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PubMed2004

[Uteroglobin G38A polymorphism is associated with the progression of IgA nephropathy in Chinese patients].

OBJECTIVE: Uteroglobin is a multifunctional protein. Both uteroglobin gene knockout and antisense transgenic mouse models developed the pathological and clinical features of IgA nephropathy. Uteroglobin G38A polymorphism has been reported to be associated with the progression of IgA nephropathy in some Caucasian and Asian populations, but there are no documents on Chinese population. The present report was to investigate the associations of uteroglobin G38A polymorphism with the development and progression of IgA nephropathy in Chinese patients. METHODS: Three hundred patients with biopsy proven IgA nephropathy were identified from Renal Disease database. Ninety-three patients had been followed-up for 2-6 years. 145 healthy donors served as normal controls. Genomic DNAs were extracted from peripheral blood leucocytes. The uteroglobin G38A polymorphism was determined by PCR-RFLP. Uteroglobin G38A genotype and allele frequency were compared between patients with IgA nephropathy and normal controls. In addition, associations of G38A polymorphism with blood pressure, hematuria, proteinuria, pathological lesions and prognosis of renal function were analyzed in patients with IgA nephropathy. RESULTS: Distribution of uteroglobin G38A polymorphism in patients with IgA nephropathy (38AA: 13.2%; 38AG: 57.6%; 38GG: 30.2%) and normal controls (38AA: 18.2%; 38AG: 60%; 38GG: 21.8%; P > 0.05) showed no difference. But patients with the 38AA genotype showed a higher odds ratio for progression of renal function (OR = 2.37, 95% CI = 1.12-5.01) as compared to patients with the 38AG/GG genotype. CONCLUSION: Uteroglobin G38A polymorphism had no association with the development of IgA nephropathy, but the homogeneous 38AA genotype maybe one of the genetic markers for disease progression in Chinese IgA nephropathy.

Adult↗
PubMed1979

Progesterone-induced secretory protein. NH2-Terminal sequence of pre-uteroglobin.

Uteroglobin is a protein secreted by the rabbit uterus in response to progesterone. In cell-free translation systems, the mRNA for uteroglobin codes for a protein larger in size than the secreted protein. To investigate the relationship between these two forms, the NH2-terminal sequences of pre-uteroglobin and of uteroglobin have been determined. Uteroglobin was purified from rabbit uterine flushings and pre-uteroglobin was obtained by immunoprecipitation of the products of translation of poly(A)-rich endometrial RNA in the wheat germ system in the presence of single or multiple radioactive amino acids. Sequencing was performed by automated Edman degradation and the residue at each cycle was identified by chromatography. The larger size of pre-uteroglobin is accounted for by a 21-amino-acid leader sequence, containing 15 hydrophobic residues, at the NH2 terminus. The sequence Thr-Leu-Ala-Leu occurs twice in the leader region. In common with other secretory proteins, the transient hydrophobic extension at the NH2 terminus of pre-uteroglobin may function to assist transfer of the nascent peptide into the lumen of the endoplasmic reticulum, as proposed in the "signal" hypothesis.

Amino Acid Sequence↗
PubMed1984

Uteroglobin mRNA from the lung of the hare (Lepus capensis): cell-free translation and properties.

Poly(A)-containing RNA was obtained from the lung of hares (Lepus capensis) and uteroglobin mRNA was characterized by cell-free translation and molecular hybridization to a rabbit uteroglobin cDNA probe. In the cell-free system, hare uteroglobin mRNA was preferentially translated as compared to the whole lung mRNA and it directed the synthesis of a precursor, preuteroglobin, containing about twenty additional amino acids. Hare uteroglobin mRNA was about 40 nucleotides larger than the homologous rabbit one, as analyzed by electrophoresis on agarose gel. Thermal stability of the hybrids formed between rabbit or hare uteroglobin mRNAs and the rabbit cDNA probe indicated differences in the nucleotide sequence of both mRNAs. The levels of uteroglobin mRNA and uteroglobin synthesis in lung are about two-fold higher in hare than in rabbit lung.

Animals↗
PubMed1988

Expression of a uteroglobin-like protein in human prostate.

