Inhibition of urokinase-type plasminogen activator (uPA) abrogates myogenesis in vitro

Thrombosis and Haemostasis

Volumn 77, Issue 3, 1997, Pages 526-534

  Muñoz Cánoves, Pura ^a   Miralles, Francesc ^a,b   Baiget, Montserrat ^b   Félez, Jordi ^a  

^a Institut de Recerca Oncologica   (Spain)

^b HOSPITAL DE LA SANTA CREU I SANT PAU   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTIN; GENE PRODUCT; MESSENGER RNA; MYOGENIC FACTOR; MYOSIN; PLASMINOGEN ACTIVATOR; PROTEINASE; UROKINASE;

ANIMAL CELL; ARTICLE; CELL ADHESION; CELL DIFFERENTIATION; CELL FUSION; CELL INVASION; CELL MEMBRANE; CELL MIGRATION; CELL TRANSFORMATION; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVITY; ENZYME INHIBITION; FIBRINOLYSIS; FIBROBLAST; MOUSE; MUSCLE DEVELOPMENT; MYOBLAST; MYOTUBE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STEM CELL; TRANSCRIPTION REGULATION;

EID: 0030999185     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1656001     Document Type: Article

References (56)

1. Collen D, Lijnen HR. Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 1991; 78: 3114-24.
2. Lijnen HR, Collen D. Regulation and control of the fibrinolytic system. In: Serine proteases and their serpin inhibitors in the nervous system, Festoff BW, ed. Plenum Press, New York, 1990; pp 9-20.
3. Mignatti P, Robbins E, Rifkin DB. Tumor invasion through the human amniotic membrane: Requirement for a proteinase cascade. Cell 1986; 47: 487-98.
4. Anderson JM, Swenarchuk LE, Champaneria S. Localized extracellular proteolysis may convey inductive signals between nerve and muscle cells during synaptogenesis. In: Serine proteases and their inhibitors in the nervous system, Festoff BW, ed. Plenum Press, New York, 1990; pp 255-73.
5. Tienari J, Alanko T, Lehtonen E, Saksela O. The expression and localization of urokinase-type plasminogen activator and its type 1 inhibitor are regulated by retionic acid and fibroblast growth factor in human teratocarcinoma cells. Cell Regul 1991; 2: 285-97.
6. Muñoz-Cánoves P, Félez J. Role of plasminogen activators in muscle regeneration. Biol Clin Hematol 1993; 15: 163-71.
7. Saksela O, Rifkin DB. Cell-associated plasminogen activation: Regulation and physiological functions. Ann Rev Cell Biol 1988; 4: 93-126.
8. Carmeliet P, Collen D. Evaluation of the plasminogen/plasmin system in transgenic mice. Fibrinolysis 1994; 8, Suppl. 1: 269-76.
9. Carmeliet P, Schoonjans L, Kieckens L, Ream B, Degen J, Bronson R, De Vos R, Van den Oord JJ, Collen D, Mulligan RC. Physiological consequences of loss of plasminogen activator gene function in mice. Nature 1994; 368: 419-24.
10. Carmeliet P, Bouché A, De Clercq C, Pollefeyt S, Wijns S, Mulligan RC, Collen D. Biological effects of disruption of the tissue-type plasminogen activator, urokinase type plasminogen activator and plasminogen activator inhibitor-1 genes in mice. Ann NY Acad Sci 1995; 7480: 367.
11. Blau HM, Pavlath GK, Hardeman EC, Chiu Ch-P, Silberstein L, Webster SG, Miller SC, Webster C. Plasticity of the differentiated state. Science 1985; 230: 758-66.
12. Mohun T. Muscle differentation. Curr Opin Cell Biol 1992; 4: 923-8.
13. Olson EN. Interplay between proliferation and differentiation within the myogenic lineage. Dev Biol 1992; 154: 261-72.
14. Sorrentino V, Pepperkok R, Davis RL, Ansorge W, Philipson L. Cell proliferation inhibited by MyoD1 independently of myogenic differentiation. Nature 1990; 345: 813-5.
15. Trouche D, Grigoriev M, Lenormand J-L, Robin P, Leibovitch SA, Sassone-Corsi P, Harel-Bellan A. Repression of c-fos promoter by MyoD on muscle cell differentiation. Nature 1993; 363: 79-82.
16. Fulton AB, Prives J, Farmer SR, Penman S. Developmental reorganization of the skeletal framework and its surface lamina in fusing muscle cells. J Cell Biol 1981; 91: 103-12.
