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  • 1
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Chorionic villi from first trimester and term human placentas have been incubated in vitro and shown to release the lysosomal enzymes, β-hexosaminidase, α-glucosidase and β-gluctlronidase. There was negligible release of the cytoplasmic enzyme, lactate dehydrogenase, under the same conditions. The first trimester villi released proportionally more of their lysosomal enzyme content than did the term villi. Extracellular levels of β-hexosaminidase were raised and those of α-glucosidase and, β-glucuronidase were lowered when tissue was incubated with 1 μM colchicine, suggesting that microtubules are involved in the control of lysosomal enzyme release from placental villi.
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  • 2
    ISSN: 0730-2312
    Keywords: α2-macroglobulin ; albumin ; placenta ; zinc ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have investigated the binding and internalization of α2-macroglobulin and serum albumin by human placental syncytiotrophoblast cells in vitro. The time course (obtained at 4°C) of α2-macroglobulin binding indicated that an equilibrium was reached after 4 h. The binding of 125I-labelled α2-macroglobulin to syncytiotrophoblast cells was competitively reduced in the presence of excess unlabelled α2-macroglobulin. When the concentration-dependence of binding was examined over a wide concentration range, non-linear regression analysis yielded a Kd of 6.4 nM. In the case of albumin, binding was weak and ligand dissociated from the cell surface during aqueous washing making it impractical to analyze the binding reaction. In other experiments, syncytiotrophoblast cells were incubated with 125I-labelled α2-macroglobulin at 37°C. Under these conditions, trypsin-resistant cell-associated radioactivity increased with time consistent with ligand internalization. 125I-Labelled-ligand was internalized with a t1/2 of about 5 min. After a lag period some radioactivity was released back into the incubation medium. When measured at times up to 210 min, this was found to consist of mostly TCA-precipitable material that had been lost from the cell surface. However, when the incubation was extended to 24 h, almost 15% of the initial cell-associated radioactivity was released to the extracellular medium as TCA-soluble material, consistent with a slow rate of ligand degradation. The specific binding of 65Zn-labelled α2M was similar to that of the 125I-labelled ligand and trypsin-resistance measurements provided evidence of α2M-mediated 65Zn uptake. These results support a role for syncytiotrophoblast in the metabolism of α2-macroglobulin during pregnancy and are also consistent with a role for α2-macroglobulin in the maternal-fetal transport of zinc. J. Cell. Biochem. 68:427-435, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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  • 3
    ISSN: 0730-2312
    Keywords: placenta ; planar-polar compounds ; hCG ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Dimethyl sulfoxide (DMSO) exerts a number of biological effects, the most frequently cited being induction of cell differentiation. The compound also increases invasiveness and metastatic potential. In contrast to the many reports of DMSO-induced cell differentiation, we report here that DMSO inhibits the morphological differentiation of human cytotrophoblast cells to syncytiotrophoblast, as revealed by immunofluorescence staining for desmosomal protein and nuclei. Cytotrophoblast cells treated with DMSO under differentiation-inducing conditions remained mononucleated with intense desmosomal staining. The effect was dose dependent, with a maximal effect seen at 1.5% DMSO. Concentrations of ≤0.5% had no effect and concentrations 〉2% were cytotoxic. In addition to these morphological changes, DMSO inhibited secretion of human chorionic gonadotropin in a dose-dependent manner. At a concentration of 1.5%, DMSO inhibited secretion by 70%. If cytotrophoblast cells were cultured in the presence of DMSO and then switched to DMSO-free medium, they proceeded to differentiate normally. While the precise mechanism of action remains unknown, judicious use of DMSO may be a useful tool for studying and manipulating the differentiation of human trophoblast cells in vitro. The findings also indicate that care should be used in interpreting results obtained using DMSO as a carrier in drug and inhibitor studies. J. Cell Biochem. 65:460-468. © 1997 Wiley-Liss Inc.
    Additional Material: 6 Ill.
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