Phospholipase A2 (PLA2) is a key enzyme that initiates the arachidonic acid cascade responsible for the synthesis of prostaglandins and leukotrienes, compounds well known for their inflammatory properties. Inhibition of this enzyme may modulate prostaglandin and leukotriene tissue levels. Uteroglobin is a potent PLA2 inhibitor found in rabbit uterus, prostate, seminal vesicle, and tracheobronchial tree. Tissue from ten human patients undergoing prostatectomy was examined for presence of a uteroglobin-like protein. Seven patients underwent transurethral resection and three had an open prostatectomy. Preoperative diagnosis in nine of the 10 patients was benign prostatic hypertrophy. One suspected, poorly differentiated, adenocarcinoma was confirmed and one unsuspected, well differentiated, adenocarcinoma was discovered. Specimens were submitted for Western blot, electron microscopy with immunogold staining, radioimmunoassay, and immunofluorescence. Six patients had evidence of uteroglobin-like protein, three with high levels (greater than or equal to 1000 pg./mg. protein), two with moderate levels (75 to 250 pg.), one with a low level (less than or equal to 75 pg.). Uteroglobin-like protein was present in all three patients who underwent open prostatectomy and in three of the seven patients with transurethral resections. The uteroglobin-like protein level was 2.5 to five times greater in both prostatic utricle specimens. All four assays corroborated these results. Because rabbit uteroglobin coats sperm and masks spermatic antigenicity in the rabbit female genital tract, this report of biochemical and immunological evidence for uteroglobin-like protein in the human prostate may have implications for human male fertility.

Adenocarcinoma↗
PubMed2002

Role of uteroglobin G38A polymorphism in the progression of IgA nephropathy in Japanese patients.

BACKGROUND: Uteroglobin is a multifunctional protein and both its gene knockout and antisense transgenic mouse models develop the pathological and clinical features of IgA nephropathy. A genetic polymorphism in uteroglobin has been reported to be associated with progression of IgA nephropathy in a Caucasian population, but the findings remain controversial. METHODS: Genomic DNA was isolated from 595 individuals including 239 patients with IgAN, 160 patients with glomerulonephritis distinct from IgAN, and 196 healthy controls. The uteroglobin G38A genotype was determined by PCR-RFLP with Sau96I. To examine the possible association of uteroglobin gene polymorphism in the patients with and without IgAN, the uteroglobin genotype and allele frequency were compared between the two groups. In addition, associations between the polymorphism and blood pressure, proteinuria and prognosis of renal function were analyzed in the patients with IgAN to investigate the role of this gene polymorphism in the risk of progressive renal dysfunction in IgAN patients. RESULTS: The Cox proportional hazard regression model revealed that hypertension and proteinuria at the time of renal biopsy were independent risk factors for poor renal survival. Uteroglobin genotype was not significantly associated with the renal survival rate. However, in the patients with heavy proteinuria (more than 2 g/day) or in those with hypertension at the time of renal biopsy, the renal survival of patients with the GG genotype was significantly worse than the other genotypes. CONCLUSION: Uteroglobin GG genotype may be a genetic marker for rapid disease progression to end-stage renal failure, especially in the IgAN patients with heavy proteinuria or high blood pressure.

Adult↗
PubMed1992

Human CC10, the homologue of rabbit uteroglobin: genomic cloning, chromosomal localization and expression in endometrial cell lines.

Human and rat cDNAs to Clara Cell 10 kDa protein (CC10) have been previously isolated. Comparison of the amino acid sequences showed that CC10 is homologous to rabbit uteroglobin. Here we present further evidence that human CC10 is the human counterpart of rabbit uteroglobin. We have isolated the gene and have mapped its genomic localization to chromosome 11q11-qter. Sequence analysis of the 5'-flanking region reveals that the homology between the human and the rabbit gene starts at the first exon/intron boundary and extends up to -1.4 kb. A second region of 0.74 kb from -1.77 to -2.51 kb in the human 5'-flanking gene region is homologous to rabbit sequences that include four progesterone receptor binding sites which have been implicated in progesterone regulation of rabbit uteroglobin gene expression in endometrium. Sequence alignment of this region on the nucleotide level shows that only two weak progesterone receptor binding sites are partially conserved. In addition, close inspection of the human and rabbit promoters reveals that the estrogen responsive element and two recently identified cis elements of the rabbit promoter located between -177 and -258 bp are also absent in the human uteroglobin promoter. Despite these differences in the 5'-flanking regions of the genes, we report that the human uteroglobin mRNA is expressed in a human cell line of endometrial origin indicating that human uteroglobin is expressed in the uterus like its rabbit homologue. Thus, it appears that human uteroglobin is not only a marker for lung Clara cells but also an endometrial differentiation marker.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenocarcinoma↗
PubMed1986

