Eosinophils are cellular targets of the novel uteroplacental heparin-binding cytokine decidual/trophoblast prolactin-related protein

Wang, D; Ishimura, Ryuta; Walia, D.; Dai, Guoli; Hunt, Joan S.; Lee, N A; Lee, J J; Soares, Michael J.

doi:10.1677/joe.0.1670015

Cited by 27 publications

(22 citation statements)

References 63 publications

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“…DPRP is a cytokine possessing an affinity for heparin-containing structures (Rasmussen et al, 1996;Wang et al, 2000). Evidence suggests that DPRP does not circulate but instead is deposited within the decidual extracellular matrix.…”

Section: Discussionmentioning

confidence: 99%

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A uterine decidual cell cytokine ensures pregnancy-dependent adaptations to a physiological stressor

et al. 2007

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In the mouse, decidual cells differentiate from uterine stromal cells in response to steroid hormones and signals arising from the embryo. Decidual cells are crucially involved in creating the intrauterine environment conducive to embryonic development. Among their many functions is the production of cytokines related to prolactin (PRL), including decidual prolactin-related protein (DPRP). DPRP is a heparin-binding cytokine, which is abundantly expressed in uterine decidua. In this investigation, we have isolated the mouse Dprp gene, characterized its structure and evaluated its biological role. Dprp-null mice were made by replacing exons 2 to 6 of the Dprp gene with an in-frame enhanced green fluorescent protein (EGFP) gene and a neomycin (neo) resistance cassette. Heterozygous intercross breeding of the mutant mice yielded the expected mendelian ratio. Pregnant heterozygote females expressed EGFP within decidual tissue in locations identical to endogenous Dprp mRNA and protein expression. Homozygous Dprpnull mutant male and female mice were viable, exhibited normal postnatal growth rates, were fertile and produced normal litter sizes. A prominent phenotype was observed when pregnant Dprp-null mice were exposed to a physiological stressor. DPRP deficiency interfered with pregnancy-dependent adaptations to hypoxia resulting in pregnancy failure. Termination of pregnancy was associated with aberrations in mesometrial decidual cells, mesometrial vascular integrity, and disruptions in chorioallantoic placenta morphogenesis. The observations suggest that DPRP participates in pregnancy-dependent adaptations to a physiological stressor.

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Section: Discussionmentioning

confidence: 99%

“…DPRP is secreted as a glycoprotein by uterine decidual cells and resides in the decidual extracellular matrix where it binds with high affinity to heparin-containing molecules (Rasmussen et al, 1996;Rasmussen et al, 1997;Orwig et al, 1997b;Wang et al, 2000). Little is known about the physiological actions of DPRP.…”

Section: Introductionmentioning

confidence: 99%

A uterine decidual cell cytokine ensures pregnancy-dependent adaptations to a physiological stressor

et al. 2007

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“…The temporal-and spatial-specific patterns of hormone production probably have an effect on hormone delivery and the biology of pregnancy. Members of the PRL family target and influence a wide range of maternal targets, including the reproductive tract, liver and other classic PRL targets (Goffin et al 2002), hematopoietic and immune systems (Lin & Linzer 1999, Müller et al1999, Bittorf et al 2000, Wang et al 2000, Ain et al 2002, Yu-Lee 2002 and vasculature (Jackson et al 1994, Corbacho et al 2002. Some members act via classical mechanisms involving the PRL receptor-signaling pathway, whereas others influence their targets via mechanisms that are at present not well understood.…”

Section: Introductionmentioning

confidence: 99%

Migratory trophoblast cells express a newly identified member of the prolactin gene family

