽  
pp. 120-121
Author(s):  
Robert M. Glaeser ◽  
Thea B. Scott
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Particle Diameter ◽  
Cellular Functions ◽  
Animal Cells ◽  
Replica Technique ◽  
Carbon Replica ◽  
Characteristic Particle ◽  
Cell Surface Structure ◽  
Carbon Replicas

The carbon-replica technique can be used to obtain information about cell-surface structure that cannot ordinarily be obtained by thin-section techniques. Mammalian erythrocytes have been studied by the replica technique and they appear to be characterized by a pebbly or “plaqued“ surface texture. The characteristic “particle” diameter is about 200 Å to 400 Å. We have now extended our observations on cell-surface structure to chicken and frog erythrocytes, which possess a broad range of cellular functions, and to normal rat lymphocytes and mouse ascites tumor cells, which are capable of cell division. In these experiments fresh cells were washed in Eagle's Minimum Essential Medium Salt Solution (for suspension cultures) and one volume of a 10% cell suspension was added to one volume of 2% OsO4 or 5% gluteraldehyde in 0.067 M phosphate buffer, pH 7.3. Carbon replicas were obtained by a technique similar to that employed by Glaeser et al. Figure 1 shows an electron micrograph of a carbon replica made from a chicken erythrocyte, and Figure 2 shows an enlarged portion of the same cell.

Cell surface structure of rodent sperm heads

1975 ◽  
Vol 191 (1) ◽  
pp. 1-8 ◽  
Author(s):  
David M. Phillips
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Cell Surface Structure

New Concepts of the Control of Cell Surface Structure and Function

1983 ◽  
pp. 153-201 ◽  
Author(s):  
Janet M. Oliver ◽  
Joan M. Caron ◽  
Richard D. Berlin
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Structure And Function ◽  
New Concepts ◽  
Cell Surface Structure ◽  
And Function

scholarly journals Cadaverine Covalently Linked to Peptidoglycan Is Required for Interaction between the Peptidoglycan and the Periplasm-Exposed S-Layer-Homologous Domain of Major Outer Membrane Protein Mep45 in Selenomonas ruminantium

2010 ◽  
Vol 192 (22) ◽  
pp. 5953-5961 ◽  
Author(s):  
Seiji Kojima ◽  
Kyong-Cheol Ko ◽  
Yumiko Takatsuka ◽  
Naoki Abe ◽  
Jun Kaneko ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Outer Membrane ◽  
Specific Interaction ◽  
Coiled Coil ◽  
Major Protein ◽  
Rich Region ◽  
Selenomonas Ruminantium ◽  
Covalently Linked ◽  
Cell Surface Structure

ABSTRACT The peptidoglycan of Selenomonas ruminantium is covalently bound to cadaverine (PG-cadaverine), which likely plays a significant role in maintaining the integrity of the cell surface structure. The outer membrane of this bacterium contains a 45-kDa major protein (Mep45) that is a putative peptidoglycan-associated protein. In this report, we determined the nucleotide sequence of the mep45 gene and investigated the relationship between PG-cadaverine, Mep45, and the cell surface structure. Amino acid sequence analysis showed that Mep45 is comprised of an N-terminal S-layer-homologous (SLH) domain followed by α-helical coiled-coil region and a C-terminal β-strand-rich region. The N-terminal SLH domain was found to be protruding into the periplasmic space and was responsible for binding to peptidoglycan. It was determined that Mep45 binds to the peptidoglycan in a manner dependent on the presence of PG-cadaverine. Electron microscopy revealed that defective PG-cadaverine decreased the structural interactions between peptidoglycan and the outer membrane, consistent with the proposed role for PG-cadaverine. The C-terminal β-strand-rich region of Mep45 was predicted to be a membrane-bound unit of the 14-stranded β-barrel structure. Here we propose that PG-cadaverine possesses functional importance to facilitate the structural linkage between peptidoglycan and the outer membrane via specific interaction with the SLH domain of Mep45.

Red cell surface structure: Stabilization by cholesterol sulfate as evidenced by scanning electron microscopy

1975 ◽  
Vol 375 (2) ◽  
pp. 220-223 ◽  
Author(s):  
Gilles Bleau ◽  
Gaston Lalumière ◽  
Alcide Chapdelaine ◽  
Kenneth D. Roberts
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Cell Surface ◽  
Surface Structure ◽  
Red Cell ◽  
Cholesterol Sulfate ◽  
Cell Surface Structure ◽  
Structure Stabilization ◽  
Scanning Electron

Modulation, through a peculiar epitope, of the T-cell surface structure responsible for rosette formation with sheep erythrocytes (E)

1982 ◽  
Vol 5 (2) ◽  
pp. 141
Author(s):  
A. Bernard ◽  
C. Gelin ◽  
M. Amiot ◽  
L. Boumsell
Keyword(s):  
T Cell ◽  
Cell Surface ◽  
Surface Structure ◽  
Rosette Formation ◽  
Sheep Erythrocytes ◽  
Cell Surface Structure

Anomalous cell surface structure of sickle cell anemia erythrocytes as demonstrated by cell surface labeling and endo-β-galactosidase treatment

1981 ◽  
Vol 17 (3) ◽  
pp. 289-297 ◽  
Author(s):  
Minoru Fukuda ◽  
Michiko N. Fukuda ◽  
Sen-Itiroh Hakomori ◽  
Thalia Papayannopoulou
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Sickle Cell ◽  
Sickle Cell Anemia ◽  
Cell Surface Structure
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