Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P11684 (Uteroglobin)
 114 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Uteroglobin is a protein that is synthesized in large quantities by the rabbit uterine endometrial cells and secreted into the uterine lumen around the time of implantation of the developing blastocysts. The protein is also synthesized constitutively at a low level in the lung. In the uterus, synthesis of the protein is induced by progesterone but repressed by estradiol; whereas in the lung, it is not hormonally responsive. Using a full-length cDNA clone, we have established the nucleotide sequence of uteroglobin mRNA and have determined its levels in uterus and lung during early pregnancy. The clone, pUG617, contains all but 24 nucleotides at the 5' untranslated region of the structural gene. To establish the full mRNA sequence, we isolated a 5' end-labeled DNA fragment from pUG617 and extended its length using reverse transcriptase after hybridization with uterine poly(A)-containing RNA. The 5'-terminal sequence of uteroglobin mRNA was established by sequencing the extended DNA fragment. The nucleotide sequence of the peptide-coding portion of the gene has resolved some previously reported discrepancies in the amino acid sequence of the mature protein and those in the signal peptide. By comparison of sequences with a partial uteroglobin cDNA clone isolated by another laboratory, a polymorphic nucleotide at position 246 of the gene has been identified, where a G-A transition has caused an amino acid substitution from aspartic acid to asparagine at residue 46 of the mature protein. Analysis of steady-state RNA levels in the uterus has shown that the induction and repression of uteroglobin synthesis during early pregnancy is the result of accumulation and depletion of its mRNA, respectively. During the same period in the lung, no consistent changes in uteroglobin mRNA level were evident, reflecting the constitutive levels of the protein in this tissue.
 ...
PMID:Hormonally regulated mammalian gene expression: steady-state level and nucleotide sequence of rabbit uteroglobin mRNA. 629 63

Uteroglobin (UG) is an anti-inflammatory, secreted protein with soluble phospholipase A2 (sPLA2)-inhibitory activity. However, the mechanism by which UG inhibits sPLA2 activity is unknown. UG is a homodimer in which each of the 70-amino acid subunits forms four alpha-helices. We previously reported that sPLA2-inhibitory activity of UG may reside in a segment of alpha-helix 3 that is exposed to the solvent. In addition, it has been suggested that UG may inhibit sPLA2 activity by binding and sequestering Ca++, essential for sPLA2 activation. By site-specific mutation, we demonstrate here that Lys 43 Glu, Asp 46 Lys or a combination of the two mutations in the full-length, recombinant human UG (rhUG) abrogates its sPLA2-inhibitory activity. We demonstrate further that recombinant UG does not bind Ca++ although when it is expressed with histidine-tag (H-tag) it is capable of binding Ca++. Taken together our results show that: (i) Lys 43 and Asp 46 in rhUG are critical residues for the sPLA2-inhibitory activity of UG and (ii) Ca++-sequestration by rhUG is not likely to be one of the mechanisms responsible for its sPLA2-inhibitory activity.
 ...
PMID:Lys 43 and Asp 46 in alpha-helix 3 of uteroglobin are essential for its phospholipase A2 inhibitory activity. 1212 76

Between the 3rd and 6th day post coitum the dry substance of uterine fluid contains nearly 60% peptide chains, on the 6th day 19 h p.c. only 35%. The remaining 40 and 65% resp. consist mainly of carbohydrates (cf. III.1). By means of disc electrophoresis, thin layer chromatography following hydrolysis and molecular sieve chromatography, we were able to characterize 4 uterine specific proteins, 2 of which are carbohydrate rich glycoproteins. Their relative concentrations were determined between 0 and 8 day p.c. (of. III.2): Glycoprotein I can already be found during oestrus. Its concentration increases slightly from the 3rd to the 5th day p.c., more rapidly up to the 6th day 6 h p.c., and decreases later (of.III.2b). The molecular weight is estimated to be around 50,000 (cf.III.4). Postalbumin as well as Uteroglobin can be found shortly after ovulation. Its concentration stays nearly constant between 3rd and 6th day p.c., and decreases during the 6th day p.c. (of.III.2b). Its molecular weight is in the same range as that of Uteroglobin, nearly 30,000 (of.III.4. Uteroglobin is most probably free of carbohydrates. Its concentration increases rapidly between 16 and 40 h p.c., slightly until the 5th day p.c., and decreases later (cf.III.2b). At 6th day p.c. about 50% of the peptide chains of uterine fluid are Uteroglobin (cf.III.2.g). Glycoprotein II is not secreted before the 6th day p.c. It has a comparativly high content of galactose (cf.III.3.d). Its concentration increases rapidly during the 6th day p.c. (cf.III.2.b). The moleculare weight is higher than 70,000 (cf.III. 4).These proteins and glycoproteins have also been found inblastocoelic fluid after the 5th day p.c. (cf.III.2.c).Aftersuperovulation induced by hormones, and natural mating, the pregnancy specific protein pattern is not fully developed (cf.III.2.d). Inpseudopregnancy, triggered by mating with vasectomized males, the same proteins as in normal pregnancy were found from the 6th day 6 h to the 6th day 19 h p.c. If no blastocysts are implanted, the protein pattern of the 6th day 19 h p.c. persists nearly unchanged until the 9th day p.c. (cf.III.2.e).Duringimplantation uterus and blastocyst lumens are filled with serum proteins, which tend to cover up the secretion proteins (cf.III.2.f).9 constituents of carbohydrates could be identified in uterine fluid. There was no evidence for freemonohexoses, particularly free glucose. Theoligomere carbohydrates were free or bound to proteins (cf.III.3.). We were able to separate Glycoprotein I, Glycoprotein II, Albumin + Uteroglobin with Sephadex G 150 and G 75 SF (cf.III.4).21 freeamino acids were found in uterine and blastocoelic fluid by means of thin layer chromatography. The concentrations of amino acids in uterine fluid were comparable to those of serum. The dry substance of uterine fluid contains more glycine, alanine, glutamic acid and aspartic acid than that of serum (cf.III.5).The possible role of amino acids in thenutrition of the blastocyst and the possible influence of uterine specific proteins and glycoproteins onnutrition and morphogenesis of the rabbit embryo were discussed.
 ...
PMID:[Studies of uterine specific glycoproteins during early pregnancy of the rabbitOryctolagus cuniculus]. 2830 64