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Journal of Toxicology
Volume 2012 (2012), Article ID 325250, 8 pages
A Lipocalin-Derived Peptide Modulating Fibroblasts and Extracellular Matrix Proteins
1Laboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, Brazil
2Center for Applied Toxinology, Butantan Institute, 05503-900 São Paulo, SP, Brazil
3Department of Orthopedics and Traumatology, Faculty of Medicine, University of São Paulo, 01246-903 São Paulo, SP, Brazil
Received 3 January 2012; Revised 23 February 2012; Accepted 15 April 2012
Academic Editor: Yonghua Ji
Copyright © 2012 Linda Christian Carrijo-Carvalho et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- R. J. McAnulty, “Fibroblasts and myofibroblasts: their source, function and role in disease,” International Journal of Biochemistry and Cell Biology, vol. 39, no. 4, pp. 666–671, 2007.
- G. J. Fisher, J. Varani, and J. J. Voorhees, “Looking older: fibroblast collapse and therapeutic implications,” Archives of Dermatology, vol. 144, no. 5, pp. 666–672, 2008.
- J. P. Hodde and C. E. Johnson, “Extracellular matrix as a strategy for treating chronic wounds,” American Journal of Clinical Dermatology, vol. 8, no. 2, pp. 61–66, 2007.
- H. Ihn, “Scleroderma, fibroblasts, signaling, and excessive extracellular matrix,” Current Rheumatology Reports, vol. 7, no. 2, pp. 156–162, 2005.
- T. A. Wynn, “Cellular and molecular mechanisms of fibrosis,” Journal of Pathology, vol. 214, no. 2, pp. 199–210, 2008.
- G. Riley, “Chronic tendon pathology: molecular basis and therapeutic implications,” Expert Reviews in Molecular Medicine, vol. 7, no. 5, pp. 1–25, 2005.
- E. Black, J. Vibe-Petersen, L. N. Jorgensen et al., “Decrease of collagen deposition in wound repair in type 1 diabetes independent of glycemic control,” Archives of Surgery, vol. 138, no. 1, pp. 34–40, 2003.
- R. L. Chevalier, B. A. Thornhill, M. S. Forbes, and S. C. Kiley, “Mechanisms of renal injury and progression of renal disease in congenital obstructive nephropathy,” Pediatric Nephrology, vol. 25, no. 4, pp. 687–697, 2010.
- O. Sacco, M. Silvestri, F. Sabatini, R. Sale, A. C. Defilippi, and G. A. Rossi, “Epithelial cells and fibroblasts: structural repair and remodelling in the airways,” Paediatric Respiratory Reviews, vol. 5, pp. S35–S40, 2004.
- S. Rutschow, J. Li, H. P. Schultheiss, and M. Pauschinger, “Myocardial proteases and matrix remodeling in inflammatory heart disease,” Cardiovascular Research, vol. 69, no. 3, pp. 646–656, 2006.
- S. Xu and P. Venge, “Lipocalins as biochemical markers of disease,” Biochimica et Biophysica Acta, vol. 1482, no. 1-2, pp. 298–307, 2000.
- E. A. Thomas, S. M. Laws, J. G. Sutcliffe et al., “Apolipoprotein D levels are elevated in prefrontal cortex of subjects with Alzheimer's disease: no relation to apolipoprotein E expression or genotype,” Biological Psychiatry, vol. 54, no. 2, pp. 136–141, 2003.
- A. L. Hemdahl, A. Gabrielsen, C. Zhu et al., “Expression of neutrophil gelatinase-associated lipocalin in atherosclerosis and myocardial infarction,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 26, no. 1, pp. 136–142, 2006.
- K. Mori and K. Nakao, “Neutrophil gelatinase-associated lipocalin as the real-time indicator of active kidney damage,” Kidney International, vol. 71, no. 10, pp. 967–970, 2007.
- J. Yang and M. A. Moses, “Lipocalin 2: a multifaceted modulator of human cancer,” Cell Cycle, vol. 8, no. 15, pp. 2347–2352, 2009.
- H. J. Kim, H. J. Je, H. M. Cheon et al., “Accumulation of 23 kDa lipocalin during brain development and injury in Hyphantria cunea,” Insect Biochemistry and Molecular Biology, vol. 35, no. 10, pp. 1133–1141, 2005.
