Document Detail

Alterations in cyclic AMP phosphodiesterase activities during differentiation of 3T3-L1 cells.
MedLine Citation:
PMID:  6196386     Owner:  NLM     Status:  MEDLINE    
3T3-L1 cells contain multiple forms of cyclic nucleotide phosphodiesterase in both supernatant (100,000 X g, 40 min) and particulate fractions. Supernatant fractions from both undifferentiated and differentiated cells contained calmodulin-sensitive activity. In undifferentiated 3T3-L1 cells, only a small fraction of the total cAMP phosphodiesterase activity was found in the particulate fraction and the specific activity of the particulate was lower than the supernatant. With differentiation the specific activity of the particulate doubled, and there was a dramatic increase in total activity in this fraction, while in the supernatant total cAMP phosphodiesterase activity increased less and specific activity decreased. The particulate fraction accounted for approximately 70% of the total cAMP phosphodiesterase activity in differentiated cells in contrast to about one-third in undifferentiated cells. In addition, there was a qualitative change in particulate phosphodiesterase activity. In fractions from 3T3-L1 adipocytes, with either cAMP or cGMP as substrate, Lineweaver-Burk plots were nonlinear, with low Km components of less than 1 microM, and cGMP inhibited cAMP hydrolysis. In particulate fractions from undifferentiated cells, cGMP did not inhibit and often enhanced hydrolysis of cAMP. With differentiation, there was also a marked increase in particulate cGMP phosphodiesterase activity. cAMP and cGMP phosphodiesterase activities solubilized from particulate fraction of differentiated cells coeluted from DEAE-Biogel and exhibited kinetic properties similar to the crude particulate fractions. During differentiation, there seems to be an alteration in the distribution of phosphodiesterase activity as well as the appearance of a particulate phosphodiesterase with kinetic properties similar to a particulate phosphodiesterase found in mature rat adipocytes.
V C Manganiello; B C Reed; F S Lieberman; J Moss; M D Lane; M Vaughan
Related Documents :
18337116 - Control of lipolysis by natriuretic peptides and cyclic gmp.
6276376 - Phosphorylation by guanosine 3':5'-monophosphate-dependent protein kinase of synthetic ...
14660486 - Role of cgmp-dependent protein kinase in development of tolerance to nitric oxide in pu...
9247116 - Cgmp as second messenger during dictyostelium chemotaxis.
9020176 - Phosphorylation-dependent monoclonal tau antibodies do not reliably report phosphorylat...
17319846 - A high-throughput screen of cell-death-inducing factors in nicotiana benthamiana identi...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of cyclic nucleotide and protein phosphorylation research     Volume:  9     ISSN:  0746-3898     ISO Abbreviation:  J Cyclic Nucleotide Protein Phosphor Res     Publication Date:  1983  
Date Detail:
Created Date:  1984-01-07     Completed Date:  1984-01-07     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8309334     Medline TA:  J Cyclic Nucleotide Protein Phosphor Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  143-54     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
1-Methyl-3-isobutylxanthine / pharmacology
3',5'-Cyclic-AMP Phosphodiesterases / metabolism*
3',5'-Cyclic-GMP Phosphodiesterases / metabolism
Adipose Tissue / cytology,  enzymology*
Calmodulin / pharmacology
Cell Differentiation
Cells, Cultured
Clone Cells / enzymology
Dexamethasone / pharmacology
Insulin / pharmacology
Reg. No./Substance:
0/Calmodulin; 11061-68-0/Insulin; 28822-58-4/1-Methyl-3-isobutylxanthine; 50-02-2/Dexamethasone; EC',5'-Cyclic-AMP Phosphodiesterases; EC',5'-Cyclic-GMP Phosphodiesterases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Effect of adenosine on synthesis and release of cyclic AMP by cultured vascular cells from swine.
Next Document:  Acid sensitivity of glycolysis in normal and proton-permeable cells of Streptococcus mutans GS-5.