Wiemers¹,

Ain²,

Ohboshi³

et al. 2003

Journal of Endocrinology

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Rodents possess an expanded prolactin (PRL) family of genes. These genes encode for a family of structurally related hormones/cytokines that are expressed most prominently in the anterior pituitary, uterus and placenta. In this study, we have identified a new member of the rat PRL family through a search of the National Center for Biotechnology Information expressed sequence database. The cDNA was sequenced and its corresponding mRNA characterized. On the basis of existing nomenclature, the rat cDNA was termed PRL-like protein-N (PLP-N). PLP-N has structural features indicative of its inclusion in the PRL family and is most closely related to PRL-like protein-F (PLP-F) and proliferin related protein (PLF-RP). A survey of PLP-N mRNA expression by Northern analysis indicated that PLP-N showed extensive expression in the metrial gland and minimal expression in the chorioallantoic placenta or other tissues. Expression of PLP-N mRNA was restricted to migratory trophoblast cells. Junctional zone trophoblast cells isolated from day 13 of gestation placenta differentiated in vitro and exhibited a capacity for PLP-N expression. In summary, we have discovered a new member of the PRL family that is prominently expressed in migratory trophoblast cells residing in the metrial gland.

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“…A similar strategy was previously used to identify cellular targets for other PRL family ligands (Muller et al 1998, Lin & Linzer 1999, Wang et al 2000, Noel et al 2003.…”

Section: Discussionmentioning

confidence: 99%

“…Binding to extracellular matrix (ECM) components has been reported for several cytokines and growth factors, such as oncostatin M , basic fibroblast growth factor (Faham et al 1998), platelet-derived growth factor (Somasundaram & Schuppan 1996), hepatocyte growth factor (Lyon et al 1994), transforming growth factor-b 1 (Paralkar et al 1991), tumor necrosis factor-a and interleukin-2 (Somasundaram et al 2000), interleukin-7 (Ariel et al 1997), and a member of the rat PRL family, decidual/trophoblast PRP (d/t PRP; Rasmussen et al 1996, Wang et al 2000. The purpose of the present study was to explore the target sites of bPL, bPRP-I, and bPRP-VI in situ and to dissect the targetbinding characteristics of bPRP-I.…”

Section: Introductionmentioning

confidence: 99%

Bovine prolactin-related protein-I is anchored to the extracellular matrix through interactions with type IV collagen

Takahashi¹,

Soares²,

Hashizume³

2007

Journal of Endocrinology

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The bovine placenta produces an array of proteins structurally similar to pituitary prolactin (PRL). At least ten genes of the bovine placental PRL family, including bovine placental lactogen (bPL) and ten bovine PRL-related protein-I to -X (bPRP-I to -X), encode hormones/cytokines predicted to be involved in the establishment and maintenance of pregnancy. Targets and biological roles for most members of the bovine PRL family have yet to be specified. This study focused on three members of bovine PRL family, bPL, bPRP-I, and bPRP-VI. An alkaline phosphatase (AP) tagging strategy was used to monitor interactions of the ligands with their targets. AP-bPRP-I and AP-bPRP-VI specifically bound to tissue sections of the bovine placentome. AP-bPRP-I and AP-bPRP-VI binding within the placentome mimicked the distribution of the extracellular matrix (ECM). Consequently, AP fusion protein binding to individual ECM components (heparin, laminin, fibronectin, type I collagen, and type IV collagen) was evaluated. AP-bPRP-I specifically bound to type IV collagen, but not to the other ECM components. AP-bPRP-VI exhibited weak interactions with ECM components, while AP-bPL and AP did not show significant binding to any of the ECM components. Binding of AP-bPRP-I to type IV collagen was concentration-dependent, influenced by salt concentrations, and specific to the N-terminal cross-linking domain (7S) of type IV collagen but not its triple-helical domain. The interaction of bPRP-I with type IV collagen suggests that bPRP-I accumulates in the ECM where it likely acts on cells traversing the bovine placentome.

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Eosinophils are cellular targets of the novel uteroplacental heparin-binding cytokine decidual/trophoblast prolactin-related protein

Cited by 27 publications

References 63 publications

A uterine decidual cell cytokine ensures pregnancy-dependent adaptations to a physiological stressor

A uterine decidual cell cytokine ensures pregnancy-dependent adaptations to a physiological stressor

Migratory trophoblast cells express a newly identified member of the prolactin gene family

Bovine prolactin-related protein-I is anchored to the extracellular matrix through interactions with type IV collagen

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