Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An immunohistochemical study analyzing distributions of beta-subunit human chorionic gonadotropin (beta HCG), human placental lactogen (HPL), placental alkaline phosphatase (PLAP), and monoclonal anti-cytokeratin (PKK1) was undertaken to determine whether the reactivity of these antigens might assist in the differential diagnosis of molar and non-molar hydropic placentas. A total of 16 complete hydatidiform moles, 15 partial hydatidiform moles, 12 hydropic abortuses and 39 non-hydropic placentas with gestational age ranging from 4 to 40 weeks was examined. In both the complete and partial moles, many syncytiotrophoblasts stained for beta HCG, HPL, PLAP and PKK1 although the staining intensity of beta HCG in the partial moles was weak compared with the complete moles. The staining patterns in the hydropic abortuses were almost the same as those in the normal first trimester placentas and had no distinct features from the partial moles. Trophoblastic hyperplasia is an essential feature in differentiating partial moles from hydropic abortuses. With regard to the immunostaining patterns of these antibodies, there was no significant difference to enable delineation between partial and complete moles, or between a hydropic abortus and a partial mole. Monoclonal anti-cytokeratin was most sensitive for trophoblasts, but less specific for intermediate trophoblasts than HPL. Although an immunohistochemical study using antibodies against beta HCG, HPL, PLAP and PKK1 is very useful for characterizing various trophoblasts, it is considered that an immunohistochemical study may not be a suitable tool for the differential diagnosis of molar and non-molar hydropic placentas.
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PMID:Immunohistochemistry of molar and non-molar placentas with special reference to their differential diagnosis. 750 73

Non-trophoblastic neoplasms are the most frequent, benign tumors of the placenta, occurring in approximately 1% of all placentas examined. A case is described of a 24-year-old woman who presented with severe, early-onset pre-eclampsia, high human chorionic gonadotropin (hCG) levels, and a triploid fetus and who was found to have a small choriohemangioma. The woman, gravida 2 para 1, was referred to our hospital for perinatal evaluation. The fetus, gestational age 18 weeks 3 days, had fetal growth restriction with multiple congenital anomalies. The fetal karyotype was 69,XXY. Compared with the normal range for this gestational age, the beta-hCG level was significantly elevated (1,054,000 mIU/ml) as was the maternal serum alpha-feto-protein measurement (539.1 ng/ml). Sonographically, the placenta appeared hydropic, irregularly shaped, and gelatinous. A suction dilatation and evacuation under sonographic guidance was performed. Histological examination of placental tissue revealed hydropic degeneration of the chorionic villi. The specific histological features of a partial molar pregnancy were not present. However, there were changes consistent with a choriohemangioma. Flow cytometric DNA analysis performed on formalin-fixed, paraffin-embedded tissue blocks of placenta showed triploidy. Immunohistochemical staining with human placental alkaline phosphatase was consistent with a hydropic degeneration pattern. We conclude, first, that triploidy does not always imply the presence of a partial mole. Second, the dictum, that pre-eclampsia, if it occurs under 20 weeks' gestation, must be associated with a molar pregnancy, may not hold when placental aneuploidy is present. Although the findings in this pregnancy could have been incidental, there may be an association between a choriohemangioma and polyploidy.
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PMID:A non-trophoblastic tumor co-existing with a triploid fetus. 936 38

GPI-anchored proteins are ubiquitous on the eukaryotic cell surface, where they are involved in a variety of functions ranging from adhesion to enzymatic catalysis. Indirect evidence suggests that the GPI anchor may hold the protein close to the plasma membrane; however, there is a lack of direct information on the proximity of the protein portion of GPI-anchored proteins to the bilayer surface. The present study uses fluorescence resonance energy transfer (FRET) to address this important problem. The GPI-anchored ectoenzyme placental alkaline phosphatase (PLAP) was purified from a plasma membrane extract of human placental microsomes without the use of butanol. The protein was fluorescently labeled at the N-terminus with 7-(dimethylamino)coumarin-4-acetic acid succinimidyl ester (DMACA-SE) or Oregon Green 488 succinimidyl ester (OG488-SE), and each was reconstituted by detergent dilution into defined lipid bilayer vesicles containing an increasing mole fraction of a fluorescent lipid probe. The fluorescence of the labeled PLAP donors was quenched in a concentration-dependent manner by the lipid acceptors. The energy transfer data were analyzed using an approach that describes FRET between a uniform distribution of donors and acceptors in an infinite plane. The distance of closest approach between the protein moiety of PLAP and the lipid-water interfacial region of the bilayer was estimated to be smaller than 10-14 A. This indicates that the protein portion of PLAP is located very close to the lipid bilayer, possibly resting on the surface. This contact may allow transmission of structural changes from the membrane surface to the protein, which could influence the behavior and catalytic properties of GPI-anchored proteins.
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PMID:Proximity of the protein moiety of a GPI-anchored protein to the membrane surface: a FRET study. 1208 85