Polymorphism of Prolactin Secreted by Human Prolactinoma Cells: Immunological, Receptor Binding, and Biological Properties of the Glycosylated and Nonglycosylated Forms*

1988 
Multiple forms of PRL differing in their physicochemical and biological characteristics have been described. We have analyzed the molecular forms of human (h) PRL released in culture by pure hPRL-secreting tumors with a particular attention to glycosylated hPRL. The prolactinoma cells from six different tumors released, in serum-free conditions, 10- 28 mg hPRL. The combination of polyacrylamide gel electrophoresis and immunoblotting techniques using a [125I]anti-hPRL monoclonal antibody allowed qualitative and quantitative analysis of the hPRL variants. The ratio of the glycosylated 25,000- mol wt form (G-hPRL) to the 23,000-mol wt nonglycosylated monomeric hPRL (NG-hPRL) varied from 0.13 to 0.25. Under the conditions of our studies, cleaved forms of the hormone (19,000 and 15,000 mol wt) accounted for less than 5% of the total immunoreactivity. G- and NG-hPRL were subsequently purified by gel filtration and lectin affinity chromatography. GhPRL appeared fully sensitive to endoglycosidase F digestion, fur...
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