Purification and characterization of the glycoprotein hormone .alpha.-subunit-like material secreted by HeLa cells

Biochemistry ◽  
1988 ◽  
Vol 27 (17) ◽  
pp. 6474-6487 ◽  
Author(s):  
G. Stanley Cox ◽  
Ronald A. Rimerman
Keyword(s):  
Hela Cells ◽  
Alpha Subunit ◽  
Purification And Characterization ◽  
Glycoprotein Hormone

Partial purification and characterization of mitotic factors from HeLa cells

1985 ◽  
Vol 160 (2) ◽  
pp. 471-482 ◽  
Author(s):  
Ramesh C. Adlakha ◽  
David A Wright ◽  
Chintaman G. Sahasrabuddhe ◽  
Frances M. Davis ◽  
Nagindra Prashad ◽  
...  
Keyword(s):  
Hela Cells ◽  
Partial Purification ◽  
Purification And Characterization

Purification and characterization of primer recognition proteins from HeLa cells

Biochemistry ◽  
1990 ◽  
Vol 29 (20) ◽  
pp. 4767-4773 ◽  
Author(s):  
Hitesh K. Jindal ◽  
Jamboor K. Vishwanatha
Keyword(s):  
Hela Cells ◽  
Purification And Characterization

scholarly journals The characterization of alpha-subunit of glycoprotein hormone produced by undifferentiated carcinoma.

1982 ◽  
Vol 29 (1) ◽  
pp. 11-19
Author(s):  
RYUICHIRO NISHIMURA ◽  
TAMOTSU HAMAMOTO ◽  
NORIHIKO MORIMOTO ◽  
MITSURU OZAWA ◽  
YOSHIHIKO ASHITAKA ◽  
...  
Keyword(s):  
Undifferentiated Carcinoma ◽  
Alpha Subunit ◽  
Glycoprotein Hormone

scholarly journals Dual effects of 2-deoxyglucose on synthesis of the glycoprotein hormone common alpha-subunit in butyrate-treated HeLa cells.

1987 ◽  
Vol 7 (5) ◽  
pp. 1592-1601 ◽  
Author(s):  
G S Cox ◽  
D S McClure ◽  
D E Cosgrove
Keyword(s):  
Hela Cells ◽  
Chromatin Modification ◽  
Gel Filtration ◽  
Fold Increase ◽  
Alpha Subunit ◽  
Mrna Levels ◽  
Glycoprotein Hormone ◽  
Subunit Mrna ◽  
Histone Hyperacetylation ◽  
Induction Process

Sodium butyrate (Btr) (3 mM) causes a 10-fold increase in production of the glycoprotein hormone alpha-subunit in HeLa cells. The following report demonstrates that this response could be inhibited about 95% by 5 mM 2-deoxy-D-glucose (dGlc), whereas alpha-subunit production in uninduced cells was affected little or not at all. Addition of D-mannose restored the Btr induction of Hela-alpha in cultures that had been treated with dGlc. When the alpha-subunits secreted by cells cultured in Btr plus dGlc or in Btr alone were compared by gel filtration (Sephadex G-75) and lectin affinity (concanavalin A and ricin) chromatography, differences were noted that probably reflect changes in their carbohydrate moieties. Immunoprecipitation of [35S]methionine-labeled HeLa-alpha and incubation with endoglycosidase H indicated that the subunit secreted from cells in the presence of dGlc contained oligosaccharide side chains that were not processed to the complex type. Cells that were simultaneously treated with Btr plus dGlc showed no increase in alpha-subunit production over cells receiving Btr only; in contrast, cells that were preincubated with Btr for either 16 or 36 h before dGlc was added exhibited high levels of subunit synthesis. Measurement of alpha-mRNA levels at various times after Btr and dGlc were added to cultures indicated that Btr brought about a dramatic increase in alpha-specific mRNA about 24 h after being added to cultures. This increase could be prevented by dGlc when added simultaneously with Btr but not when added after a 24-h preincubation. Although dGlc prevented the induction of alpha-subunit and alpha-mRNA in response to Btr, it had no effect on histone hyperacetylation, suggesting that if this chromatin modification is necessary for the induction process, it is not in itself sufficient. Together, the data demonstrate that dGlc inhibits the accumulation of alpha-subunit mRNA normally produced in response to Btr and that the subunit produced contains altered oligosaccharide constituents.

Characterization of Glycoprotein Hormone Free α-Subunit from Human Pituitary and Placenta Extracts

1986 ◽  
Vol 23 (1) ◽  
pp. 38-49 ◽  
Author(s):  
Roulwhai Chen ◽  
Eytan Barnea ◽  
Robert Benveniste
Keyword(s):  
Alpha Subunit ◽  
Glycoprotein Hormone ◽  
Human Pituitary

scholarly journals Purification and Characterization of Native Conventional Kinesin, HSET, and CENP-E from Mitotic HeLa Cells

2001 ◽  
Vol 276 (30) ◽  
pp. 28014-28021 ◽  
Author(s):  
Jennifer G. DeLuca ◽  
Cori N. Newton ◽  
Richard H. Himes ◽  
Mary Ann Jordan ◽  
Leslie Wilson
Keyword(s):  
Hela Cells ◽  
Purification And Characterization ◽  
Conventional Kinesin
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