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Titolo:
HUMAN OSTEOCLAST-LIKE CELLS SELECTIVELY RECOGNIZE LAMININ ISOFORMS, AN EVENT THAT INDUCES MIGRATION AND ACTIVATES CA2+ MEDIATED SIGNALS
Autore:
COLUCCI S; GIANNELLI G; GRANO M; FACCIO R; QUARANTA V; ZALLONE AZ;
Indirizzi:
UNIV BARI,INST HUMAN ANAT BARI ITALY UNIV BARI,INST HUMAN ANAT BARI ITALY UNIV BARI,IST CLIN MED 2 BARI ITALY SCRIPPS CLIN & RES INST,DEPT CELL BIOL LA JOLLA CA 00000
Titolo Testata:
Journal of Cell Science
, volume: 109, anno: 1996,
parte:, 6
pagine: 1527 - 1535
SICI:
0021-9533(1996)109:<1527:HOCSRL>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXTRACELLULAR-MATRIX RECEPTORS; HUMAN-ENDOTHELIAL CELLS; BASEMENT-MEMBRANES; MONOCLONAL-ANTIBODIES; ADHESION RECEPTORS; INTEGRIN RECEPTOR; LINE PC12; FIBRONECTIN; ATTACHMENT; COLLAGEN;
Keywords:
OSTEOCLAST; LAMININ; ADHESION; MIGRATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
S. Colucci et al., "HUMAN OSTEOCLAST-LIKE CELLS SELECTIVELY RECOGNIZE LAMININ ISOFORMS, AN EVENT THAT INDUCES MIGRATION AND ACTIVATES CA2+ MEDIATED SIGNALS", Journal of Cell Science, 109, 1996, pp. 1527-1535

Abstract

Osteoclast precursors are chemotactically attracted to sites of bone resorption via migration pathways that include transendothelial crossing in blood capillaries. Transendothelial migration involves poorly understood interactions with basal lamina molecules, including laminins. To investigate osteoclast-laminin interactions, we used human osteoclast-like cell lines obtained from giant cell tumors of bone (GCT 23 and GCT 24). These cell lines are a well-characterized model for osteoclast functions, such as bone resorption and the behaviour of osteoclastprecursors. Both GCT cell lines adhered to laminin-2 (merosin) coatedwells in standard adhesion assays, but failed to adhere to laminin-1 (EHS-laminin). By light microscopy, GCT cells on laminin-2 were partially spread, with a motile morphology. None of the anti-integrin antibodies tested inhibited GCT cells adhesion to laminin-2. Peptides containing the integrin adhesion site RGD or the laminin adhesion sequence IKVAV did not inhibit GCT cell adhesion to laminin-2. By immunofluorescence, beta(1) integrins were organized in focal adhesions. However, inthe presence of monensin this reorganization of beta(1) integrins wasabolished, indicating that it was probably due to secretion of fibronectin by GCT cells subsequent to adhesion to laminin-2. GCT cells transmigrated through membranes coated with laminin-2, much more efficiently than through membranes coated with collagen. Migration was induced by osteocalcin, as a chemoattractant, in a dose-dependent manner. At low osteocalcin concentrations, transmigration was detectable on laminin-2 but not collagen. In cells loaded with fura-2, a sharp increase inintracellular Ca2+ was detected upon addition of soluble laminin-2, but not laminin-1, due to release from thapsigargin-dependent intracellular stores. In summary, osteoclasts may recognize laminin isoforms differentially. Initial adhesion to laminin-2 appears to be due to integrin-independent mechanisms. Such adhesion, though, may trigger secretion of fibronectin that could then support spreading and efficient chemotactic migration. These mechanisms may play an important role in facilitating chemotactic migration of osteoclast precursors toward the bone surface.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:19:11