Uterine and lung uteroglobins in the rabbit

Torkkeli, Tuula; Krusius, Tom; Jänne, Olli A.

doi:10.1016/0304-4165(78)90332-x

Cited by 45 publications

(12 citation statements)

References 30 publications

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“…Uteroglobin (UG) is a small secretory protein composed of two identical subunits held together by disulfide bridges which was first isolated from the rabbit endometrium where its gene is transcriptionally activated by progesterone in early pregnancy (see [1,2] for reviews). UG is also synthesized in other tissues under the control of different steroid hormones: glucocorticoids in lung [3,4], estrogens in the oviduct [5] and androgens in the epididymis [6]. The protein appears to be widely distributed among mammals.…”

Section: Introductionmentioning

confidence: 99%

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Binding of retinoids to uteroglobin

et al. 1994

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Uteroglobin, a progesterone-binding secretory protein, was shown to bind retinoic acid and retinol in a non-saturable manner, at least up to concentrations of retinoids of 20 PM. Binding is increased about IO-fold by previous reduction of uteroglobin with 10 mM dithothreitol and it is not affected by previous saturation of the progesterone binding site, suggesting different binding sites for the steroid and the retinoids. The results are discussed in relation to a possible physiological role for this protein.

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Section: Introductionmentioning

confidence: 99%

“…UG is also synthesized in other tissues under the control of different steroid hormones: glucocorticoids in lung [3,4], estrogens in the oviduct [5] and androgens in the epididymis [6]. The protein appears to be widely distributed among mammals.…”

Section: Introductionmentioning

confidence: 99%

Binding of retinoids to uteroglobin

et al. 1994

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“…Moreover, both proteins are synthesized as a larger precursor (pre-uteroglobin) containing a N-terminal additional peptide (Beato & Nieto, 1976;Bullock, 1977;Malsky et al, 1979;Savouret et al, 1980). However, the uteroglobin concentration in the lung does not seem to be regulated by ovarian hormones, but it appears to be controlled by glucocorticoids (Feigelson et al, 1977;Torkkeli et al, 1978). A subsequent report indicates that this control could be at a post-transcriptional level (Savouret et al, 1980).…”

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confidence: 99%

“…A uteroglobin-like protein was also found in other tissues of the rabbit, particularly in the lung (Noske & Feigelson, 1976). On the basis of immunological and chemical studies (Beato & Beier, 1978;Torkkeli et al, 1978), it appears that uterine and lung Abbreviations used: poly(A)+ mRNA, poly(A)-containing mRNA; SDS, sodium dodecyl sulphate. * To whom reprint requests should be addressed.…”

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confidence: 99%

Glucocorticoid and developmental regulation of uteroglobin synthesis in rabbit lung

Lombardero¹,

Nieto²

1981

Biochemical Journal

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The synthesis of uteroglobin in rabbit lung was studied after the administration of glucocorticoids to intact adult animals as well as during the late stages of rabbit development. The synthesis of uteroglobin was compared with levels of translatable uteroglobin mRNA in the lung. Uteroglobin synthesis was determined both by incorporation of [25S]methionine into the protein by lung explants incubated in vitro and by radioimmunoassay measurements of uteroglobin concentration in lung. Lung poly(A)-containing mRNA, isolated by oligo(dT)--cellulose chromatography, was translated in cell-free systems and the activity of uteroglobin mRNA was determined after immunoprecipitation. Dexamethasone administration increased about 2-fold the synthesis of lung uteroglobin compared with the controls. The effect of cortisol was more moderate. Both glucocorticoids did not affect the degradation rate of lung uteroglobin, but produced increases in the translatable levels of uteroglobin mRNA parallel to those observed for uteroglobin synthesis. During the late stages of rabbit development, both the synthesis of lung uteroglobin and the translatable levels of its mRNA increase in parallel about 12-fold in a biphasic fashion. A first increase occurred between 2 days before and 2 days after birth. Starting at 5 days of age, there was a second increase in both parameters, which at 12 days of age reached values close to those observed in adult rabbits. Our results suggest that the rate of lung uteroglobin synthesis could be mainly determined by the translatable levels of its mRNA.

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“…Uteroglobin expression in rabbits has been originally reported in the uterus during the preirnplantation phase { 10). More recently, the protein was also detected in oviduct (11), male genital organs {12), esophagus {13) and Jung {13, 14). In vitro, several distinct properties of uteroglobin have been described.…”

Section: Introductionmentioning

confidence: 97%

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

Wolf

Klug

Hackenberg³

et al. 1992

Hum Mol Genet

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Human and rat cDNAs to Clara CeU 10 kDa protein {CClO) have been previously isolated. Comparison of the amino acid sequences showed that CCIO is homologous to rabbit uteroglobin. Here we present further evidence that human CClO is the human COUnterpartor rabbit uteroglobin. We have isolated the gene and have mapped its genomic Jocalization to chromosome llq11-qter. Sequence anaJysis of the 5' -ßanking region reveals tbat 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 of0.74 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 bnplicated in progesteroDe regulation of rabbit uteroglobin gene expression in endometrium. Sequence alignment ortbis region on the nucleotide Ievel shows that only two weak progesterone receptor binding sites are partially conserved. In addition, close inspection or the human and rabbit promoters reveals that the estrogen responsive element and two recently identifled cis elements of the rabbit promoter located between -177 and -258 bp are also absent in the human uteroglobin promoter. Despite these difterences in the 5'-ßanking regions or the genes, we report that the human uteroglobin mRNA is expressed in a human ceU Hne of endometrial origin indicating that human uteroglobin is expressed in the uterus like its rabbit homologue. Thus, lt appears that human uteroglobin is not onJy a marker for lung Clara ceUs bot also an endometrial differentiation marker. Human uteroglobin cDNA or antibodies to the protein may be used to characterize endometrium derived tumors.

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Uterine and lung uteroglobins in the rabbit

Cited by 45 publications

References 30 publications

Binding of retinoids to uteroglobin

Binding of retinoids to uteroglobin

Glucocorticoid and developmental regulation of uteroglobin synthesis in rabbit lung

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

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