- M. D. Ganfornina, S. Do Carmo, E. Martínez et al., “ApoD, a glia-derived apolipoprotein, is required for peripheral nerve functional integrity and a timely response to injury,” Glia, vol. 58, no. 11, pp. 1320–1334, 2010.
- S. Petta, C. Tripodo, S. Grimaudo et al., “High liver RBP4 protein content is associated with histological features in patients with genotype 1 chronic hepatitis C and with nonalcoholic steatohepatitis,” Digestive and Liver Disease, vol. 43, no. 5, pp. 404–410, 2011.
- P. Spreyer, H. Schaal, G. Kuhn et al., “Regeneration-associated high level expression of apolipoprotein D mRNA in endoneurial fibroblasts of peripheral nerve,” EMBO Journal, vol. 9, no. 8, pp. 2479–2484, 1990.
- R. J. Playford, A. Belo, R. Poulsom et al., “Effects of mouse and human lipocalin homologues 24p3/lcn2 and neutrophil gelatinase-associated lipocalin on gastrointestinal mucosal integrity and repair,” Gastroenterology, vol. 131, no. 3, pp. 809–817, 2006.
- A. Kawahara, A. Hikosaka, T. Sasado, and K. Hirota, “Thyroid hormone-dependent repression of α1-microglobulin/bikunin precursor (AMBP) gene expression during amphibian metamorphosis,” Development Genes and Evolution, vol. 206, no. 6, pp. 355–362, 1997.
- K. Yamauchi, H. A. Takeuchi, M. Overall, M. Dziadek, S. L. A. Munro, and G. Schreiber, “Structural characteristics of bullfrog (Rana catesbeiana) transthyretin and its cDNA. Comparison of its pattern of expression during metamorphosis with that of lipocalin,” European Journal of Biochemistry, vol. 256, no. 2, pp. 287–296, 1998.
- F. Stewart, M. W. Kennedy, and S. Suire, “A novel uterine lipocalin supporting pregnancy in equids,” Cellular and Molecular Life Sciences, vol. 57, no. 10, pp. 1373–1378, 2000.
- F. D. Cancedda, B. Dozin, B. Zerega, S. Cermelli, and R. Cancedda, “Ex-FABP: a fatty acid binding lipocalin developmentally regulated in chicken endochondral bone formation and myogenesis,” Biochimica et Biophysica Acta, vol. 1482, no. 1-2, pp. 127–135, 2000.
- A. Pagano, P. Giannoni, A. Zambotti et al., “CALβ, a novel lipocalin associated with chondrogenesis and inflammation,” European Journal of Cell Biology, vol. 81, no. 5, pp. 264–272, 2002.
- D. Sanchez, M. D. Ganfornina, and M. J. Bastiani, “Developmental expression of the lipocalin Lazarillo and its role in axonal pathfinding in the grasshopper embryo,” Development, vol. 121, no. 1, pp. 135–147, 1995.
- C. Gentili, G. Tutolo, B. Zerega, E. Di Marco, R. Cancedda, and F. Descalzi Cancedda, “Acute phase lipocalin Ex-FABP is involved in heart development and cell survival,” Journal of Cellular Physiology, vol. 202, no. 3, pp. 683–689, 2005.
- Z. Li, V. Korzh, and Z. Gong, “Localized rbp4 expression in the yolk syncytial layer plays a role in yolk cell extension and early liver development,” BMC Developmental Biology, vol. 7, article 117, 2007.
- M. E. Ricci-Silva, R. H. Valente, I. R. León et al., “Immunochemical and proteomic technologies as tools for unravelling toxins involved in envenoming by accidental contact with Lonomia obliqua caterpillars,” Toxicon, vol. 51, no. 6, pp. 1017–1028, 2008.
- A. B. G. Veiga, J. M. C. Ribeiro, J. A. Guimarães, and I. M. B. Francischetti, “A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome,” Gene, vol. 355, no. 1-2, pp. 11–27, 2005.
- D. R. Flower, A. C. T. North, and T. K. Attwood, “Structure and sequence relationships in the lipocalins and related proteins,” Protein Science, vol. 2, no. 5, pp. 753–761, 1993.
- D. R. Flower, “The lipocalin protein family: structure and function,” Biochemical Journal, vol. 318, no. 1, pp. 1–14, 1996.