Uteroglobin messenger ribonucleic acid: localization in rabbit uterus and lung by in situ hybridization.

The messenger RNA (mRNA) coding for uteroglobin has been localized in the rabbit uterus and lung by in situ hybridization. Tissue sections fixed in ethanol-acetic acid were hybridized to the cloned complementary DNA probe labeled with tritium. The hybridization sites were detected by radioautography. Control experiments using [3H]pBR322 DNA demonstrated the specificity of the observed labeling. In the lung, uteroglobin mRNA, present in small concentrations, could be clearly visualized only after background was decreased by incubation of sections with S1 nuclease. In pregnant rabbit uterine horns, uteroglobin mRNA, visualized by silver grains, was found in the endometrial epithelium. The concentration was greater in the cells of glandular epithelium than in the cells of surface epithelium. Specific and intense labeling was spread through the cytoplasm. Practically all epithelial cells contained uteroglobin mRNA. Hybridization was very weak in the uterine epithelial cells of the nonpregnant rabbit. In the lung, a high degree of labeling occurred on the ciliated and bronchiolar cells of the epithelium of bronchi and bronchioles whereas the goblet cells remained unlabeled. Certain cells lining alveolar ducts and alveoli in the pulmonary parenchyma also showed a slight labeling. No differences in the labeling were observed in the lung of either pregnant or non-pregnant animals. There are several differences in the intensity and distribution of labeling between our hybridization experiments and previous studies involving immunocytochemical detection of uteroglobin protein. The latter technique thus probably not only reflects the pattern of synthesis of the protein but also depends on uteroglobin retention in the cells. Moreover, no evidence was found to bear out the hypothesis that some endometrial cells which contain uteroglobin do not synthesize this protein but take it up from endometrial fluid.

Animals↗
PubMed1976

Interaction of uteroglobin with progesterone, 5alphapregnane-3,20-dione and estrogens.

Uteroglobin was obtained from 5 day pregnant rabbits and purified to homogeneity by Sephadex G 75 and DEAE-cellulose chromatographies. Progesterone binding to uteroglobin was decreased by lyophilization and enhanced by SH-reducing agents. Dithiothreitol was more effective than dithioerythritol, and beta-mercaptoethanol was only active at 25 to 100 mM concentrations. SH-blocking agents (iodoacetate, iodoacetamide, phydroxymercuribenzoate and, dithiobisnitrobenzoic acid) inhibited binding. In the absence of SH-reducing agents only one in every 500 uteroglobin molecules bound the hormone, whereas under optimal conditions (20 mM dithiothreitol) one in every two molecules bound progesterone. There was no significant difference in equilibrium dissociation constants under these two conditions. Uteroglobin had a relatively high affinity for progesterone (KD=4.1 X 10(-7)M) but a threefold higher affinity for 5alpha-pregnane-3,20-dione (KD=1.3 X 10(-7)M). Estradiol was bound but non-specifically with a very low affinity, and its binding was not enhanced by SH-reducing agents. Hormonal specificity of binding to uteroglobin was different from that of binding to rabbit uterine progesterone receptor. Various synthetic progestagens (chlormadinone acetate, norethisterone, R5020) were bound to the latter but not to the former protein. Diethylstilbestrol had some affinity (15% of that of progesterone) for uteroglobin and no affinity for the progesterone receptor. Uteroglobin incubated in the presence or absence of cofactors (NADH and NADPH) with or without dithiothreitol did not metabolize progesterone.

Androgens↗
PubMed1990

The uteroglobin promoter contains a noncanonical estrogen responsive element.

