Lactate down-regulates cellular poly(ADP-ribose) formation in cultured human skin fibroblasts

European Journal of Clinical Investigation

Volumn 37, Issue 2, 2007, Pages 134-139

  Wagner, S ^a   Hussain, M Z ^b   Beckert, S ^a   Ghani, Q P ^b   Weinreich, J ^a   Hunt, T K ^c   Becker, H D ^a   Konigsrainer A ^a  

^a UNIVERSITY HOSPITAL TÜBINGEN   (Germany)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Fibroblast culture; Lactate; NAD+; Poly(ADP ribose); Wound healing

Indexed keywords

3 AMINOBENZAMIDE; LACTIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; POLY(ADENOSINE DIPHOSPHATE RIBOSE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; CELL ADHESION; CELL COUNT; CELL CULTURE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SYNTHESIS; GENE EXPRESSION; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; NEWBORN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SKIN FIBROBLAST; STAINING; TISSUE REPAIR; WOUND; WOUND HEALING;

CELLS, CULTURED; DOWN-REGULATION; FIBROBLASTS; HUMANS; LACTIC ACID; POLY(ADP-RIBOSE) POLYMERASES; SKIN; WOUND HEALING;

EID: 33846072514     PISSN: 00142972     EISSN: 13652362     Source Type: Journal    
DOI: 10.1111/j.1365-2362.2007.01760.x     Document Type: Article

References (42)

