Prolactin enhances uteroglobin gene expression by uteri of immature rabbits

Randall, Gary W.; Daniel, J. C.; Chilton, Beverly S.

doi:10.1530/jrf.0.0910249

Cited by 40 publications

(22 citation statements)

References 8 publications

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“…Moreover, a polypeptide hormone, prolactin, appears to enhance further steroid-induced UG gene-expression www.academicpress.com BBRC q Abbreviations: rhUG, recombinant human uteroglobin; sPLA 2 , soluble phospholipase A 2 ; DTNB, 5,5 0 -dithiobis-nitrobenzoate; IFNc, interferon-c; H-tag, histidine-tag; AA, arachidonic acid; NMR, nuclear magnetic resonance. [16][17][18][19]. Recently, a pro-inflammatory cytokine, interferon-c (IFN-c), was found to have a stimulatory effect on UG production in the murine lungs [20] and an IFNc-response element in the 5 0 -promoter region of the mouse UG gene has been identified [21].…”

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confidence: 99%

Lys 43 and Asp 46 in α-helix 3 of uteroglobin are essential for its phospholipase A2 inhibitory activity

Chowdhury¹,

Mantile-Selvaggi²,

Miele³

et al. 2002

Biochemical and Biophysical Research Communications

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Uteroglobin (UG) is an anti-inflammatory, secreted protein with soluble phospholipase A 2 (sPLA 2 )-inhibitory activity. However, the mechanism by which UG inhibits sPLA 2 activity is unknown. UG is a homodimer in which each of the 70-amino acid subunits forms four a-helices. We previously reported that sPLA 2 -inhibitory activity of UG may reside in a segment of a-helix 3 that is exposed to the solvent. In addition, it has been suggested that UG may inhibit sPLA 2 activity by binding and sequestering Ca þþ , essential for sPLA 2 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 sPLA 2 -inhibitory activity. We demonstrate further that recombinant UG does not bind Ca þþ although when it is expressed with histidine-tag (H-tag) it is capable of binding Ca þþ . Taken together our results show that: (i) Lys 43 and Asp 46 in rhUG are critical residues for the sPLA 2 -inhibitory activity of UG and (ii) Ca þþ -sequestration by rhUG is not likely to be one of the mechanisms responsible for its sPLA 2 -inhibitory activity. Ó 2002 Elsevier Science (USA). All rights reserved.

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confidence: 99%

Lys 43 and Asp 46 in α-helix 3 of uteroglobin are essential for its phospholipase A2 inhibitory activity

Chowdhury¹,

Mantile-Selvaggi²,

Miele³

et al. 2002

Biochemical and Biophysical Research Communications

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“…However, it is now clear that nonsteroid hormones, such as prolactin, may also enhance progesterone-induced expression of the UG gene (28,29,59,60). Recent reports indicate that this effect of prolactin involves novel response elements in the promoter region of the UG gene and are functional targets for prolactin signaling (30,31,(61)(62)(63).…”

Section: Fig 4 Affinity Purified Ug-binding Protein(s)mentioning

confidence: 99%

“…For example, while progesterone up-regulates UG production in the uterus, its induction in the fallopian tubes is dependent upon estrogen. Prolactin appears to enhance the progesterone-induced UG gene expression in the uterus (28,29). Moreover, it is now clear that prolactin transcriptionally augments progesterone-induced UG gene expression in the endometrium via a specific protein that binds at the 5Ј-flanking region of the UG gene (30,31).…”

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Uteroglobin (UG) Suppresses Extracellular Matrix Invasion by Normal and Cancer Cells That Express the High Affinity UG-binding Proteins