Uteroglobin is expressed in various tissues of the rabbit under complex hormonal control. In the endometrium the uteroglobin gene is transcribed only in epithelial cells after administration of ovarian hormones. In this paper we demonstrate that within the promoter region of the rabbit uteroglobin gene, there is a functional estrogen-responsive element (ERE) located between -265 and -252. Hybrid constructions containing sequences of the uteroglobin promoter up to -299, linked to the chloramphenicol acetyltransferase gene of E. coli respond to estrogens in gene transfer experiments, whereas a deletion that removes half of the ERE does not. A synthetic oligonucleotide corresponding to the putative ERE is able to confer estrogen inducibility to an otherwise unresponsive promoter. Binding experiments with purified estrogen receptor from calf uterus reveal a DNase-I footprint over the ERE. Within this protected region six guanine residues that have been shown to be contacted by the receptor in other EREs are protected against methylation by dimethylsulfate in the presence of the estrogen receptor. We compare this ERE with the vitellogenin A2 ERE from Xenopus and find that the relative affinity of the uteroglobin ERE is slightly lower than that of the vitellogenin ERE. Thus, this uteroglobin ERE could be involved in physiological regulation of uteroglobin expression in the genital tract.

Animals↗
PubMed2001

Adenoviral mediated uteroglobin gene transfer to the adventitia reduces arterial intimal hyperplasia.

PURPOSE: The aim of this study was to investigate the feasibility of gene transfer of uteroglobin, a potent anti-inflammatory and immunomodulatory agent, via adenoviral mediated gene transfer to the adventitia in the mouse carotid ligation injury model and also to investigate the efficacy of uteroglobin in reducing neointimal hyperplasia. METHODS: Forty-five C57bl/6NHSD mice were anesthetized and left common carotid artery ligation was performed. Adenoviral vector encoding the uteroglobin gene (Ad.UG; 15 microl of 1.35 x 10(11) pfu/mL) was applied to the adventitia of the injured artery in 16 mice. In our control groups, 16 mice received adenoviral vector encoding the beta-galactosidase reporter gene (Ad.lacZ; 15 microl of 1.0 x 10(11) pfu/mL) and 13 mice received PBS only. Six mice from each group were sacrificed at 4 days for carotid artery protein extraction and Western blot analysis. The remainder were harvested at 30 days for histologic and morphometric analysis. The intima/media area ratios were calculated for each artery. The results were analyzed and compared using ANOVA and Bonferroni/Dunn post hoc testing. RESULTS: Two mice from the LacZ group and one from the PBS group died before the 30-day endpoint. Uteroglobin expression was demonstrated in the Ad.UG treated arteries by Western blot analysis. Morphometric analysis demonstrated a statistically significant reduction in the intima/media area ratio of Ad.UG treated carotids compared to controls. There was a reduction of intima/media ratio with Ad. UG treatment of 68% compared to Ad.lacZ treatment (P < 0.0001) and 62% compared to PBS treatment (P = 0.0006). There was no statistical difference between the control groups. CONCLUSION: Adenoviral mediated gene transfer via the adventitia is an effective mode of gene delivery. Adventitial uteroglobin gene transfer using an adenoviral vector induces uteroglobin protein production and significantly reduces neointimal hyperplasia in the mouse carotid ligation injury model.

Adenoviridae↗
PubMed1978

Uteroglobin-like antigen in the pulmonary epithelium and secretion of the lung.

The immunological identity of a uteroglobin-like protein, occurring in respiratory tract secretions and tissue, with uteroglobin from rabbit endometrial secretion is demonstrated. A uteroglobin-like antigen has been localized in bronchial epithelial cells and in bronchioles by immunofluorescence. This secretory protein is, in contrast to the authentic uteroglobin, hormone-independent, as far as estrogens and progesterone are concerned. The possible significance of comparative studies on uteroglobin and the uteroglobin-like antigen is discussed, taking into account cytological, endocrinological, and molecularbiological aspects.

Animals↗
PubMedDate not supplied

Ultrastructural and kinetic studies on uteroglobin secretion in the uterus and oviduct of the pseudopregnant rabbit.

