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. 1990 Sep 1;270(2):391–395. doi: 10.1042/bj2700391

Treatment of cardiac myocytes with 8-(4-chlorophenylthio)-adenosine 3',5'-cyclic monophosphate, forskolin or cholera toxin does not stimulate cellular or heparin-releasable lipoprotein lipase activities.

R Carroll 1, A Juhasz 1, D L Severson 1
PMCID: PMC1131734  PMID: 2169239

Abstract

Incubation of isolated cardiac myocytes with 500 microM-8-(4-chlorophenylthio)adenosine 3',5'-cyclic monophosphate (CPT-cAMP) or 100 microM-forskolin for 2 1/2 h did not increase the heparin-induced release of lipoprotein lipase (LPL) into the medium. When LPL activity in cardiac myocytes was depleted by treatment of rats with cycloheximide (2 mg/kg; 2.5 h) and inclusion of the protein-synthesis inhibitor in the isolation solutions, incubation with CPT-cAMP or forskolin did not influence the rate of repletion of LPL activity in cells or the recovery of heparin-releasable LPL activity. Although the administration of cholera toxin (0.5 mg/kg; 16-17 h) to rats increased LPL activity in a low-speed supernatant fraction from heparin-perfused hearts, LPL activity was not increased in cardiac myocytes from cholera-toxin-treated rat hearts, and the heparin-induced release of LPL was unchanged. Incubation of cultured ventricular myocytes with 1 microgram of cholera toxin/ml or 500 microM-CPT-cAMP for 24 h did not increase cellular LPL activity or LPL released into the culture medium after a 40 min incubation with heparin. Therefore interventions that stimulate adenylate cyclase activity (forskolin, cholera toxin) or incubation with CPT-cAMP do not increase cellular LPL activity or promote the translocation of LPL to a heparin-releasable fraction in cardiac myocytes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bagby G. J., Corll C. B. Comparison of lipoprotein lipase activity in heart myocytes and perfused hearts. J Mol Cell Cardiol. 1989 Mar;21(3):253–262. doi: 10.1016/0022-2828(89)90740-2. [DOI] [PubMed] [Google Scholar]
  2. Björntorp P., Hansson G. K., Jonasson L., Pettersson P., Sypniewska G. Isolation and characterization of endothelial cells from the epididymal fat pad of the rat. J Lipid Res. 1983 Feb;24(2):105–112. [PubMed] [Google Scholar]
  3. Blanchette-Mackie E. J., Masuno H., Dwyer N. K., Olivecrona T., Scow R. O. Lipoprotein lipase in myocytes and capillary endothelium of heart: immunocytochemical study. Am J Physiol. 1989 Jun;256(6 Pt 1):E818–E828. doi: 10.1152/ajpendo.1989.256.6.E818. [DOI] [PubMed] [Google Scholar]
  4. Borensztajn J., Otway S., Robinson D. S. Effect of fasting on the clearing factor lipase (lipoprotein lipase) activity of fresh and defatted preparations of rat heart muscle. J Lipid Res. 1970 Mar;11(2):102–110. [PubMed] [Google Scholar]
  5. Chohan P., Cryer A. The lipoprotein lipase (clearing-factor lipase) activity of cells isolated from rat cardiac muscle. Biochem J. 1978 Aug 15;174(2):663–666. doi: 10.1042/bj1740663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cryer A., Chohan P., Smith J. J. Effectors of lipoprotein lipase secretion from isolated cardiac muscle cells incubated in vitro. Life Sci. 1981 Aug 31;29(9):923–929. doi: 10.1016/0024-3205(81)90394-5. [DOI] [PubMed] [Google Scholar]
  7. Friedman G., Chajek-Shaul T., Stein O., Noe L., Etienne J., Stein Y. Beta-adrenergic stimulation enhances translocation, processing and synthesis of lipoprotein lipase in rat heart cells. Biochim Biophys Acta. 1986 Jun 11;877(1):112–120. doi: 10.1016/0005-2760(86)90125-6. [DOI] [PubMed] [Google Scholar]
  8. Friedman G., Chajek-Shaul T., Stein O., Stein Y. Modulation of lipoprotein lipase activity in cultured rat mesenchymal heart cells and preadipocytes by dibutyryl cyclic AMP, cholera toxin and 3-isobutyl-1-methylxanthine. Biochim Biophys Acta. 1983 Jun 16;752(1):106–117. doi: 10.1016/0005-2760(83)90238-2. [DOI] [PubMed] [Google Scholar]
  9. Hamosh M., Hamosh P. Lipoprotein lipase: its physiological and clinical significance. Mol Aspects Med. 1983;6(3):199–289. doi: 10.1016/0098-2997(83)90006-7. [DOI] [PubMed] [Google Scholar]
  10. Hülsmann W. C., Dubelaar M. L. Lipoprotein lipases and stress hormones: studies with glucocorticoids and cholera toxin. Biochim Biophys Acta. 1986 Jan 3;875(1):69–75. doi: 10.1016/0005-2760(86)90012-3. [DOI] [PubMed] [Google Scholar]
