Mouse Placental Cells Secrete Soluble Leptin Receptor (sOB-R): cAMP Inhibits sOB-R Production

Yamaguchi, Masatoshi; Murakami, Takashi; Yasui, Yumiko; Otani, Shizuka; Kawai, Motoyuki; Kishi, Kurajiro; Kurachi, Hirohisa; Shima, Kenji; Aono, Toshihiro; Murata, Yuji

doi:10.1006/bbrc.1998.9636

Cited by 26 publications

(22 citation statements)

References 26 publications

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“…In mice, the circulating concentration of the soluble form of the leptin receptor (Re) is markedly (40-fold) raised in pregnancy and, by binding leptin and inhibiting its metabolism, 40 it appears to be responsible for a rise of similar magnitude in circulating leptin levels. 41 Since placental cells secrete soluble leptin receptor, 42 it is possible that reduced production of a binding protein around the time of parturition greatly enhanced the metabolism of the infused leptin. In addition, there may be a significant clearance of leptin bound to placenta 43 and decidua.…”

Section: Discussionmentioning

confidence: 99%

Modulation of susceptibility to weight gain and insulin resistance in low birthweight rats by treatment of their mothers with leptin during pregnancy and lactation

et al. 2003

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OBJECTIVES:To investigate whether administration of leptin to rats during pregnancy and lactation affects placental 11b-hydroxysteroid dehydrogenase (11b-HSD2) activity and the susceptibility of their offspring to weight gain and insulin resistance. DESIGN: Pregnant rats fed on a low-protein diet were administered leptin or saline by subcutaneous minipump from day 14 of gestation and throughout lactation. A further group was fed a normal diet and given saline. After weaning, the offspring of each group were fed on a normal diet until 6 weeks of age and then half of each group was transferred to a high-fat diet until 12 months of age. RESULTS: Plasma leptin levels were raised two-fold on days 16-18 of pregnancy in the leptin-treated dams, but, despite a constant rate of infusion, at parturition they dipped to control levels before rising again. The activity of placental 11b-HSD2 was reduced by the low-protein diet; this reduction was prevented by treating the dams with leptin. The male offspring of the salinetreated dams gained more weight and had higher plasma leptin levels on the high fat than the chow diet, but the offspring of the leptin-treated dams did not. Fasting blood glucose and intraperitoneal glucose tolerance at 6 and 12 months of age was unaffected by the high-fat diet, but only the offspring of the leptin-treated dams achieved this control without raised insulin levels. CONCLUSIONS: The rate of leptin clearance appears to increase at parturition. The administration of leptin to rats during late pregnancy and lactation makes their male offspring less susceptible to high-fat-diet-induced weight gain and insulin resistance.

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Section: Discussionmentioning

confidence: 99%

Modulation of susceptibility to weight gain and insulin resistance in low birthweight rats by treatment of their mothers with leptin during pregnancy and lactation

et al. 2003

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“…The CHO cell clone, which stably expresses rat OB-Re (Yamaguchi et al 1998), was incubated with serum-free medium S-Clone SF-02 (Sanko Junyaku Co. Ltd, Tokyo, Japan). The conditioned media was dialyzed against buffer A (25 mM HEPES (pH 7·4), 100 mM NaCl), followed by two passes through a wheat germ lectin Sepharose 6 MB column (Amersham Pharmacia Biotech Ltd, Amersham, Bucks, UK).…”

Section: Partial Purification Of Rat Ob-rementioning

confidence: 99%

“…The resulting protein was used as the antigen for immunizing Hartley guinea pigs (obtained from Japan SLC, Inc.) and anti-OB-R antiserum was obtained as described previously (Yamaguchi et al 1998).…”

