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J. Biol. Chem., Vol. 265, Issue 15, 8361-8364, 05, 1990
A Gougos and M Letarte
Endoglin is a major glycoprotein of human vascular endothelium. As observed
with monoclonal antibody 44G4, the distribution of endoglin is restricted
to endothelial cells in all tissues except bone marrow. cDNA clones were
isolated from an endothelial cell lambda gt11 cDNA library using a rabbit
antibody prepared against endoglin purified from placenta. Eleven
antibody-positive and cross-hybridizing clones were obtained; reactivity
with endothelial cell 3.4-kilobase mRNA transcript was observed. The
N-terminal sequence of placental endoglin was determined and found within
the deduced protein sequence, thus confirming the identity of the cDNA and
revealing a partial signal peptide. Endoglin is a type I integral membrane
protein of Mr = 68,051 with an extracellular region of 561 amino acids, a
hydrophobic transmembrane domain, and a 47-residue cytoplasmic tail. There
are four potential N-linked glycosylation sites in the N-terminal domain
and a probable O-glycan domain rich in Ser and Thr residues proximal to the
membrane-spanning domain. Data base searches revealed that endoglin is a
novel protein. The sequence contains an RGD tripeptide (374-376), the first
identified on a surface protein of endothelium. The presence of RGD, a key
recognition structure in cellular adhesion, suggests a critical role for
endoglin in the binding of endothelial cells to integrins and/or other RGD
receptors.
Primary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells
Research Institute, Hospital for Sick Children, Toronto, Canada.
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