  11. Jansen H., Stam H., Kalkman C., Hülsmann W. C. On the dual localization of lipoprotein lipase in rat heart. Studies with a modified perfusion technique. Biochem Biophys Res Commun. 1980 Jan 29;92(2):411–416. doi: 10.1016/0006-291x(80)90348-4. [DOI] [PubMed] [Google Scholar]
  12. Knobler H., Chajek-Shaul T., Stein O., Etienne J., Stein Y. Modulation of lipoprotein lipase in the intact rat by cholera toxin--an irreversible agonist of cyclic AMP. Biochim Biophys Acta. 1984 Sep 12;795(2):363–371. doi: 10.1016/0005-2760(84)90087-0. [DOI] [PubMed] [Google Scholar]
  13. Kousvelari E. E., Grant S. R., Baum B. J. beta-Adrenergic receptor regulation of N-linked protein glycosylation in rat parotid acinar cells. Proc Natl Acad Sci U S A. 1983 Dec;80(23):7146–7150. doi: 10.1073/pnas.80.23.7146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kryski A., Jr, Kenno K. A., Severson D. L. Stimulation of lipolysis in rat heart myocytes by isoproterenol. Am J Physiol. 1985 Feb;248(2 Pt 2):H208–H216. doi: 10.1152/ajpheart.1985.248.2.H208. [DOI] [PubMed] [Google Scholar]
  15. Kuiper J., Zijlstra F. J., Kamps J. A., Van Berkel T. J. Cellular communication inside the liver. Binding, conversion and metabolic effect of prostaglandin D2 on parenchymal liver cells. Biochem J. 1989 Aug 15;262(1):195–201. doi: 10.1042/bj2620195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Miller W. C., Palmer W. K., Arnall D. A., Oscai L. B. Effect of cholera toxin on triacylglycerol lipase activity and triacylglycerol content of rat heart. Can J Physiol Pharmacol. 1987 Jan;65(1):60–63. doi: 10.1139/y87-011. [DOI] [PubMed] [Google Scholar]
  17. Piper H. M., Jacobson S. L., Schwartz P. Determinants of cardiomyocyte development in long-term primary culture. J Mol Cell Cardiol. 1988 Sep;20(9):825–835. doi: 10.1016/s0022-2828(88)80007-5. [DOI] [PubMed] [Google Scholar]
  18. Ramírez I., Kryski A. J., Ben-Zeev O., Schotz M. C., Severson D. L. Characterization of triacylglycerol hydrolase activities in isolated myocardial cells from rat heart. Biochem J. 1985 Nov 15;232(1):229–236. doi: 10.1042/bj2320229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Roesler W. J., Vandenbark G. R., Hanson R. W. Cyclic AMP and the induction of eukaryotic gene transcription. J Biol Chem. 1988 Jul 5;263(19):9063–9066. [PubMed] [Google Scholar]
  20. Severson D. L., Carroll R. Effect of taxol on the heparin-induced secretion of lipoprotein lipase from cardiac myocytes. 1989 Jun 27-Jul 24Mol Cell Biochem. 88(1-2):17–22. doi: 10.1007/BF00223418. [DOI] [PubMed] [Google Scholar]
  21. Severson D. L., Carroll R., Kryski A., Jr, Ramírez I. Short-term incubation of cardiac myocytes with isoprenaline has no effect on heparin-releasable or cellular lipoprotein lipase activity. Biochem J. 1987 Nov 15;248(1):289–292. doi: 10.1042/bj2480289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Severson D. L., Lee M., Carroll R. Secretion of lipoprotein lipase from myocardial cells isolated from adult rat hearts. Mol Cell Biochem. 1988 Jan;79(1):17–24. doi: 10.1007/BF00229393. [DOI] [PubMed] [Google Scholar]
  23. Simpson J. Rapid effects of isoprenaline, glucagon, pacing and potassium arrest on post-heparin lipoprotein lipase activity in the perfused rat heart. Biochem J. 1979 Jul 15;182(1):253–255. doi: 10.1042/bj1820253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Spector T. Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for less than or equal to 0.5 to 50 microgram of protein. Anal Biochem. 1978 May;86(1):142–146. doi: 10.1016/0003-2697(78)90327-5. [DOI] [PubMed] [Google Scholar]
  25. Stam H., Broekhoven-Schokker S., Hülsmann W. C. Studies on the involvement of lipolytic enzymes in endogenous lipolysis of the isolated rat heart. Biochim Biophys Acta. 1986 Jan 3;875(1):87–96. doi: 10.1016/0005-2760(86)90014-7. [DOI] [PubMed] [Google Scholar]
  26. Stam H., Hülsmann W. C. Effects of hormones, amino acids and specific inhibitors on rat heart heparin-releasable lipoprotein lipase and tissue neutral lipase activities during long-term perfusion. Biochim Biophys Acta. 1984 Jun 6;794(1):72–82. doi: 10.1016/0005-2760(84)90299-6. [DOI] [PubMed] [Google Scholar]
  27. Xenophontos X. P., Watson P. A., Chua B. H., Haneda T., Morgan H. E. Increased cyclic AMP content accelerates protein synthesis in rat heart. Circ Res. 1989 Sep;65(3):647–656. doi: 10.1161/01.res.65.3.647. [DOI] [PubMed] [Google Scholar]

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