title: Regional distribution and hormonal control of estrogen-dependent oviduct-specific glycoprotein messenger ribonucleic acid in the baboon (Papio anubis).
abstract: Our objective in this study was to complete the sequence of the baboon oviductal glycoprotein, examine the hormonal regulation of the oviductal glycoprotein mRNA, and determine whether there was a regional variation within the oviduct in the level of oviductal glycoprotein mRNA expression. Finally, because of the structural similarity of the amino terminal end of the oviductal glycoprotein to chitinases, we sought to determine whether the oviductal glycoprotein functions as a glycosyl hydrolase. The total transcript length of the baboon oviductal glycoprotein was determined to be 2228 nucleotides in length plus a poly(A) tail. The largest open reading frame was 623 amino acids, which would produce a protein of 69.3 kDa. The first 420 amino acids were highly homologous to the amino acid sequence of other oviductal glycoproteins, but the remainder of the sequence differed considerably from that of all other species except the human. Although the N-terminal region exhibited sequence similarity to chitinases, the oviductal glycoprotein did not exhibit any activity towards typical chitinase substrates. The oviductal glycoprotein mRNA levels were elevated to approximately the same extent in the fimbria, ampulla, and isthmus of the oviduct after estradiol treatment and in the late follicular stage of the menstrual cycle. The oviductal glycoprotein mRNA levels were lower in the early follicular stage and early luteal stage and were not detectable in the late luteal stage or in progesterone-treated baboons. These results indicate that the oviductal glycoprotein mRNA is induced by estradiol and is present at the highest levels at the time of fertilization. Although there is structural homology with chitinases, no such glycosyl hydrolase activity could be detected. However, the common structure of the N-terminal region of the oviductal glycoproteins implies that it has the same, as yet unknown, function in all species.
authors.affiliation: Department of Physiology and Biophysics, University of Illinois at Chicago 60612, USA. rcjaffe@uic.edu
authors.forename: R C
authors.initials: RC
authors.lastname: Jaffe
authors.forename: E B
authors.initials: EB
authors.lastname: Arias
authors.forename: M B
authors.initials: MB
authors.lastname: O'Day-Bowman
authors.forename: K M
authors.initials: KM
authors.lastname: Donnelly
authors.forename: P A
authors.initials: PA
authors.lastname: Mavrogianis
authors.forename: H G
authors.initials: HG
authors.lastname: Verhage
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry; D004958:Estradiol / Q000494:pharmacology; D005187:Fallopian Tubes / Q000737:chemistry*; D005260:Female; D005786:Gene Expression Regulation / Q000187:drug effects*; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics*; D006026:Glycoside Hydrolases / Q000032:analysis / Q000378:metabolism; D006728:Hormones / Q000494:pharmacology*; D006801:Humans; D007163:Immunosorbent Techniques; D008969:Molecular Sequence Data; D010215:Papio; D012333:RNA, Messenger / Q000032:analysis* / Q000378:metabolism*
chemical_list: D018076:DNA, Complementary; D006023:Glycoproteins; D006728:Hormones; C091468:OVGP1 protein, human; D012333:RNA, Messenger; D004958:Estradiol; D006026:Glycoside Hydrolases