Human extravillous trophoblasts express laeverin, a novel protein that belongs to membrane-bound gluzincin metallopeptidases

Human extravillous trophoblasts (EVTs) invade the maternal decidua. To identify the molecules involved in EVT invasion, we raised a murine monoclonal antibody (CHL2) that reacts with human EVTs. The molecular mass of CHL2 antigen purified from placental tissues was 160 kDa. Although the N-terminal p...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2004-01, Vol.313 (4), p.962-968
Main Authors: Fujiwara, Hiroshi, Higuchi, Toshihiro, Yamada, Shigetoshi, Hirano, Takeshi, Sato, Yukiyasu, Nishioka, Yoshihiro, Yoshioka, Shinya, Tatsumi, Keiji, Ueda, Masamichi, Maeda, Michiyuki, Fujii, Shingo
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Antibodies, Monoclonal
Base Sequence
Catalytic Domain
CD13 Antigens - genetics
Cloning, Molecular
DNA, Complementary - genetics
Extravillous trophoblast
Female
Gluzincin metallopeptidase
Humans
Immunohistochemistry
In Vitro Techniques
Laeverin
Metalloproteases - chemistry
Metalloproteases - genetics
Metalloproteases - metabolism
Mice
Molecular Sequence Data
Molecular Weight
Monoclonal antibody
Pregnancy
Sequence Homology, Amino Acid
Trophoblasts - enzymology
Zinc - metabolism
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Summary:Human extravillous trophoblasts (EVTs) invade the maternal decidua. To identify the molecules involved in EVT invasion, we raised a murine monoclonal antibody (CHL2) that reacts with human EVTs. The molecular mass of CHL2 antigen purified from placental tissues was 160 kDa. Although the N-terminal partial amino acid sequence and one internal sequence are still unreported, the other three internal sequences matched those deduced from the coding region of the estimated sequence tag (1672 bp, AK075131). Based on this information, the full-length of the coding cDNA sequence of CHL2 antigen (2970 bp), which has not been reported elsewhere, was determined by 5 ′ RACE. This novel protein, named laeverin, has a peptidase M1 motif containing a zinc-binding active site. It also has a transmembrane domain near the N-terminus. Its amino acid sequence is homologous with aminopeptidase N. These data indicate that human EVTs express laeverin, a novel protein belonging to gluzincin metallopeptidases.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2003.12.024