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INTEGRIN SYNTHESIS AND UTILIZATION IN CULTURED HUMAN OSTEOBLASTS
Author(s) -
PISTONE M.,
SANGUINETI C.,
FEDERICI A.,
SANGUINETI F.,
DEFILIPPI P.,
SANTOLINI F.,
QUERZÉ G.,
MARCHISIO P. C.,
MANDUCA P.
Publication year - 1996
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1996.0062
Subject(s) - fibronectin , integrin , vitronectin , laminin , extracellular matrix , microbiology and biotechnology , focal adhesion , adhesion , cell adhesion , polyclonal antibodies , chemistry , biology , antibody , immunology , biochemistry , cell , signal transduction , organic chemistry
This study describes the adhesion of human osteoblasts, cultured in vitro , to proteins of the extracellular matrix, the biosynthesis of integrins, their topography and organization in focal contacts. The adhesion of osteoblasts to laminin, type I collagen, vitronectin and fibronectin was 77–100%, in 2h and at 55n m substrata concentration, and it was accompained by spreading of the cells. Adhesion to fibronectin (FN), laminin (LN) and type I collagen (COL) was inhibited by antibodies to the β1 integrin and antibodies to the α5 chain affected adhesion only to fibronectin. Using a panel of polyclonal antibodies against α2, α3, α5, αv, β1 and β3 integrins we detected synthesis of α3β1, α5β1, αvβ3, and an αvβ1‐like dimer by immunoprecipitation of metabolically labelled cell lysates. Studies of immunolocalization demonstrated the presence of the same integrins identified in lysates, plus α4, α1 and β5 subunits. In cells adhering in the presence of serum we showed organization of β3 and αv integrins in focal contacts. In cells adhering to fibronectin α5 and β1 integrins were localized in focal contacts. In cells spread on laminin or type I collagen none of the integrins investigated was localized in focal contacts.