Kundu

Mandal

Zhang

et al. 1998

Journal of Biological Chemistry

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Uteroglobin (UG) is a steroid-inducible, multifunctional, secreted protein with antiinflammatory and antichemotactic properties. Recently, we have reported a high affinity UG-binding protein (putative receptor), on several cell types, with an apparent molecular mass of 190 kDa (Kundu, G. C., Mantile, G., Miele, L., CordellaMiele, E., and Mukherjee, A. B. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 2915-2919). Since UG is a homodimer in which the 70 amino acid subunits are connected by two disulfide bonds, we sought to determine whether UG monomers also interact with the 190-kDa UG-binding protein and if so, whether it has the same biological activity as the dimer. Surprisingly, we discovered that in addition to the 190-kDa species, another protein, with an apparent molecular mass of 49 kDa, binds reduced UG with high affinity and specificity. Both 49-and 190-kDa proteins are readily detectable on nontransformed NIH 3T3 and some murine cancer cells (e.g. mastocytoma, sarcoma, and lymphoma), while lacking on others (e.g. fibrosarcoma). Most interestingly, pretreatment of the cells, which express the binding proteins, with reduced UG dramatically suppresses extracellular matrix (ECM) invasion, when such treatment had no effect on fibrosarcoma cells that lack the UG-binding proteins. Tissue-specific expression studies confirmed that while both 190-and 49-kDa UG-binding proteins are present in bovine heart, spleen, and the liver, only the 190-kDa protein is detectable in the trachea and in the lung. Neither the 190-kDa nor the 49-kDa protein was detectable in the aorta. Purification of these binding proteins from bovine spleen by UG-affinity chromatography and analysis by SDS-polyacrylamide gel electrophoresis followed by silver staining identified two protein bands with apparent molecular masses of 40 and 180 kDa, respectively. Treatment of the NIH 3T3 cells with specific cytokines (i.e. interleukin-6) and other agonists (i.e. lipopolysaccharide) caused a substantially increased level of 125 I-UG binding but the same cells, when treated with platelet-derived growth factor, tumor necrosis factor-␣, interferon-␥, and phorbol 12-myristate 13-acetate, did not alter the UG binding. Taken together, these findings raise the possibility that UG, through its binding proteins, plays critical roles in the regulation of cellular motility and ECM invasion.Some of the most important biological processes, such as inflammation, wound healing, embryo implantation, and cancer cell metastasis, involve cellular migration and invasion of the extracellular matrix (ECM).1 However, the mechanisms that regulate these processes are not clearly understood. Recent studies have focused on understanding the receptor-mediated pathways that play critical roles in regulating cellular motility and invasion of the ECM.More than three decades ago, a steroid-inducible secreted protein in the uterus of pregnant rabbits was discovered and was named blastokinin by Krishnan and Daniel (1) and uteroglobin (UG) by Beier (2). Several years later it was recogni...

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“…The precise role of lactogenic hormones (PRL/PL) in the foetomaternal environment is currently unknown. One hypothesis is that lactogenic hormones are not only involved in endometrial -glandular -epithelial hypertrophy and differentiation (Chilton & Daniel 1985, Gray et al 2001a, but also in influencing uterine secretions (Young et al 1989, Randall et al 1991. Because implantation is a process involving a precise synchronization between blastocyst development and uterine receptivity, lactogenic hormones may constitute essential factors in the dialogue between mother and conceptus during this critical period.…”

Section: Introductionmentioning

confidence: 99%

Interferon-τ upregulates prolactin receptor mRNA in the ovine endometrium during the peri-implantation period

Martin

Pessemesse²,

Llosa-Hermier³

et al. 2004

Reproduction

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Our objective was to determine the effect of ovine interferon-t (IFN-t) on prolactin receptor (PRL-R) gene expression in the ovine endometrium. IFN-t is an embryonic cytokine which, via its paracrine anti-luteolytic activity, plays a critical role in maternal recognition of pregnancy in ruminants. Using ribonuclease protection assay procedures, we compared endometrial PRL-R mRNA levels in ewes that were intrauterine injected with either 2 mg bovine serum albumin or 2 mg recombinant ovine IFN-t on day 10 of the oestrous cycle (day 0 5 day of oestrus). IFN treatment significantly increased the abundance of both the long and short forms of PRL-R mRNA in the ovine uterus, but had no effect on the long:short form ratio. In situ hybridization experiments revealed that the increase in abundance of PRL-R mRNA in the uterus was localized to the glandular compartment of the endometrium. In pregnant ewes, a similar increase in PRL-R mRNA abundance was found to occur in ovine endometrium on days 14-15 post conception. Collectively, these data provided strong evidence that IFN-t modulates the level of lactogenic hormone receptor mRNA in the ovine uterus. Whether the effect of IFN-t on PRL-R expression is mediated directly or influenced, at least in part, by progesterone remains to be elucidated.

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Prolactin enhances uteroglobin gene expression by uteri of immature rabbits

Cited by 40 publications

References 8 publications

Lys 43 and Asp 46 in α-helix 3 of uteroglobin are essential for its phospholipase A2 inhibitory activity

Lys 43 and Asp 46 in α-helix 3 of uteroglobin are essential for its phospholipase A2 inhibitory activity

Uteroglobin (UG) Suppresses Extracellular Matrix Invasion by Normal and Cancer Cells That Express the High Affinity UG-binding Proteins

Interferon-τ upregulates prolactin receptor mRNA in the ovine endometrium during the peri-implantation period

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