17. Weintraub H, Davis RL, Tapscott S, Thayer M, Krause M, Benezra R, Blackwell TK, Turner D, Rupp R, Hollenberg S, Zhuang Y, Lassar AB. The MyoD gene family: Nodal point during specification of the muscle cell lineage. Science 1991; 251: 761-6.
18. Boukamp P, Fusenig NE. Trans-differentiation from epidermal to mesenchymal/myogenic phenotype is associated with a drastic change in cell-cell and cell-matrix adhesion molecules. J Cell Biol 1993; 120: 981-93.
19. Weintraub H, Tapscott SJ, Davis RL, Thayer MJ, Adam MA, Lassar AB, Miller AD. Activation of muscle-specific genes in pigment, nerve, fat, liver, and fibroblast cell lines by forced expression of MyoD. Proc Natl Acad Sci USA 1989; 86: 5434-8.
20. Davis RL, Weintraub H, Lassar AB. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell 1987; 51: 987-1000.
21. Bengal E, Ransone L, Scharfmann R, Dwarki VJ, Tapscott SJ, Weintraub H, Verma IM. Functional antagonism between c-jun and MyoD proteins: A direct physical association. Cell 1992; 68: 507-19.
22. Li L, Chambard JC, Karin M, Olson EN. Fos and Jun repress transcriptonal activation by myogenin and MyoD: The amino terminus of Jun can mediate repression. Genes Dev 1992; 6: 676-89.
23. Shimizu M, Webster C, Morgan DO, Blau HM, Roth RA. Insulin and insulinlike growth factor receptors and responses in cultured human muscle cells. Am J Physiol 1986; 251: E611-5.
24. Hantai D, Soria C, Soria J, Blondet B, Barlovatz-Meimom G, Rao JS, Festoff BW. Plasminogen activators in development, injury and pathology of the neuromuscular system. In: Serine proteases and their inhibitors in the nervous system, Festoff BW, ed. Plenun Press, New York, 1991; pp 219-29.
25. Miskin R, Easton TG, Reich E. Plasminogen activator in chick embryo muscle cells: Induction of enzyme by RSV, PMA and retinoic acid. Cell 1978; 15: 1301-12.
26. Quax PHA, Frisdal E, Pedersen N, Bonavaud S, Thiberst PH, Martelly I, Verheijen JH, Blasi F, Barlovatz-Meimon G. Modulation of activities and RNA level of the components of the plasminogen activation system during fusion of human myogenic satellite cells in vitro. Dev Biol 1992; 151: 166-75.
27. Belin D, Vassalli J-D, Combepine Ch, Godeau F, Nagamine Y, Reich E, Kocher HP, Duvoisin RM. Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator. Eur J Biochem 1985; 148: 225-32.
28. Hu MC-T, Sharp SB, Davidson D. The complete sequence of the mouse skeletal alpha-actin genes reveals several conserved and inverted repeat sequences outside of the protein coding region. Mol Cell Biol 1986; 6: 15-25.
29. Sabath DE, Broome HE, Prystowsky MB. Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major interleukin 2-induced trascript in a cloned T-helper lymphocyte. Gene 1990; 91: 185-91.
30. Ben-Ze'ev A. Cell and muscle motility, Shay JW, ed. Plenum Press, New York, 1985; pp 23-53.
31. Longstaff C, Clough AM, Gaffney PJ. Kinetics of plasmin activation of single chain urinary-type plasminogen activator (scu-PA) and demonstration of a high affinity interaction between scu-PA and plasminogen. J Biol Chem 1992; 267: 173-9.
32. Longstaff C. In vivo significance of kinetic constants of tight binding reversible proteinase inhibitors. Thromb Haemost 1992; 67: 533-6.
33. Yaffe D, Saxel O. Serial passaging and differentation of myogenic cells isolated from dystrophic mouse muscle. Nature 1977; 270: 725-7.
34. Blau HM, Chiu Ch-P, Webster C. Cytoplasmic activation of human nuclear genes in stable heterocaryons. Cell 1983; 32: 1171-80.
35. Devlin RB, Emerson CP. Coordinate regulation of contractile protein synthesis during myoblast differentiation. Cell 1978; 13: 599-611.
