Open Access
Issue
Vet. Res.
Volume 41, Number 5, September–October 2010
Number of page(s) 11
DOI http://dx.doi.org/10.1051/vetres/2010047
Published online 29 July 2010
How to cite this article Vet. Res. (2010) 41:75
  • Ackermann M.R., Brogden K.A., Response of the ruminant respiratory tract to Mannheimia (Pasteurella) haemolytica, Microbes Infect. (2000) 2:1079–1088. [CrossRef] [PubMed]
  • Amato I., Ciapetti G., Pagani S., Marletta G., Satriano C., Baldini N., Granchi D., Expression of cell adhesion receptors in human osteoblasts cultured on biofunctionalized poly-(epsilon-caprolactone) surfaces, Biomaterials (2007) 28:3668–3678. [CrossRef] [PubMed]
  • Barja-Fidalgo C., Coelho A.L., Saldanha-Gama R., Helal-Neto E., Mariano-Oliveira A., Freitas M.S., Disintegrins: integrin selective ligands which activate integrin-coupled signaling and modulate leukocyte functions, Braz. J. Med. Biol. Res. (2005) 38:1513–1520. [CrossRef] [PubMed]
  • Berton G., Lowell C.A., Integrin signalling in neutrophils and macrophages, Cell. Signal. (1999) 11:621–635. [CrossRef] [PubMed]
  • Bianchi S.M., Dockrell D.H., Renshaw S.A., Sabroe I., Whyte M.K., Granulocyte apoptosis in the pathogenesis and resolution of lung disease, Clin. Sci. (Lond.) (2006) 110:293–304. [CrossRef]
  • Broxterman H.J., Hoekman K., Direct activation of caspases by RGD-peptides may increase drug sensitivity of tumour cells, Drug Resist. Updat. (1999) 2:139–141. [CrossRef] [PubMed]
  • Carman C.V., Springer T.A., Integrin avidity regulation: are changes in affinity and conformation underemphasized?, Curr. Opin. Cell Biol. (2003) 15:547–556. [CrossRef] [PubMed]
  • Castel S., Pagan R., Mitjans F., Piulats J., Goodman S., Jonczyk A., et al., RGD peptides and monoclonal antibodies, antagonists of alpha(v)-integrin, enter the cells by independent endocytic pathways, Lab. Invest. (2001) 81:1615–1626. [PubMed]
  • Chen L.W., Lin M.W., Hsu C.M., Different pathways leading to activation of extracellular signal-regulated kinase and p38 MAP kinase by formyl-methionyl-leucyl-phenylalanine or platelet activating factor in human neutrophils, J. Biomed. Sci. (2005) 12:311–319. [CrossRef] [PubMed]
  • Chun A.L., Moralez J.G., Webster T.J., Fenniri H., Helical rosette nanotubes: a biomimetic coating for orthopedics?, Biomaterials (2005) 26:7304–7309. [CrossRef] [PubMed]
  • Dos Santos C., Davidson D., Neutrophil chemotaxis to leukotriene B4 in vitro is decreased for the human neonate, Pediatr. Res. (1993) 33:242–246. [PubMed]
  • Fenniri H., Mathivanan P., Vidale K.L., Sherman D.M., Hallenga K., Wood K.V., Stowell J.G., Helical rosette nanotubes: design, self-assembly, and characterization, J. Am. Chem. Soc. (2001) 123:3854–3855. [CrossRef] [PubMed]
  • Fenniri H., Deng B.L., Ribbe A.E., Helical rosette nanotubes with tunable chiroptical properties, J. Am. Chem. Soc. (2002) 124:11064–11072. [CrossRef] [PubMed]