The intracellular localization of uteroglobin, a progesterone-induced protein, was studied in uterus and oviduct by means of immunoelectron microscopy with the protein A-gold technique. In the uterus, uteroglobin was synthesized in the columnar epithelium of the endometrium where most of the cells were immunoreactive. The protein was localized mainly in small secretory granules which were seen in the process of release into the uterine lumen. The luminal microvilli were also heavily stained. In the oviduct, the secretory cells contained large immunoreactive granules at the apical zone, some of which were observed while discharging into the lumen. Within these secretory granules, uteroglobin accumulated particularly in lens-shaped patches at the periphery of the granules. In vitro kinetic studies on the secretion of newly synthesized uteroglobin indicated that the ability to store uteroglobin is greater in the oviduct than in the uterus; however, the rate of uteroglobin secretion is greater in the uterus than in the oviduct. Thus, there appears to be a good correlation between the microscopic and the functional observations.

Animals↗
PubMed1988

Inhibition of phagocyte chemotaxis by uteroglobin, an inhibitor of blastocyst rejection.

Uteroglobin, a steroid-dependent secretory protein first discovered in the rabbit uterus during early pregnancy, is a potent phospholipase A2 inhibitor. We found that uteroglobin also inhibited human and rabbit phagocyte chemotaxis in response to formyl peptide attractants in a dose-dependent manner. Half-maximal inhibition was at 1.2 microM. Uteroglobin did not compete with a formyl peptide for its receptor but inhibited internalization of radiolabeled formyl peptide. Uteroglobin appears to inhibit chemotaxis by a mechanism different from that of dansylcadaverine, a well studied inhibitor of endocytosis. Unlike dansylcadaverine, uteroglobin did not have any effect upon the synthesis of phosphatidylcholine or phosphatidylinositol. It is suggested that uteroglobin may protect trophoblastic cells from the defense system of the host not only by binding to antigenic determinants of embryonic cells but also by impairing migration of phagocytes, one of the primary components of the immune defense system. These results may explain why embryonic cells do not elicit an inflammatory response in the uterine endometrium during pregnancy.

Animals↗
PubMed2006

Association of uteroglobin G38A polymorphism with IgA nephropathy: a meta-analysis.

Both uteroglobin knockout and antisense transgenic mice develop pathological and clinical features similar to immunoglobulin A (IgA) nephropathy. However, several association studies of uteroglobin G38A polymorphism and IgA nephropathy showed controversial findings. We used meta-analysis to assess the impact of the uteroglobin G38A polymorphism on susceptibility to and progression of IgA nephropathy. Six studies involving uteroglobin G38A genotyping of 930 patients with IgA nephropathy and 768 healthy controls were included. No significant publication bias was found (Egger's linear regression, P = 0.763; 95% confidence interval [CI], -0.610 to 0.476). All control samples were in Hardy-Weinberg proportion. No association between the AA genotype and risk for IgA nephropathy relative to both other genotypes (odds ratio [OR], 1.05; 95% CI, 0.71 to 1.54) or A allele and risk for IgA nephropathy (OR, 0.96; 95% CI, 0.84 to 1.11) were shown in the total meta-analysis. In both Asian and European subgroups, the overall effect of the AA genotype and A allele also showed no significant difference. There also was no significant association between uteroglobin AA genotype or A allele and IgA nephropathy progression (OR, 3.62; 95% CI, 0.59 to 22.34; OR, 2.19, 95% CI, 0.37 to 13.14, respectively). We suggest that uteroglobin G38A polymorphism is not related to the development and progression of IgA nephropathy.

Genetic Predisposition to Disease↗
PubMed2000

Adenoviral-mediated uteroglobin gene transfer inhibits neointimal hyperplasia after balloon injury in the rat carotid artery.

