JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kuri-Harcuch, W.
Right arrow Articles by Green, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kuri-Harcuch, W.
Right arrow Articles by Green, H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

JBC, Vol. 252, Issue 6, 2158-2160, Mar, 1977

Increasing activity of enzymes on pathway of triacylglycerol synthesis during adipose conversion of 3T3 cells

W. Kuri-Harcuch and H. Green

When preadipose 3T3 cells pass from growing to resting state, they increase their rate of synthesis of triacylglycerol from precursors and convert to adipose cells. The behavior of two enzymes involved in the synthesis of triacylglycerol, glycerophosphate acyltransferase, and malic enzyme have been examined during the adipose conversion of 3T3-F442A in surface culture and in suspension culture stabilized with methylcellulose. Glycerophosphate acyltransferase activity rises sharply during the conversion and reaches a level of 80 times higher than that of another 3T3 subline in which practically no adipose conversion takes place (3T3-C2). The activity of malic enzyme also rises during the adipose conversion of 3T3-F442A and reaches a level of 15-fold higher than that of 3T3-C2. The activity of glycerophosphate acyltransferase responds more sharply than that of malic enzyme but the rise in activity is not sustained as long, so that the relative levels of the two enzymes change during the conversion. The adipose conversion appears to be the result of increases in the activity of the synthesizing enzymes, brought about by either of the two most physiological methods available for arresting the growth of cultured cells.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol. Pharmacol.Home page
M. Gary-Bobo, G. Elachouri, B. Scatton, G. Le Fur, F. Oury-Donat, and M. Bensaid
The Cannabinoid CB1 Receptor Antagonist Rimonabant (SR141716) Inhibits Cell Proliferation and Increases Markers of Adipocyte Maturation in Cultured Mouse 3T3 F442A Preadipocytes
Mol. Pharmacol., February 1, 2006; 69(2): 471 - 478.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
E. R. Hugo, T. D. Brandebourg, C. E. S. Comstock, K. S. Gersin, J. J. Sussman, and N. Ben-Jonathan
LS14: A Novel Human Adipocyte Cell Line that Produces Prolactin
Endocrinology, January 1, 2006; 147(1): 306 - 313.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
M. Bensaid, M. Gary-Bobo, A. Esclangon, J. P. Maffrand, G. Le Fur, F. Oury-Donat, and P. Soubrie
The Cannabinoid CB1 Receptor Antagonist SR141716 Increases Acrp30 mRNA Expression in Adipose Tissue of Obese fa/fa Rats and in Cultured Adipocyte Cells
Mol. Pharmacol., April 1, 2003; 63(4): 908 - 914.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. G. Parton, J. C. Molero, M. Floetenmeyer, K. M. Green, and D. E. James
Characterization of a Distinct Plasma Membrane Macrodomain in Differentiated Adipocytes
J. Biol. Chem., November 22, 2002; 277(48): 46769 - 46778.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Endocrinol. Metab.Home page
I. J. Bujalska, E. A. Walker, M. Hewison, and P. M. Stewart
A Switch in Dehydrogenase to Reductase Activity of 11{beta}-Hydroxysteroid Dehydrogenase Type 1 upon Differentiation of Human Omental Adipose Stromal Cells
J. Clin. Endocrinol. Metab., March 1, 2002; 87(3): 1205 - 1210.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. K. Hajra, L. K. Larkins, A. K. Das, N. Hemati, R. L. Erickson, and O. A. MacDougald
Induction of the Peroxisomal Glycerolipid-synthesizing Enzymes during Differentiation of 3T3-L1 Adipocytes. ROLE IN TRIACYLGLYCEROL SYNTHESIS
J. Biol. Chem., March 24, 2000; 275(13): 9441 - 9446.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
E Juarez-Aguilar, F Castro-Munozledo, N. Guerra-Rodriguez, D Resendez-Perez, H. Martinez-Rodriguez, H. Barrera-Saldana, and W Kuri-Harcuch
Functional domains of human growth hormone necessary for the adipogenic activity of hGH/hPL chimeric molecules
J. Cell Sci., January 9, 1999; 112(18): 3127 - 3135.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
J. Lieber and R. Evans
Disruption of the vimentin intermediate filament system during adipose conversion of 3T3-L1 cells inhibits lipid droplet accumulation
J. Cell Sci., January 12, 1996; 109(13): 3047 - 3058.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
L. Salazar-Olivo, F Castro-Munozledo, and W Kuri-Harcuch
A preadipose 3T3 cell variant highly sensitive to adipogenic factors and to human growth hormone
J. Cell Sci., January 5, 1995; 108(5): 2101 - 2107.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1977 by the American Society for Biochemistry and Molecular Biology.