T. Tani et al., FOCAL ADHESION KINASE PP125(FAK) IS ASSOCIATED WITH BOTH INTERCELLULAR-JUNCTIONS AND MATRIX ADHESION SITES IN-VIVO, HISTOCHEM C, 105(1), 1996, pp. 17-25
Previous studies have characterized pp125(FAK) as a focal adhesion (FA
)-associated non-receptor tyrosine kinase. However, there are few data
available on the expression and localization of this kinase in tissue
s. In this study we show that in human tissues the highest expression
of pp125(FAK) is found in some developing epithelia, where pp125(FAK)
is associated with either intercellular junctions or with sites of adh
esion to the basement membrane, whereas the same adult tissues show on
ly a faint reactivity. Connective tissue cells do not show any reactiv
ity for pp125(FAK) in vivo, but developing arterial smooth muscle expr
esses pp125(FAK) at high levels. The expression pattern in malignant t
issues is variable, but most carcinomas do not express this kinase. In
primary cultures of human amnion epithelial cells pp125(FAK) first be
comes associated with the polarized adhesion lamellae, but is subseque
ntly translocated to the forming adherens junctions (AJs). Later upon
culturing pp125(FAK) becomes associated with prominent FAs, as in cult
ured cell lines. Taken together, our results suggest that the associat
ion of pp125(FAK) With FAs in cultured cells is principally due to a p
rocess of adaptation, whereas in vivo pp125(FAK) mainly functions as a
regulatory component of intercellular AJs and cell-matrix adhesions o
f developing epithelia and also in developing arterial smooth muscle.