PMID- 20335639
OWN - NLM
STAT- MEDLINE
DCOM- 20101027
LR  - 20211020
IS  - 1529-7268 (Electronic)
IS  - 0006-3363 (Print)
IS  - 0006-3363 (Linking)
VI  - 83
IP  - 1
DP  - 2010 Jul
TI  - Human pregnancy specific beta-1-glycoprotein 1 (PSG1) has a potential role in 
      placental vascular morphogenesis.
PG  - 27-35
LID - 10.1095/biolreprod.109.082412 [doi]
AB  - Previous studies suggest that human pregnancy specific beta-1-glycoproteins 
      (PSGs) play immunomodulatory roles during pregnancy; however, other possible 
      functions of PSGs have yet to be explored. We have observed that PSGs induce 
      transforming growth factor beta 1 (TGFB1), which among its other diverse 
      functions inhibits T-cell function and has proangiogenic properties. The present 
      study investigates a potential role for PSG1, the most abundant PSG in maternal 
      serum, as a possible inducer of proangiogenic growth factors known to play an 
      important role in establishment of the vasculature at the maternal-fetal 
      interface. To this end, we measured TGFB1, vascular endothelial growth factors 
      (VEGFs) A and C, and placental growth factor (PGF) protein levels in several cell 
      types after PSG1 treatment. In addition, tube formation and wound healing assays 
      were performed to investigate a possible direct interaction between PSG1 and 
      endothelial cells. PSG1 induced up-regulation of both TGFB1 and VEGFA in human 
      monocytes, macrophages, and two human extravillous trophoblast cell lines. We did 
      not observe induction of VEGFC or PGF by PSG1 in any of the cells tested. PSG1 
      treatment resulted in endothelial tube formation in the presence and absence of 
      VEGFA. Site-directed mutagenesis was performed to map the essential regions 
      within the N-domain of PSG1 required for functional activity. We found that the 
      aspartic acid at position 95, previously believed to be required for binding of 
      PSGs to cells, is not required for PSG1 activity but that the amino acids 
      implicated in the formation of a salt bridge within the N-domain are essential 
      for PSG1 function.
FAU - Ha, Cam T
AU  - Ha CT
AD  - Department of Pathology, Uniformed Services University of the Health Sciences, 
      4301 Jones Bridge Road, Bethesda, MD 20814, USA.
FAU - Wu, Julie A
AU  - Wu JA
FAU - Irmak, Ster
AU  - Irmak S
FAU - Lisboa, Felipe A
AU  - Lisboa FA
FAU - Dizon, Anne M
AU  - Dizon AM
FAU - Warren, James W
AU  - Warren JW
FAU - Ergun, Suleyman
AU  - Ergun S
FAU - Dveksler, Gabriela S
AU  - Dveksler GS
LA  - eng
GR  - R01 HD 035832/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20100324
PL  - United States
TA  - Biol Reprod
JT  - Biology of reproduction
JID - 0207224
RN  - 0 (PGF protein, human)
RN  - 0 (Pregnancy Proteins)
RN  - 0 (Pregnancy-Specific beta 1-Glycoproteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (TGFB1 protein, human)
RN  - 0 (Transforming Growth Factor beta1)
RN  - 0 (VEGFA protein, human)
RN  - 0 (Vascular Endothelial Growth Factor A)
RN  - 144589-93-5 (Placenta Growth Factor)
SB  - IM
MH  - Endothelial Cells/metabolism
MH  - Female
MH  - Humans
MH  - Macrophages/metabolism
MH  - Mutagenesis, Site-Directed
MH  - *Neovascularization, Physiologic
MH  - Placenta/blood supply/*metabolism
MH  - Placenta Growth Factor
MH  - Placentation
MH  - Pregnancy
MH  - Pregnancy Proteins/metabolism
MH  - Pregnancy-Specific beta 1-Glycoproteins/genetics/*metabolism
MH  - Recombinant Proteins/metabolism
MH  - Transforming Growth Factor beta1/*metabolism
MH  - Trophoblasts/metabolism
MH  - Vascular Endothelial Growth Factor A/*metabolism
PMC - PMC2888962
EDAT- 2010/03/26 06:00
MHDA- 2010/10/28 06:00
PMCR- 2010/07/01
CRDT- 2010/03/26 06:00
PHST- 2010/03/26 06:00 [entrez]
PHST- 2010/03/26 06:00 [pubmed]
PHST- 2010/10/28 06:00 [medline]
PHST- 2010/07/01 00:00 [pmc-release]
AID - biolreprod.109.082412 [pii]
AID - 10.1095/biolreprod.109.082412 [doi]
PST - ppublish
SO  - Biol Reprod. 2010 Jul;83(1):27-35. doi: 10.1095/biolreprod.109.082412. Epub 2010 
      Mar 24.