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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-4-19
pubmed:abstractText
Endostatin, the C-terminal proteolytic fragment of the noncollagenous domain 1 (NC1) of the basement membrane protein collagen XVIII, inhibits cell proliferation and migration. Placental and decidual expression of the peptide suggested a role in angiogenesis and/or extravillous trophoblast differentiation. Here, we demonstrate that supernatants of trophoblastic SGHPL-5 cells, purified first trimester villous trophoblasts and villous explant cultures contain proteases which in vitro cleave 20kDa endostatin from purified, recombinant NC1 domains. However, supernatants of decidual and villous fibroblasts failed to generate the 20kDa endostatin fragment. Moreover, we show that recombinant endostatin inhibits invasion of SGHPL-5 cells through Matrigel invasion chambers. Since mesenchymal cells but not trophoblasts produce collagen XVIII we suspect that invasive trophoblasts may produce endostatin upon contacting the extracellular matrix deposited by decidual stromal cells. Generation of endostatin through trophoblast-derived proteases could play a role in the regulation of trophoblast invasiveness.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0143-4004
pubmed:author
pubmed:issnType
Print
pubmed:volume
26 Suppl A
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S42-5
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Invasive trophoblasts generate regulatory collagen XVIII cleavage products.
pubmed:affiliation
Department of Obstetrics and Gynecology, Medical University of Vienna, Waehringer Guertel 18-20, A-1090 Vienna, Austria.
pubmed:publicationType
Journal Article