Article (Scientific journals)
The gene encoding bovine pregnancy-associated glycoprotein-1, an inactive member of the aspartic proteinase family
Xie, S.; Green, J.; Beckers, Jean-François et al.
1995In Gene, 159 (2), p. 193-197
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Keywords :
Binucleate cell; Gene expression; Gene structure
Abstract :
[en] Bovine pregnancy-associated glycoprotein 1 (bPAG1) is a member of the aspartic proteinase family. It becomes detectable in maternal serum soon after implantation and is produced specifically in the invasive binucleate cells of the placenta. As a result of a key mutation within its catalytic center, bPAG1 appears to be proteolytically inactive. Its gene consists of nine exons (size range 99-281 bp) and eight introns (87-1800 bp) organized in a manner very similar to those of proteolytically active mammalian aspartic proteinases. The transcription start point (tsp) is located 53 or 54 bp upstream from the start codon (ATG) and 19 bp downstream from a 5'-TATATAA sequence. Southern blot analyses have indicated the presence of two bPAG1 genes. By screening with an antiserum raised against bPAG1, a less common cDNA with 91% sequence identity to the bPAG1 transcript has been isolated from a placental cDNA library and presumably represents the second gene. At least eight other genes with sequences that hybridize relatively weakly to the bPAG1 probe are present in the bovine genome. Despite the similarities in the transcribed portion of the genes encoding PAG1, pepsinogen and other mammalian aspartic proteinases, the sequences upstream from the tsp of bPAG1 are unique.
Disciplines :
Veterinary medicine & animal health
Author, co-author :
Xie, S.
Green, J.
Beckers, Jean-François  ;  Université de Liège - ULiège > Département de sciences fonctionnelles > Physiologie de la reproduction
Roberts, R. M.
Language :
English
Title :
The gene encoding bovine pregnancy-associated glycoprotein-1, an inactive member of the aspartic proteinase family
Publication date :
July 1995
Journal title :
Gene
ISSN :
0378-1119
eISSN :
1879-0038
Publisher :
Elsevier, Netherlands
Volume :
159
Issue :
2
Pages :
193-197
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 03 March 2009

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