  • Fenniri H., Deng B.L., Ribbe A.E., Hallenga K., Jacob J., Thiyagarajan P., Entropically driven self-assembly of multichannel rosette nanotubes, Proc. Natl Acad. Sci. USA (2002) 99 (Suppl. 2):6487–6492. [CrossRef]
  • Giancotti F.G., Ruoslahti E., Integrin signaling, Science (1999) 285:1028–1032. [CrossRef] [PubMed]
  • Ginsberg M.H., Partridge A., Shattil S.J., Integrin regulation, Curr. Opin. Cell Biol. (2005) 17:509–516. [CrossRef] [PubMed]
  • Hii C.S., Stacey K., Moghaddami N., Murray A.W., Ferrante A., Role of the extracellular signal-regulated protein kinase cascade in human neutrophil killing of Staphylococcus aureus and Candida albicans and in migration, Infect. Immun. (1999) 67:1297–1302. [PubMed]
  • Hofmann U.B., Westphal J.R., Zendman A.J., Becker J.C., Ruiter D.J., van Muijen G.N., Expression and activation of matrix metalloproteinase-2 and its co-localization with membrane-type 1 matrix metalloproteinase correlate with melanoma progression, J. Pathol. (2000) 191:245–256. [CrossRef] [PubMed]
  • Huang C., Jacobson K., Schaller M.D., MAP kinases and cell migration, J. Cell Sci. (2004) 117:4619–4628. [CrossRef] [PubMed]
  • Journeay W.S., Suri S.S., Fenniri H., Singh B., High-aspect ratio nanoparticles in nanotoxicology, Integr. Environ. Assess. Manag. (2008) 4:128–129. [CrossRef] [PubMed]
  • Journeay W.S., Suri S.S., Moralez J.G., Fenniri H., Singh B., Low inflammatory activation by self-assembling Rosette nanotubes in human Calu-3 pulmonary epithelial cells, Small (2008) 4:817–823. [CrossRef] [PubMed]
  • Journeay W.S., Suri S.S., Moralez J.G., Fenniri H., Singh B., Rosette nanotubes show low acute pulmonary toxicity in vivo, Int. J. Nanomedicine (2008) 3:373–383. [PubMed]
  • Juliano R.L., Reddig P., Alahari S., Edin M., Howe A., Aplin A., Integrin regulation of cell signalling and motility, Biochem. Soc. Trans. (2004) 32:443–446. [CrossRef] [PubMed]
  • Klemke R.L., Cai S., Giannini A.L., Gallagher P.J., de Lanerolle P., Cheresh D.A., Regulation of cell motility by mitogen-activated protein kinase, J. Cell Biol. (1997) 137:481–492. [CrossRef] [PubMed]
  • Lawson M.A., Maxfield F.R., Ca(2+)- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils, Nature (1995) 377:75–79. [CrossRef] [PubMed]
  • Lekeux P., BRDC and the modulation of lung inflammation, Vet. J. (2006) 171:14–15. [CrossRef] [PubMed]
  • Matute-Bello G., Martin T.R., Science review: apoptosis in acute lung injury, Crit. Care (2003) 7:355–358. [CrossRef] [PubMed]
  • Meszaros A.J., Reichner J.S., Albina J.E., Macrophage-induced neutrophil apoptosis, J. Immunol. (2000) 165:435–441. [PubMed]
  • Montet X., Funovics M., Montet-Abou K., Weissleder R., Josephson L., Multivalent effects of RGD peptides obtained by nanoparticle display, J. Med. Chem. (2006) 49:6087–6093. [CrossRef] [PubMed]
  • Moon C., Han J.R., Park H.J., Hah J.S., Kang J.L., Synthetic RGDS peptide attenuates lipopolysaccharide-induced pulmonary inflammation by inhibiting integrin signaled MAP kinase pathways, Respir. Res. (2009) 10:18.
