Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells.
- 1 June 1986
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 83 (11) , 3781-3785
- https://doi.org/10.1073/pnas.83.11.3781
Abstract
The expression of human placental-type alkaline phosphatase (ALPase) in the placenta and in three choriocarcinoma cell lines was examined by translation in vitro and RNA blot analysis using a cDNA for placental ALPase. Placental RNA directed the synthesis of two polypeptides that could be immunoprecipitated with antiserum to placental ALPase. Translation of RNA from the choriocarcinoma cell lines, with or without sodium butyrate treatment, yielded a single immunoprecipitable product of molecular weight intermediate between those of the products from the placenta mRNA. Two cDNA clones for placental ALPase were isolated by antibody screening of a placental cDNA library constructed in .lambda.gt11. The overlapping cDNAs include 462 nucleotides of coding sequence. RNA blot analysis has confirmed that induction of placental-type ALPase levels during placental development is accompanied by an increase in steady-state placental ALPase mRNA concentrations. Examination of the mRNAs revealed a placental ALPase mRNA of 3.0 kilobases (kb) and a distinct choriocarcinoma placental-type ALPase mRNA of 2.6 kb, implying that transformation of normal to malignant trophoblast is associated with the expression of a distinct placental-type ALPase gene transcript and its protein product.This publication has 32 references indexed in Scilit:
- Yeast RNA Polymerase II Genes: Isolation with Antibody ProbesScience, 1983
- A simple and very efficient method for generating cDNA librariesGene, 1983
- Purification and partial sequencing of human placental alkaline phosphataseBiochemical and Biophysical Research Communications, 1983
- A technique for radiolabeling DNA restriction endonuclease fragments to high specific activityAnalytical Biochemistry, 1983
- Biosynthesis and processing of placental alkaline phosphataseBiochemical and Biophysical Research Communications, 1983
- Two mRNAs can be produced from a single immunoglobulin μ gene by alternative RNA processing pathwaysCell, 1980
- Characteristics of alkaline phosphatase from two continuous lines of human choriocarcinoma cellsExperimental Cell Research, 1977
- An Efficient mRNA‐Dependent Translation System from Reticulocyte LysatesEuropean Journal of Biochemistry, 1976
- Perspectives on alkaline phosphatase isoenzymesThe American Journal of Medicine, 1974
- L-leucine sensitive, heat-stable alkaline-phosphatase isoenzyme detected in a patient with pleuritis carcinomatosaClinica Chimica Acta; International Journal of Clinical Chemistry, 1970