{'fraction_non_alphanumeric': 0.02294792586054722, 'fraction_numerical': 0.01235657546337158, 'mean_word_length': 5.265193370165746, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Endoglin (CD105) expression in non-neoplastic and neoplastic human tissues and human cancer cell lines.

Endoglin is an integral membrane glycoprotein that binds TGF-beta(1,3) with high affinity and is thought to play an important role in modulating the interaction of TGF-beta with its cell surface receptors. In this study a recently characterized monoclonal antibody (29-G8) recognizing endoglin was used to examine expression in a variety of human tissues and human cancer cell lines. Formalin-fixed, paraffin-embedded sections were examined by light microscopy and cell lines were analyzed by now cytometry. Immunostaining was noted in a variety of non-neoplastic epithelia from different organs; most of the neoplastic tissues surveyed also demonstrated prominent immunoreactivity for 29-G8. Flow cytometric analysis of the cell lines revealed strong 29-G8 immunoreactivity in almost all lines examined. Our results suggest that endoglin expression 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.