  • Narducci D., An introduction to nanotechnologies: what’s in it for us?, Vet. Res. Commun. (2007) 31 (Suppl. 1):131–137. [CrossRef] [PubMed]
  • Nopp A., Lundahl J., Stridh H., Caspase activation in the absence of mitochondrial changes in granulocyte apoptosis, Clin. Exp. Immunol. (2002) 128:267–274. [CrossRef] [PubMed]
  • Perl M., Chung C.S., Perl U., Biffl W.L., Cioffi W.G., Ayala A., Beneficial versus detrimental effects of neutrophils are determined by the nature of the insult, J. Am. Coll. Surg. (2007) 204:840–852; discussion 852–843. [CrossRef] [PubMed]
  • Pullikuth A.K., Catling A.D., Scaffold mediated regulation of MAPK signaling and cytoskeletal dynamics: a perspective, Cell. Signal. (2007) 19:1621–1632. [CrossRef] [PubMed]
  • Quint J.K., Wedzicha J.A., The neutrophil in chronic obstructive pulmonary disease, J. Allergy Clin. Immunol. (2007) 119:1065–1071. [CrossRef] [PubMed]
  • Roberts M.S., Woods A.J., Shaw P.E., Norman J.C., ERK1 associates with alpha(v)beta 3 integrin and regulates cell spreading on vitronectin, J. Biol. Chem. (2003) 278:1975–1985. [CrossRef] [PubMed]
  • Roets E., Burvenich C., Diez-Fraile A., Noordhuizen-Stassen E.N., Evaluation of the role of endotoxin and cortisol on modulation of CD18 adhesion receptors in cows with mastitis caused by Escherichia coli, Am. J. Vet. Res. (1999) 60:534–540. [PubMed]
  • Sano J., Oguma K., Kano R., Yazawa M., Tsujimoto H., Hasegawa A., High expression of Bcl-xL in delayed apoptosis of canine neutrophils induced by lipopolysaccharide, Res. Vet. Sci. (2005) 78:183–187. [CrossRef] [PubMed]
  • Snowder G.D., Van Vleck L.D., Cundiff L.V., Bennett G.L., Bovine respiratory disease in feedlot cattle: environmental, genetic, and economic factors, J. Anim. Sci. (2006) 84:1999–2008. [CrossRef] [PubMed]
  • Stupack D.G., Cho S.Y., Klemke R.L., Molecular signaling mechanisms of cell migration and invasion, Immunol. Res. (2000) 21:83–88. [CrossRef] [PubMed]
  • Suri S.S., Rakotondradany F., Myles A.J., Fenniri H., Singh B., The role of RGD-tagged helical rosette nanotubes in the induction of inflammation and apoptosis in human lung adenocarcinoma cells through the p38 MAPK pathway, Biomaterials (2009) 30:3084–3090. [CrossRef] [PubMed]
  • Sweeney J.F., Nguyen P.K., Omann G.M., Hinshaw D.B., Lipopolysaccharide protects polymorphonuclear leukocytes from apoptosis via tyrosine phosphorylation-dependent signal transduction pathways, J. Surg. Res. (1998) 74:64–70. [CrossRef] [PubMed]
  • Takagi J., Petre B.M., Walz T., Springer T.A., Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling, Cell (2002) 110:599–611. [CrossRef] [PubMed]
  • Tsukada H., Ying X., Fu C., Ishikawa S., McKeown-Longo P.J., Albelda S.M., et al., Ligation of endothelial alpha v beta 3 integrin increases capillary hydraulic conductivity of rat lung, Circ. Res. (1995) 77:651–659. [PubMed]
  • Ulijn R.V., Smith A.M., Designing peptide based nanomaterials, Chem. Soc. Rev. (2008) 37:664–675. [CrossRef] [PubMed]
  • Van Oostveldt K., Dosogne H., Burvenich C., Paape M.J., Brochez V., Van den Eeckhout E., Flow cytometric procedure to detect apoptosis of bovine polymorphonuclear leukocytes in blood, Vet. Immunol. Immunopathol. (1999) 70:125–133. [CrossRef] [PubMed]
  • Vucic D., Fairbrother W.J., The inhibitor of apoptosis proteins as therapeutic targets in cancer, Clin. Cancer Res. (2007) 13:5995–6000. [CrossRef] [PubMed]
  • Wu W.S., Wu J.R., Hu C.T., Signal cross talks for sustained MAPK activation and cell migration: the potential role of reactive oxygen species, Cancer Metastasis Rev. (2008) 27:303–314. [CrossRef] [PubMed]