scholarly journals Expression of a cell surface immobilization antigen during serotype transformation in Tetrahymena thermophila.

1985 ◽  
Vol 5 (8) ◽  
pp. 1925-1932 ◽  
Author(s):  
N E Williams ◽  
F P Doerder ◽  
A Ron
Keyword(s):  
Cell Surface ◽  
Microsomal Fraction ◽  
Cytochalasin B ◽  
Actinomycin D ◽  
Tetrahymena Thermophila ◽  
Temperature Shift ◽  
Surface Immobilization ◽  
Immobilization Antigen ◽  
A Cell ◽  
Major Surface

A temperature shift from 40 to 28 degrees C rapidly induced expression of a specific immobilization antigen at the cell surface in Tetrahymena thermophila. This transformation was inhibited by actinomycin D and cycloheximide but not by colchicine or cytochalasin B. The major surface antigen expressed at 28 degrees C in cells homozygous for the SerH3 allele was partially purified, and an antiserum against this preparation was raised in rabbits. Electrophoresis, immunoblot, and [35S]methionine incorporation studies are reported which support the conclusion that the H3 antigen is an acidic protein with an Mr of approximately 52,000 daltons. An induced synthesis of the H3 immobilization antigen was detected within 30 min after a shift from 40 to 28 degrees C. This protein appeared to be synthesized in the microsomal fraction and transferred without cleavage to the cell surface, where it was inserted first into nonciliated regions.

Expression of a cell surface immobilization antigen during serotype transformation in Tetrahymena thermophila

1985 ◽  
Vol 5 (8) ◽  
pp. 1925-1932
Author(s):  
N E Williams ◽  
F P Doerder ◽  
A Ron
Keyword(s):  
Cell Surface ◽  
Microsomal Fraction ◽  
Cytochalasin B ◽  
Actinomycin D ◽  
Tetrahymena Thermophila ◽  
Temperature Shift ◽  
Surface Immobilization ◽  
Immobilization Antigen ◽  
A Cell ◽  
Major Surface

A temperature shift from 40 to 28 degrees C rapidly induced expression of a specific immobilization antigen at the cell surface in Tetrahymena thermophila. This transformation was inhibited by actinomycin D and cycloheximide but not by colchicine or cytochalasin B. The major surface antigen expressed at 28 degrees C in cells homozygous for the SerH3 allele was partially purified, and an antiserum against this preparation was raised in rabbits. Electrophoresis, immunoblot, and [35S]methionine incorporation studies are reported which support the conclusion that the H3 antigen is an acidic protein with an Mr of approximately 52,000 daltons. An induced synthesis of the H3 immobilization antigen was detected within 30 min after a shift from 40 to 28 degrees C. This protein appeared to be synthesized in the microsomal fraction and transferred without cleavage to the cell surface, where it was inserted first into nonciliated regions.

Cytoskeletal involvement in the sequential capping of rat thymocyte surface glycoproteins

1988 ◽  
Vol 89 (3) ◽  
pp. 309-319
Author(s):  
C.E. Turner ◽  
M.R. Newton ◽  
D.M. Shotton
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Cytoskeletal Proteins ◽  
The Other ◽  
A Cell ◽  
Major Surface ◽  
Surface Glycoproteins

The independent capping of the three major rat thymocyte glycoproteins, the leucocyte-common (L-C) antigen, the leucocyte sialoglycoprotein (LSGP) and Thy-1, was investigated using specific monoclonal antibodies. The capping of each antigen did not require redistribution of the other major surface glycoproteins, and was accompanied by a partial co-capping of the cytoskeletal proteins fodrin and actin, but not of tubulin. A study of the ability of a cell that already possesses one glycoprotein cap to cap a second different glycoprotein showed that this was possible in all cases to varying degrees, the second cap always forming at the same position on the cell surface as the first. Colchicine failed to perturb this observed sequential capping polarity, indicating that microtubules did not direct this second capping event.

scholarly journals Leukocytes with chromosome Y loss have reduced abundance of the cell surface immunoprotein CD99

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jonas Mattisson ◽  
Marcus Danielsson ◽  
Maria Hammond ◽  
Hanna Davies ◽  
Caroline J. Gallant ◽  
...  
Keyword(s):  
Cell Surface ◽  
Single Cells ◽  
Surface Protein ◽  
Protein Abundance ◽  
Blood Leukocytes ◽  
Chromosome Y ◽  
Increased Risk ◽  
A Cell ◽  
Pseudoautosomal Regions ◽  
Male Specific

AbstractMosaic loss of chromosome Y (LOY) in immune cells is a male-specific mutation associated with increased risk for morbidity and mortality. The CD99 gene, positioned in the pseudoautosomal regions of chromosomes X and Y, encodes a cell surface protein essential for several key properties of leukocytes and immune system functions. Here we used CITE-seq for simultaneous quantification of CD99 derived mRNA and cell surface CD99 protein abundance in relation to LOY in single cells. The abundance of CD99 molecules was lower on the surfaces of LOY cells compared with cells without this aneuploidy in all six types of leukocytes studied, while the abundance of CD proteins encoded by genes located on autosomal chromosomes were independent from LOY. These results connect LOY in single cells with immune related cellular properties at the protein level, providing mechanistic insight regarding disease vulnerability in men affected with mosaic chromosome Y loss in blood leukocytes.

Fe(iii)-complex mediated bacterial cell surface immobilization of eGFP and enzymes

2021 ◽  
Author(s):  
Lilin Feng ◽  
Liang Gao ◽  
Daniel F. Sauer ◽  
Yu Ji ◽  
Haiyang Cui ◽  
...  
Keyword(s):  
Cell Surface ◽  
Bacterial Cell ◽  
Surface Immobilization ◽  
E Coli ◽  
Bacterial Cell Surface ◽  
Reversible Method

A facile and reversible method to immobilize His6-tagged proteins on the E. coli cell surface through the formation of an Fe(iii)-complex.

Sign in / Sign up

Export Citation Format

Share Document