Mactinin treatment promotes wound-healing-associated inflammation in urokinase knockout mice
dc.contributor.author | Luikart, Sharon D. | en_US |
dc.contributor.author | Levay-Young, Brett | en_US |
dc.contributor.author | Hinkel, Tim | en_US |
dc.contributor.author | Shearer, Jeffry | en_US |
dc.contributor.author | Mills, Charles | en_US |
dc.contributor.author | Caldwell, Michael D. | en_US |
dc.contributor.author | Gyetko, Margaret R. | en_US |
dc.contributor.author | Oegema, Theodore R. | en_US |
dc.date.accessioned | 2010-06-01T21:29:40Z | |
dc.date.available | 2010-06-01T21:29:40Z | |
dc.date.issued | 2006-03 | en_US |
dc.identifier.citation | Luikart, Sharon D . ; Levay-Young, Brett; Hinkel, Tim; Shearer, Jeffry; Mills, Charles; Caldwell, Michael D . ; Gyetko, Margaret R . ; Oegema, Theodore R . (2006). "Mactinin treatment promotes wound-healing-associated inflammation in urokinase knockout mice." Wound Repair and Regeneration 14(2): 123-128. <http://hdl.handle.net/2027.42/74551> | en_US |
dc.identifier.issn | 1067-1927 | en_US |
dc.identifier.issn | 1524-475X | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/74551 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=16630100&dopt=citation | en_US |
dc.description.abstract | Mactinin, a 31 kDa fragment from the amino-terminal end of Α-actinin, is chemotactic for monocytes and can promote monocyte/macrophage maturation. Macrophages are essential for wound healing, in which they play key roles in debridement, angiogenesis, fibroblast proliferation, and collagen metabolism. We have previously determined that urokinase is necessary to form mactinin from extracellular Α-actinin, which may be present at sites of inflammation as a result of cell movement. Thus, urokinase knockout mice are unable to form mactinin and therefore are an ideal model to study mactinin's effects on wound healing. Saline- and mactinin-treated wounds were analyzed in a subcutaneous sponge wound model in both wild-type and urokinase knockout mice. The wounded urokinase knockout mice had markedly decreased leukocyte infiltration compared with wounded wild-type mice. In addition, production of the proinflammatory cytokine, interleukin-12, and of collagen was also decreased in knockouts. Treatment of knockout mice with mactinin resulted in leukocyte infiltration numbers, interleukin-12 levels, and hydroxyproline measurements similar to those in wild-type mice. The results suggest that impaired wound healing in urokinase-deficient mice can be restored by administration of mactinin. | en_US |
dc.format.extent | 543228 bytes | |
dc.format.extent | 3109 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Inc | en_US |
dc.rights | © 2006 by the Wound Healing Society | en_US |
dc.title | Mactinin treatment promotes wound-healing-associated inflammation in urokinase knockout mice | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Medicine (General) | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | 4. Veterans Affairs Medical Center and Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan , and | en_US |
dc.contributor.affiliationother | 1. Veterans Affairs Medical Center, Minneapolis, Minnesota | en_US |
dc.contributor.affiliationother | 2. Department of Medicine and | en_US |
dc.contributor.affiliationother | 3. Department of Surgery, University of Minnesota, Minneapolis, Minnesota | en_US |
dc.contributor.affiliationother | 5. Department of Biochemistry, Rush University, Chicago, Illinois | en_US |
dc.identifier.pmid | 16630100 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/74551/1/j.1743-6109.2006.00101.x.pdf | |
dc.identifier.doi | 10.1111/j.1743-6109.2006.00101.x | en_US |
dc.identifier.source | Wound Repair and Regeneration | en_US |
dc.identifier.citedreference | Browder W, Williams D, Lucore P, Pretus H, Jones E, McNamee R. Effect of enhanced macrophage function on early wound healing. Surgery 1988; 104: 224 – 30. | en_US |
dc.identifier.citedreference | Diegelmann RF, Cohen IK, Kaplan AM. The role of macrophages in wound repair: a review. Plast Reconstr Surg 1981; 68: 107 – 13. | en_US |
dc.identifier.citedreference | Leibovich SJ, Ross R. The role of the macrophage in wound repair. A study with hydrocortisone and antimacrophage serum. Am J Pathol 1975; 78: 71 – 100. | en_US |
dc.identifier.citedreference | Cromack DT, Porras-Reyes B, Purdy JA, Pierce GF, Mustoe TA. Acceleration of tissue repair by transforming growth factor beta 1: identification of in vivo mechanism of action with radiotherapy-induced specific healing deficits. Surgery 1993; 113: 36 – 42. | en_US |
dc.identifier.citedreference | Danon D, Kowatch MA, Roth GS. Promotion of wound repair in old mice by local injection of macrophages. Proc Natl Acad Sci USA 1989; 86: 2018 – 20. | en_US |
dc.identifier.citedreference | Schaffer CJ, Nanney LB. Cell biology of wound healing. Int Rev Cytol 1986; 169: 151 – 81. | en_US |
dc.identifier.citedreference | Andreesen R, Brugger W, Scheibenbogen C, Kreutz M, Leser H-G, Rehm A, LÖhr GW. Surface phenotype analysis of human monocyte to macrophage maturation. J Leukoc Biol 1990; 47: 490 – 7. | en_US |
