Peptides do not prevent cleavage of endoglin to produce soluble endoglin
Roxanne Hastie, Stephen Tong, Ping Cannon, Fiona Brownfoot, Natalie J Hannan, Tu'uhevaha Kaitu'u-Lino
PREGNANCY HYPERTENSION-AN INTERNATIONAL JOURNAL OF WOMENS CARDIOVASCULAR HEALTH | ELSEVIER SCI LTD | Published : 2014
MMP14 cleaves membrane bound endoglin to produce soluble endoglin (sEng), an anti-angiogenic factor that causes endothelial dysfunction in preeclampsia. A recent publication proposed peptides with an amino acid sequence straddling the MMP14 cleavage site on endoglin decreases sEng release. This may be an exciting therapeutic approach and requires validation. We administered peptides to JAR cells, and primary placental explants and endothelial cells. The peptides had no effect on sEng production, and did not block sEng production in HEK293 with MMP14 and endoglin overexpressed. Peptides with an amino acid sequence encompassing the cleavage site do not prevent sEng production in vitro.
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Awarded by National Health and Medical Research Council of Australia
The National Health and Medical Research Council of Australia provided salary (#1062418 to T.K, #628927 to N.H, #1050765 to S.T.) and project support (# 1048707) and Australian Postgraduate Award to F.B.