- A. M. Chudzinski-Tavassi, L. C. Carrijo-Carvalho, K. Waismam, S. H. P. Farsky, O. H. P. Ramos, and C. V. Reis, “A lipocalin sequence signature modulates cell survival,” FEBS Letters, vol. 584, no. 13, pp. 2896–2900, 2010.
- T. Rozario and D. W. DeSimone, “The extracellular matrix in development and morphogenesis: a dynamic view,” Developmental Biology, vol. 341, no. 1, pp. 126–140, 2010.
- S. Do Carmo, L. C. Levros Jr., and E. Rassart, “Modulation of apolipoprotein D expression and translocation under specific stress conditions,” Biochimica et Biophysica Acta, vol. 1773, no. 6, pp. 954–969, 2007.
- A. C. T. North, “Three-dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins,” International Journal of Biological Macromolecules, vol. 11, no. 1, pp. 56–58, 1989.
- C. V. Reis, S. A. Andrade, O. H. P. Ramos et al., “Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure-function insights,” Biochemical Journal, vol. 398, no. 2, pp. 295–302, 2006.
- A. M. Chudzinski-Tavassi, M. Schattner, M. Fritzen et al., “Effects of Lopap on human endothelial cells and platelets,” Haemostasis, vol. 31, no. 3–6, pp. 257–265, 2001.
- M. Fritzen, M. P. A. Flores, C. V. Reis, and A. M. Chudzinski-Tavassi, “A prothrombin activator (Lopap) modulating inflammation, coagulation and cell survival mechanisms,” Biochemical and Biophysical Research Communications, vol. 333, no. 2, pp. 517–523, 2005.
- K. Waismam, A. M. Chudzinski-Tavassi, L. C. Carrijo-Carvalho, M. T. Fernandes Pacheco, and S. H. P. Farsky, “Lopap: a non-inflammatory and cytoprotective molecule in neutrophils and endothelial cells,” Toxicon, vol. 53, no. 6, pp. 652–659, 2009.
- P. Berman, P. Gray, E. Chen et al., “Sequence analysis, cellular localization, and expression of a neuroretina adhesion and cell survival molecule,” Cell, vol. 51, no. 1, pp. 135–142, 1987.
- M. Taniike, I. Mohri, N. Eguchi, C. T. Beuckmann, K. Suzuki, and Y. Urade, “Perineuronal oligodendrocytes protect against neuronal apoptosis through the production of lipocalin-type prostaglandin D synthase in a genetic demyelinating model,” Journal of Neuroscience, vol. 22, no. 12, pp. 4885–4896, 2002.
- Z. Tong, X. Wu, D. Ovcharenko, J. Zhu, C. S. Chen, and J. P. Kehrer, “Neutrophil gelatinase-associated lipocalin as a survival factor,” Biochemical Journal, vol. 391, no. 2, pp. 441–448, 2005.
- J. Bullwinkel, B. Baron-Lühr, A. Lüdemann, C. Wohlenberg, J. Gerdes, and T. Scholzen, “Ki-67 protein is associated with ribosomal RNA transcription in quiescent and proliferating cells,” Journal of Cellular Physiology, vol. 206, no. 3, pp. 624–635, 2006.
- A. Li, M. L. Varney, J. Valasek, M. Godfrey, B. J. Dave, and R. K. Singh, “Autocrine role of interleukin-8 in induction of endothelial cell proliferation, survival, migration and MMP-2 production and angiogenesis,” Angiogenesis, vol. 8, no. 1, pp. 63–71, 2005.
- L. A. Madge and J. S. Pober, “A phosphatidylinositol 3-kinase/Akt pathway, activated by tumor necrosis factor or interleukin-1, inhibits apoptosis but does not activate NFκB in human endothelial cells,” The Journal of Biological Chemistry, vol. 275, no. 20, pp. 15458–15465, 2000.
- H. Ellingsgaard, J. A. Ehses, E. B. Hammar et al., “Interleukin-6 regulates pancreatic α-cell mass expansion,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 35, pp. 13163–13168, 2008.
- R. Gillitzer and M. Goebeler, “Chemokines in cutaneous wound healing,” Journal of Leukocyte Biology, vol. 69, no. 4, pp. 513–521, 2001.
- S. Werner and R. Grose, “Regulation of wound healing by growth factors and cytokines,” Physiological Reviews, vol. 83, no. 3, pp. 835–870, 2003.