dc.identifier.citedreference | Wu L, Yu YL, Galiano RD, Roth SI, Mustoe TA. Macrophage colony-stimulating factor accelerates wound healing and upregulates TGF-Β 1 mRNA levels through tissue macrophages. J Surg Res 1997; 72: 162 – 9. | en_US |
dc.identifier.citedreference | Luikart S, Wahl D, Hinkel T, Masri M, Oegema T. A fragment of Α-actinin promotes monocyte/macrophage maturation in vitro. Exp Hematol 1999; 27: 337 – 44. | en_US |
dc.identifier.citedreference | Luikart S, Krug H, Nelson R, Hinkel T, Majeski P, Gupta P, Mahowald M, Oegema T. Mactinin: a modulator of the monocyte response to inflammation. Arthritis Res Ther 2003; 5: R310 – 6. | en_US |
dc.identifier.citedreference | Masri MT, Wahl D, Oegema T, Luikart S. HL-60 cells degrade Α-actinin to produce a fragment that promotes monocyte/macrophage maturation. Exp Hematol 1999; 27: 345 – 52. | en_US |
dc.identifier.citedreference | Luikart S, Masri M, Wahl D, Hinkel T, Beck J, Gyetko M, Gupta P, Oegema T. Urokinase is required for the formation of mactinin, an Α-actinin fragment that promotes monocyte/macrophage maturation. Biochim Biophys Acta 2002; 1591: 99 – 107. | en_US |
dc.identifier.citedreference | Burridge K, Fath K, Kelly T, Nuckolls G, Turner C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 1988; 4: 487 – 525. | en_US |
dc.identifier.citedreference | Beck JM, Preston AM, Gyetko MR. Urokinase-type plasminogen activator in inflammatory cell recruitment and host defense against Pneumocystis carinii in mice. Infect Immun 1999; 67: 879 – 84. | en_US |
dc.identifier.citedreference | Kitching AR, Holdsworth SR, Ploplis VA, Plow EF, Collen D, Carmeliet P, Tipping PG. Plasminogen and plasminogen activators protect against renal injury in crescentic glomerulonephritis. J Exp Med 1997; 185: 963 – 8. | en_US |
dc.identifier.citedreference | Carmeliet P, Schoonjans L, Kieckens L, Ream B, Degen J, Bronson R, DeVos 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. | en_US |
dc.identifier.citedreference | Carmeliet P, Moons L, Herbert JM, Crawley J, Lupu F, Lijnen R, Collen D. Urokinase but not tissue plasminogen activator mediates arterial neointima formation in mice. Circ Res 1997; 81: 829 – 39. | en_US |
dc.identifier.citedreference | Herbert JM, Lamarche I, Carmeliet P. Urokinase and tissue-type plasminogen activator are required for the mitogenic and chemotactic effects of bovine fibroblast growth factor and platelet-derived growth factor BB for vascular smooth muscle cells. J Biol Chem 1997; 272: 23585 – 91. | en_US |
dc.identifier.citedreference | Gartner MH, Benson JD, Caldwell MD. Insulin-like growth factors I and II expression in the healing wound. J Surg Res 1992; 52: 389 – 94. | en_US |
dc.identifier.citedreference | Albina JE, Mills CD, Henry Jr WL, Caldwell MD. Temporal expression of different pathways of 1-arginine metabolism in healing wounds. J Immunol 1990; 144: 3877 – 80. | en_US |
dc.identifier.citedreference | Shearer JD, Coulter CF, Engeland WC, Roth RA, Caldwell MD. Insulin is degraded extracellularly in wounds by insulin-degrading enzyme (EC 3.4.24.56). Am J Physiol 1997; 273: E657 – 64. | en_US |
dc.identifier.citedreference | Gyetko MR, Chen GH, McDonald RA, Goodman R, Huffnagle GB, Wilkinson CC, Fuller JA, Toews GB. Urokinase is required for the pulmonary inflammatory response to Cryptococcus neoformans: a murine transgenic model. J Clin Invest 1996; 97: 1818 – 26. | en_US |
dc.identifier.citedreference | Singer VL, Jones LJ, Yue ST, Haugland RP. Characterization of picogreen reagent and development of a fluorescence-based solution assay for double-stranded DNA quantitation. Anal Biochem 1997; 249: 228 – 38. | en_US |
dc.identifier.citedreference | Reddy GK, Enwemeka CS. A simplified method for the analysis of hydroxyproline in biological tissues. Clin Biochem 1996; 29: 225 – 9. | en_US |
dc.identifier.citedreference | Bagby GC Jr, Heinrich MC. Growth factors, cytokines, and the control of hematopoiesis. In: Hoffman R, Benz Jr EJ, Shattil SJ, Furie B, Cohen HJ, Silberstein LE, McGlave P, editors. Hematology basic principles and practice. 3rd ed. New York, NY: Churchill Livingston, 2000: 154 – 202. | en_US |
dc.identifier.citedreference | Xia W, de Bock C, Murrell GA, Wang Y. Expression of urokinase-type plasminogen activator and its receptor is up-regulated during tendon healing. J Orthop Res 2003; 21: 819 – 25. | en_US |
dc.identifier.citedreference | Watanabe M, Yano W, Kondo S, Hattori Y, Yamada N, Yanai R, Nishida T. Up-regulation of urokinase-type plasminogen activator in corneal epithelial cells induced by wounding. Invest Ophthamol Vis Sci 2003; 44: 3332 – 8. | en_US |
dc.identifier.citedreference | Romani L, Puccetti P, Bistoni F. Interleukin-12 in infectious disease. Clin Microbiol Rev 1997; 10: 611 – 36. | en_US |
dc.identifier.citedreference | Gadina M, Ferguson P, Johnston J. New interleukins: are there any more? Curr Opin Infect Dis 2003; 16: 211 – 7. | en_US |
dc.identifier.citedreference | Gyetko MR, Sud S, Chen G-H, Fuller JA, Chensue SW, Toews GB. Urokinase-type plasminogen activator is required for the generation of a type 1 immune response to pulmonary Crpytococcus neoformans infection. J Immunol 2002; 168: 801 – 9. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.