Section: +mentioning

confidence: 99%

“…This is not the case for the rat, however, where the placenta does not produce significant amounts of leptin and adipose tissues per se increase leptin production during pregnancy (Kawai et al 1997). In the mouse, the placenta secretes the OB-Re and, as a result, serum leptin levels, which are measured by radioimmunoassay (RIA), increase significantly during pregnancy (Gavrilova et al 1997, Tomimatsu et al 1997, Yamaguchi et al 1998). In the case of a family with early-onset morbid obesity, as the result of a defect in the human OB-R gene (Clément et al 1998), all of the isoforms of OB-R are produced as the secretory form in affected persons who have a homozygous mutation, and who show high levels of serum leptin.…”

Section: Introductionmentioning

confidence: 99%

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Influence of the presence of OB-Re on leptin radioimmunoassay

Murakami

Otani²,

Honjoh³

et al. 2001

Journal of Endocrinology

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Leptin, a hormone derived from adipose tissue, regulates energy homeostasis and body weight. In the mouse, serum leptin levels, when measured by radioimmunoassay (RIA), increase by a factor of more than 50 times during pregnancy, compared with those in the non-pregnant state. It is well known that mouse placenta produces the secretory isoform of the leptin receptor, OB-Re. In order to investigate the issue of whether serum leptin levels are actually increased during pregnancy or whether the increased OB-Re concentration plays a role in this phenomenon, serum leptin levels were determined by the immunoprecipitation of leptin using anti-leptin antibody, and were found to be increased only by about ten times during pregnancy. To investigate the influence of OB-Re on leptin measurement by the RIA procedure, serum leptin levels were measured by the RIA after the addition of OB-Re to the serum. The apparent values of leptin levels increased in parallel with the amount of OB-Re added to the serum. Leptin levels, as determined by the RIA, might therefore provide artificially high values when serum levels of the secretory form of OB-R are high, in cases, for example, such as the last period of pregnancy in mice.

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“…Many studies have validated this cell model for studying aspects of trophoblast biology including cell cycle regulation, cell differentiation regulation, trophoblast phenotypic characterization, cell invasion, and trophoblast tumor development [14,16,24,[30][31][32][33][34][35]. Differentiation of Rcho-1 cells to yield cells with a trophoblast giant cell phenotype helps overcome the inherent difficulties in obtaining purified populations of these cells from tissues [16].…”

Section: Discussionmentioning

confidence: 99%

Expression of Cathepsin P mRNA, Protein and Activity in the Rat Choriocarcinoma Cell Line, Rcho-1, During Giant Cell Transformation

Hassanein

Korant

et al. 2007

Placenta

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Lysosomal proteases perform critical functions in protein turnover and are essential for normal growth and development. Cathepsin P is a member of a newly discovered family of lysosomal cysteine proteases uniquely expressed in rodent placenta (PECs), and is closely related to human cathepsin L. Using the rat choriocarcinoma cell line model, Rcho-1, mRNA for the PECs cathepsins P, M, Q, R, 1, 2 was found to increase in expression during differentiation into a trophoblast giant cell phenotype. By contrast, expression of cathepsin L was not regulated. A specific enzyme assay was developed to show that activity of cathepsin P mirrored mRNA expression during differentiation. Cathepsin P protein co-localizes with cathepsin B, indicating that the enzyme probably functions in the endosomal-lysosomal compartment. This study demonstrates that the PEC genes produce functional proteases that can perform specific placental roles that are probably performed by broader specificity proteases in human placenta.

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Mouse Placental Cells Secrete Soluble Leptin Receptor (sOB-R): cAMP Inhibits sOB-R Production

Cited by 26 publications

References 26 publications

Modulation of susceptibility to weight gain and insulin resistance in low birthweight rats by treatment of their mothers with leptin during pregnancy and lactation

Modulation of susceptibility to weight gain and insulin resistance in low birthweight rats by treatment of their mothers with leptin during pregnancy and lactation

Influence of the presence of OB-Re on leptin radioimmunoassay

Expression of Cathepsin P mRNA, Protein and Activity in the Rat Choriocarcinoma Cell Line, Rcho-1, During Giant Cell Transformation

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