Effect of dexamethasone on human osteoblasts in culture: involvement of beta 1 integrin and integrin-linked kinase

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art_NAVES_Effect_of_dexamethasone_on_human_osteoblasts_in_culture_2011.PDF (436.42 KB)
Citações na Scopus
13
Tipo de produção
article
Data de publicação
2011
DOI
Scopus
Web of Science
PubMed
Título da Revista
ISSN da Revista
Título do Volume
Editora
WILEY-BLACKWELL
Autores
NAVES, Marcelo A.
COMODO, Andreia N.
ALVARENGA, Erika L. F. C. de
TEIXEIRA, Vicente P. C.
Citação
CELL BIOLOGY INTERNATIONAL, v.35, n.11, p.1147-1151, 2011
Projetos de Pesquisa
Unidades Organizacionais
Fascículo
Resumo
Adhesive interactions play a critical role in cell biology, influencing vital processes from proliferation to cell death. Integrins regulate cell-ECM (extracellular matrix) adhesion and must associate with phosphorylating proteins such as ILK (integrin-linked kinase). Dysregulation of ILK expression is associated with anchorage-independent growth, cell survival and inhibition of apoptosis. Glucocorticoids influence differentiation and adhesion of osteoblasts and can affect bone protein synthesis. The objective of this study was to analyse the effect of DEX (dexamethasone) on the biology of osteoblasts, together with its influence on the expression of ILK and beta 1 integrin. For this, primary cultures of human osteoblasts were exposed to DEX at 10(-9) M (physiological dose) and 10(-6) M (pharmacological dose) for 24 and 48 h. Cell viability, apoptosis and cell adhesion were analysed, as well as protein expression of beta 1 integrin and ILK. It was observed that cell viability and adhesion were reduced in the cultures evaluated. In comparison with the control cultures, there was slightly less apoptosis in the cultures exposed to the physiological dose and considerably more apoptosis in those exposed to the pharmacological dose. In all treated cultures, protein expression of ILK was slightly higher than in the control cultures, whereas that of beta 1 integrin was significantly lower. Both proteins under study were co-localized at the cell periphery in all cultures. Our results suggest that DEX causes osteoblast anoikis, probably due to decreased beta 1 integrin expression, which might have had a direct influence upon ILK, reducing its activation and preventing it from playing its characteristic antiapoptotic role.
Palavras-chave
adhesion ability, glucocorticoid, integrin-linked kinase (ILK), osteoblast, primary cell culture, beta 1 integrin
URI
https://observatorio.fm.usp.br/handle/OPI/22599
Referências
  1. Grashoff C, 2004, CURR OPIN CELL BIOL, V16, P565, DOI 10.1016/j.ceb.2004.07.004
  2. Hannigan G, 2005, NAT REV CANCER, V5, P51, DOI 10.1038/nrc1524
  3. LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
  4. Espina B, 2008, J CELL PHYSIOL, V215, P488, DOI 10.1002/jcp.21335
  5. Claro S, 2007, J PHARMACOL EXP THER, V322, P964, DOI 10.1124/jpet.107.125930
  6. Marconi A, 2007, STEM CELLS, V25, P149, DOI 10.1634/stemcells.2006-0165
  7. Han SY, 2006, CELL TISSUE RES, V323, P321, DOI 10.1007/s00441-005-0065-4
  8. Weaver MS, 2008, J BIOL CHEM, V283, P22826, DOI 10.1074/jbc.M706563200
  9. Lian JB, 1997, ENDOCRINOLOGY, V138, P2117, DOI 10.1210/en.138.5.2117
  10. Pereira RMR, 2001, BONE, V28, P484, DOI 10.1016/S8756-3282(01)00422-7
  11. Hood JD, 2002, NAT REV CANCER, V2, P91, DOI 10.1038/nrc727
  12. Canalis E, 2007, OSTEOPOROSIS INT, V18, P1319, DOI 10.1007/s00198-007-0394-0
  13. Conradie MM, 2007, J ENDOCRINOL, V195, P229, DOI 10.1677/JOE-07-0217
  14. Oshina H, 2007, BONE, V41, P575, DOI 10.1016/j.bone.2007.06.022
  15. Simpson CD, 2008, CANCER LETT, V272, P177, DOI 10.1016/j.canlet.2008.05.029
  16. Merrill GF, 1998, METHOD CELL BIOL, V57, P229
  17. KREK W, 1995, METHOD ENZYMOL, V254, P114
  18. Frisch SM, 2001, CURR OPIN CELL BIOL, V13, P555, DOI 10.1016/S0955-0674(00)00251-9
  19. Hannigan GE, 1996, NATURE, V379, P91, DOI 10.1038/379091a0
  20. Canalis E, 1996, J CLIN ENDOCR METAB, V81, P3441, DOI 10.1210/jc.81.10.3441
  21. Beloti Márcio Mateus, 2005, Braz Dent J, V16, P156, DOI 10.1590/S0103-64402005000200013
  22. Caparbo VF, 2009, CLIN RHEUMATOL, V28, P71, DOI 10.1007/s10067-008-0985-y
  23. Cooper MS, 2004, CLIN SCI, V107, P111
  24. Coppolino MG, 1999, BIOCHEM J, V340, P41, DOI 10.1042/0264-6021:3400041
  25. Drury LJ, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0012895
  26. Forsprecher J, 2009, AMINO ACIDS, V36, P747, DOI 10.1007/s00726-008-0125-7
  27. FRISCH SM, 1994, J CELL BIOL, V124, P619, DOI 10.1083/jcb.124.4.619
  28. Giner RM, 2007, BIOCHEM BIOPH RES CO, V354, P414, DOI 10.1016/j.bbrc.2006.12.224
  29. Gkretsi V, 2007, HEPATOLOGY, V45, P1025, DOI 10.1002/hep.21540
  30. GRONOWICZ GA, 1995, ENDOCRINOLOGY, V136, P598, DOI 10.1210/en.136.2.598
  31. KRISHAN A, 1975, J CELL BIOL, V66, P188, DOI 10.1083/jcb.66.1.188
  32. Mikami Y, 2008, CELL BIOL INT, V32, P239, DOI 10.1016/j.cellbi.2007.08.033
  33. Strater J, 1996, GASTROENTEROLOGY, V110, P1776, DOI 10.1053/gast.1996.v110.pm8964403

Coleções
Artigos e Materiais de Revistas Científicas - FM/MCM
Artigos e Materiais de Revistas Científicas - HC/ICHC
Artigos e Materiais de Revistas Científicas - LIM/17