OBJECTIVE: Uteroglobin is a protein with potent anti-inflammatory and immunomodulatory effects. We hypothesize that induction of uteroglobin expression in the artery wall by local adenoviral gene transfer will decrease neointimal hyperplasia in the rat carotid artery after balloon injury. METHODS: Seven male Sprague-Dawley rats underwent balloon injury of the common carotid artery. After the injury, with flow occluded, the artery was instilled with 50 microL of the adenoviral vector encoding uteroglobin gene (Ad.UG) at a concentration of 1.35 x 10(11) pfu/mL (n = 7) or 0.68 x 10(11) pfu/mL (n = 7) (n = 7). Control animals were similarly treated: either an adenovirus encoding for beta-galactosidase gene (Ad.LacZ) at 1 x 10(11) pfu/mL (n = 7) or the phosphate-buffered saline (PBS) vehicle (n = 6) was used. The solution was allowed to dwell for 20 minutes. The rats were humanely killed after 14 days by perfusion fixation, and the carotid arteries were sectioned for analysis with computerized planimetry. The intima-media area ratios were calculated for each artery and compared with analysis of variance with Bonferroni/Dunn post hoc testing. One additional rat from the PBS, Ad.LacZ, and Ad.UG (1.35 x 10(11) pfu/mL) groups was humanely killed 4 days after treatment for carotid artery protein extraction and Western blotting. RESULTS: Uteroglobin protein production was confirmed in the Ad.UG-treated arteries with Western blotting. Morphometric analysis showed that the Ad.UG group at 1.35 x 10(11) pfu/mL had a significantly lower intima-media area ratio than both the Ad.LacZ (P =.002) and PBS (P =.004) controls. The Ad.UG group at 0.68 x 10(11) pfu/mL was also significantly different from the Ad. LacZ (P =.003) and PBS (P =.006) controls. There was no statistical difference between the two control groups or between the two Ad.UG groups. CONCLUSION: Adenoviral gene transfer of uteroglobin, delivered intraluminally after arterial injury causes the production of uteroglobin protein and has an inhibitory effect on neointimal accumulation in the rat model.

Adenoviridae↗
PubMed1981

Hormonally regulated mammalian gene expression: steady-state level and nucleotide sequence of rabbit uteroglobin mRNA.

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.

Amino Acid Sequence↗
PubMed1990

Tissue-specific expression, hormonal regulation and 5'-flanking gene region of the rat Clara cell 10 kDa protein: comparison to rabbit uteroglobin.

The amino acid sequence of rat Clara Cell 10 kDa secretory protein (CC10) shows 55% identity to rabbit uteroglobin. In order to define the relationship between rat CC10 and rabbit uteroglobin in detail, the tissue-specific expression and hormonal regulation of rat CC10 mRNA was analyzed. We report that like rabbit uteroglobin, rat CC10 mRNA is expressed in lung and esophagus, as well as in uteri of estrogen- and progesterone-treated females. Expression of CC10 mRNA in lung is regulated by glucocorticoids. The similarity in expression pattern of rat CC10 mRNA and rabbit uteroglobin mRNA is reflected by a striking similarity in the 5'-flanking regions of the two genes. Despite this overall similarity, two regions of 0.3 kb and 2.1 kb are absent in the rat CC10 upstream gene region. The larger region includes a cluster of hormone receptor binding sites, believed to be responsible for differential regulation of rabbit uteroglobin by glucocorticoids and progesterone. Thus, while the sequence identities in the coding and 5'-flanking regions point towards a common ancestor for the uteroglobin and CC10 gene, later events (deletions/insertions) might have caused species-specific differences in their regulation.

Animals↗
PubMed1989

Recombinant rabbit uteroglobin expressed at high levels in E. coli forms stable dimers and binds progesterone.

In order to express uteroglobin in Escherichia coli we have constructed a DNA coding for complete mature rabbit uteroglobin by fusing genomic sequences from the second exon of the gene to an incomplete cDNA. This DNA was inserted into various positions of the polylinker cloning region of pDS expression vectors and the uteroglobin gene was expressed in E. coli by IPTG induction. Four different uteroglobin-derived proteins were produced containing 1, 3, 5 and 7 more N-terminal amino acids than the naturally occurring mature protein. The yield of soluble protein strongly increased with increasing length of the N-terminal additions. Protein and RNA analysis showed that this variation is most likely due to progressively higher translation efficiencies of the larger recombinants. UG7, the most efficiently synthesized recombinant protein, carrying seven additional N-terminal amino acids, was purified and further characterized. Like natural uteroglobin, UG7 forms a dimer and binds progesterone with an affinity indistinguishable to the natural protein. This bacterially produced protein can be used for detailed structure-function investigations of uteroglobin.

Animals↗