36. Ragot T, Vincent N, Chafey P, Vigne E, Gilgenkrantz H, Couton D, Cartaud J, Briand P, Kaplan J-C, Perricaudet M, Kahn A. Efficient adenovirus-mediated transfer of a human minidystrophin gene to skeletal muscle of mdx mice. Nature 1993; 361: 647-50.
37. Nadal-Ginard B, Nguyen HT, Madhavi V. Induction of muscle specific genes in the absence of commitment is reversible. Exp Biol Med 1984; 9: 250-9.
38. Shani M, Zevin-Sonkin D, Saxel D, Carmon Y, Catcoff D, Nudel U, Yaffe D. The correlation between the synthesis of skeletal muscle actin, myosin heavy chain, and myosin light chain and the accumulation of corresponding mRNA sequences during myogenesis. Dev Biol 1981; 111: 324-34.
39. Nadal-Ginard B. Commitment, fusion and biochemical differentation on a myogenic cell line in the absence of DNA synthesis. Cell 1978; 15: 855-64.
40. Endo T, Nadal-Ginard B. Three types of muscle-specific gene expression in fusion-blocked rat skeletal muscle cells: Translational control in EGTA-treated cells. Cell 1987; 49: 515-26.
41. Miranda AF, Nette EG, Khan S, Brockbank K, Schonberg M. Alteration of myoblast phenotype by dimethylsulfoxide. Proc Natl Acad Sci USA 1978; 83: 8511-5.
42. Blau HM, Epstein ChJ. Manipulation of myogenesis in vitro: Reversible inhibition by DMSO. Cell 1979; 17: 95-108.
43. Strauch AR, Offord JD, Chalkley R, Rubinstein PA. Characterization of actin mRNA levels in BC3H1 cell differentiation. J Biol Chem 1986; 261: 849-55.
44. Strauch A, Rubinstein PA. Induction of vascular smooth muscle alpha-isoactin expression in BC3H1 cells. J Biol Chem 1984; 259: 3152-9.
45. Reznikoff CA, Brankow DW, Heidelberger C. Establishment and characterization of a cloned line of C3H mouse embryo cells sensitive to postconfluence inhibition of division. Cancer Res 1977; 33: 3231-8.
46. Taylor SM, Jones PA. Multiple new phenotypes induced in 10T1/2 and 3T3 cells treated with 5-azacytidine. Cell 1979; 17: 771-9.
47. Choi J, Costa ML, Mermelstein CS, Chagas C, Holtzer S, Holtzer H. MyoD converts primary dermal fibroblast, chondroblast, smooth muscle, and retinal pigmented epithelial cells into striated mononucleated myoblasts and multinucleated myotubes. Proc Natl Acad Sci USA 1990; 87: 7988-92.
48. Barlovatz-Meimon G, Frisdal E, Bassaglia Y, Hantai D, Angles-Cano E, Gautron J. Relationship between plasminogen activators and regeneration capacities of rat skeletal muscles. In: Serine proteases and their serpin inhibitors in the nervous system, Festoff BW, ed. Plenum Press, New York, 1990; pp 229-41.
49. Couch CB, Strittmatter WJ. Rat myoblast fusion requires metalloendoprotease activity. Cell 1983; 32: 257-65.
50. Yagami-Hiromasa T, Sato T, Kurisaki T, Kamijo K, Nabeshima Y-I, Fujisawa-Sehara A. A metalloprotease-disintegrin participating in myoblast fusion. Nature 1995; 377: 652-6.
51. Gogos JA, Thompson R, Lowry W, Sloane BF, Weintraub H, Horwitz M. Gene trapping in differentiating cells lines: Regulation of the lysosomal protease cathepsin B in skeletal myoblast growth and fusion. J Cell Biol 1996; 134: 837-47.
52. Guerin CW, Holland PC. Synthesis and secretion of matrix-degrading metalloproteases by human skeletal muscle satellite cells. Dev Dynam 1995; 202: 91-9.
53. Schafer BW, Blakely BT, Darlington GJ, Blau HM. Effect of cell history on response to helix-loop-helix family of myogenic regulators. Nature 1990; 344: 454-8.
54. Lassar A, Munsterberg A. Wiring diagrams: Regulatory circuits and the control of skeletal myogenesis. Curr Opin Cell Biol 1994; 6: 432-42.
55. Lassar AB, Skapek SX, Novitch B. Regulatory mechanisms that coordinate skeletal muscle differentiation and cell cycle withdrawal. Curr Opin Cell Biol 1994; 6: 788-94.
56. Brunner G, Schirrmacher V. Fibrin autography of plasminogen activator by electrophoretic transfer into fibrin agar gels. Anal Biochem 1988; 168: 411-6.