1. Bürkle A. Poly (ADP-ribosylation). Georgetown: LANDES Biosciences; 2006.
2. Bürkle A. Physiology and pathophysiology of poly (ADP-ribosyl) ation. Bioessays 2001;23:795-806.
3. +. FEBS J 2005;272:4576-89.
4. Bürkle A, Schreiber V, Oliver FJ, Dantzer F, Niedergang C, de Murcia G et al. Molecular and genetic approaches: Biological significance of poly ADP-ribosylation reactions. In: de Murcia, G, Shall, S, eds. Poly (ADP-Ribosylation) Reactions: from DNA Damage and Stress Signalling to Cell Death. Oxford: Oxford University Press; 2000. pp. 80-124.
5. Lindahl T, Satoh MS, Poirier GG, Klungland A. Post-translational modification of poly (ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem Sci 1995;20:405-11.
6. D'Amours D, Desnoyers S, D'Silva I, Poirier GG. Poly (ADP-ribosyl) ation reactions in the regulation of nuclear functions. Biochem J 1999;342:249-68.
7. Oei SL, Griesenbeck J, Schweiger M, Ziegler M. Regulation of RNA polymerase II-dependent transcription by poly (ADP- ribosyl)ation of transcription factors. J Biol Chem 1998;273:31 644-7.
8. Meisterernst M, Stelzer G, Roeder R. Poly (ADP-ribose) polymerase enhances activator-dependent transcription in vitro. Proc Natl Acad Sci USA 1997;94:2261-5.
9. Wesierska-Gadek J, Bugajska-Schretter A, Cerni C. ADPribosylation of p53 tumor suppressor protein: mutant but not wild-type p53 is modified. J Cell Biochem 1996;62:90-101.
10. Wesierska-Gadek J, Schmid G, Cerni C. ADP-ribosylation of wild-type p53 in vitro: binding of p53 protein to specific p53 consensus sequence prevents its modification. Biochem Biophys Res Commun 1996;224:96-102.
11. Rawling J, Alvarez-Gonzalez R. TFIIF a basal eukaryotic transcription factor, is a substrate for poly (ADP-ribosyl) ation. Biochem J 1997;324:249-53.
12. Rankin PW, Jacobson EL, Benjamin RC, Moss J, Jacobson MK. Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo. J Biol Chem 1989;264:4312-7.
13. Oei SL, Shi Y. Transcription factor Yin Yang 1 stimulates poly (ADP-ribosyl) ation and DNA repair. Biochem Biophys Res Commun 2001;284:450-4.
14. Kraus WL, Lis JT. PARP goes transcription. Cell 2003;113:677-83.
15. Griesenbeck J, Oei SL, Mayer-Kuckuk P, Ziegler M, Buchlow G, Schweiger M. Protein-protein interaction of the human poly (ADP-ribosyl) transferase depends on the functional state of the enzyme. Biochemistry 1997;36:7297- 304.
16. Ghani QP, Hussain MZ, Zhang J, Hunt TK. Control of procollagen gene transcription and prolyl hydroxylase activitiy by poly (ADP-ribose). In: Poirier GG, Moreau P, eds. ADP-Ribosylation Reactions. New York: Springer-Verlag; 1992. pp. 211-7.
17. Gimbel M, Hunt T, Hussain M. Lactate controls collagen gene promoter activity through poly-ADP-ribosylaton. Surg Forum 2000;51:26-7.
18. Zabel DD, Feng JJ, Scheuenstuhl H, Hunt TK, Hussain MZ. Lactate stimulation of macrophage-derived angiogenic activity is associated with inhibition of poly (ADP-ribose) synthesis. Lab Invest 1996;74:644-9.
19. Caldwell MD, Shearer J, Morris A, Mastrofrancesco B, Henry W, Albina JE. Evidence for aerobic glycolysis in lambda-carrageenan-wounded skeletal muscle. J Surg Res 1984;37:63-8.
20. Comstock JP, Gribble TJ, Udenfriend S. Further study on the activation of collagen proline hydroxylase in cultures of L-929 fibroblasts. Arch Biochem Biophys 1970;137:115-21.
21. Hunt TK. Basic principles of wound healing. J Trauma 1990;30:S122-8.
22. Hunt TK, Conolly WB, Aronson SB, Goldstein P. Anaerobic metabolism and wound healing. an hypothesis for the initiation and cessation of collagen synthesis in wounds. Am J Surg 1978;135:328-32.
23. Gladden LB. Lactate metabolism: a new paradigm for the third millennium. J Physiol 2004;558:5-30.
24. Hussain M, Ghani Q, Hunt T. Inhibition of prolyl hydroxylase by poly (ADP-ribose) and posphoribosyl-AMP. J Biol Chem 1989;264:7850-5.
25. Riquet FB, Tan L, Choy BK, Osaki M, Karsenty G, Osborne TF et al. YY1 is a positive regulator of transcription of the Col1a1 gene. J Biol Chem 2001;276:38 665-72.
26. Zaniolo K, Rufiange A, Leclerc S, Desnoyers S, Guerin SL. Regulation of the poly (ADP-ribose) polymerase-1 gene expression by the transcription factors Sp1 and Sp3 is under the influence of cell density in primary cultured cells. Biochem J 2005;389:423-33.
27. Trabold O, Wagner S, Wicke C, Scheuenstuhl H, Hussain MZ, Rosen N et al. Lactate and oxygen constitute a fundamental regulatory mechanism in wound healing. Wound Repair Regen 2003;11:504-9.
28. Bürkle A, Chen G, Kupper JH, Grube K, Zeller WJ. Increased poly (ADP-ribosyl) ation in intact cells by cisplatin treatment. Carcinogenesis 1993;14:559-61.
29. Jacobson E, Jacobson M. Pyridin nucleotide levels as a function of growth in normal and transformed 3T3 cells. Arch Biochem Biophys 1976;175:627-34.
30. Faraone-Mennella M, Gambacorta A, Nicolaus B, Farina B. Purification and biochemical characterization of a poly (ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus. Biochem J 1998;335:441-7.
31. Freshney RI. Quantitation. In: Freshney RI, ed. Culture of Animal Cells: a Manual of Basic Technique, 4th edn. New York: Wiley; 2000. pp. 309-14.
32. Ali MA, Yasui F, Matsugo S, Konishi T. The lactate-dependent enhancement of hydroxyl radical generation by the Fenton reaction. Free Radic Res 2000;32:429-38.
33. + fluxes in intact cells. FASEB J 2001;15:10-2.
34. Althaus FR, Richter C. ADP-ribosylation of proteins. Enzymology and biological significance. Mol Biol Biochem Biophys 1987;37:1-237.
35. +: NADH ratio in normal and transformed fibroblasts. J Biol Chem 1974;249:4138-43.
36. Preiss J, Schlaeger R, Hilz H. Specific inhibition of poly adpribose polymerase by thymidine and nicotinamide in HeLa cells. FEBS Lett 1971;19:244-6.
37. Levene C, Bates C. The effect of hypoxia on collagen synthesis in cultured 3T6 fibroblasts and its relationship to the mode of action of ascorbate. Biochim Biophys Acta 1976;444:446-52.
38. Green H, Goldberg B. Collagen and cell protein synthesis by established mammalian fibroblast line. Nature 1964;204:347-9.
39. Constant JS, Feng JJ, Zabel DD, Yuan H, Suh DY, Scheuenstuhl H et al. Lactate elicits vascular endothelial growth factor from macrophages: a possible alternative to hypoxia. Wound Repair Regen 2000;8:353-60.
40. Collins TM, Denish A, Sheffield J, Mitra A, Stueber K, Smith YR. Nicotinamide enhances skin flap survival. Scand J Plast Reconstr Surg Hand Surg 1989;23:177-9.
41. Kull FC Jr, Brent DA, Parikh I, Cuatrecasas P. Chemical identification of a tumor-derived angiogenic factor. Science 1987;236:843-5.
42. Malanga M, Pleschke JM, Kleczkowska HE, Althaus FR. Poly (ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions. J Biol Chem 1998;273:11 839-43.