Jh. Hughes et al., ENDOGLIN (CD105) EXPRESSION IN NONNEOPLASTIC AND NEOPLASTIC HUMAN TISSUES AND HUMAN CANCER CELL-LINES, Oncology Reports, 3(2), 1996, pp. 379-383
Endoglin is an integral membrane glycoprotein that binds TGF-beta(1,3)
with high affinity and is thought to play an important role in modula
ting the interaction of TGF-beta with its cell surface receptors. In t
his study a recently characterized monoclonal antibody (29-G8) recogni
zing endoglin was used to examine expression in a variety of human tis
sues and human cancer cell lines. Formalin-fixed, paraffin-embedded se
ctions were examined by light microscopy and cell lines were analyzed
by now cytometry. Immunostaining was noted in a variety of non-neoplas
tic epithelia from different organs; most of the neoplastic tissues su
rveyed also demonstrated prominent immunoreactivity for 29-G8. Flow cy
tometric analysis of the cell lines revealed strong 29-G8 immunoreacti
vity in almost all lines examined. Our results suggest that endoglin e
xpression is much more ubiquitous than was previously thought and that
endoglin may play a role in modulating TGF-beta binding activity in a
variety of normal and neoplastic human tissues.