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      Prolactin Isoforms Secreted by Human Prolactinomas

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          Abstract

          Prolactin (hPRL) secreted by human prolactinoma cells in culture was purified by gel filtration, lectin affinity chromatography and gel electrophoresis in order to identify the different isoforms of the hormone and to test their respective immunoreactivities and bioactivities. The nonglycosylated hPRL (NG-hPRL), unbound to lectins, was the major form and was a species (NG1-hPRL), of 23,000 (M<sub>r</sub>) apparent molecular weight. The lectin-bound glycosylated hPRL (G-hPRL) consisted of three forms, G1-, G2- and G3-hPRL, of identical molecular weights (25,000 M<sub>r</sub>). Endoglycosidase treatment indicated that these three forms differed by the heterogeneity of their carbohydrate chains. These G-PRLs proved to be 68% less immunoreactive and 50% less bioactive than NG-hPRL. It is concluded from these data that, in prolactinomas, the main variant of the hormone is the nonglycosylated form of PRL.

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          Author and article information

          Journal
          HRE
          Horm Res Paediatr
          10.1159/issn.1663-2818
          Hormone Research in Paediatrics
          S. Karger AG
          1663-2818
          1663-2826
          1992
          1992
          03 December 2008
          : 38
          : 3-4
          : 164-170
          Affiliations
          aLaboratoire de Neuroendocrinologie Expérimentale, INSERM U 297, et bLaboratoire d’lmmunochimie des Hormones Glycoprotéiques, Faculté de Médecine Nord, Marseille, France
          Article
          182534 Horm Res 1992;38:164–170
          10.1159/000182534
          1306849
          © 1992 S. Karger AG, Basel

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          Page count
          Pages: 7
          Categories
          Original Paper

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