Synthesis of alpha subunit of human chorionic gonadotrophin by presumptive HeLa cells

In Vitro. 1976 Aug;12(8):589-94. doi: 10.1007/BF02797443.

Abstract

Several cell lines, originally thought to be derived from a human placenta at term but possibly HeLa-contaminated, have been studied. These cells secrete a protein indistinguishable immunochemically from the alpha subunit of chorionic gonadotropin but not the beta subunit of chorionic gonadotropin or placental lactogen. Complete chorionic gonadotropin was detected but amounted to less than 1% of the level of the alpha subunit. The cells also produce an alkaline phosphatase similar to placental alkaline phosphatase in immunochemical, gel-electrophoretic, and heat-denaturation properties. They induce tumor growth when inoculated into nude mice. These cells are aneuploid and have a model chromosome number of 66. The common HeLa karyologic markers, designated 1, 2, and 3, and A-type glucose-6-phosphate dehydrogenase are present in these cells. HeLa cells have not previously been shown to secrete the alpha subunit of hCG.

MeSH terms

  • Alkaline Phosphatase / analysis
  • Alkaline Phosphatase / biosynthesis
  • Cell Division
  • Chorionic Gonadotropin / biosynthesis*
  • Clone Cells / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Glucosephosphate Dehydrogenase / analysis
  • HeLa Cells / enzymology
  • HeLa Cells / metabolism*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Karyotyping

Substances

  • Chorionic Gonadotropin
  • Glucosephosphate Dehydrogenase
  • Alkaline Phosphatase