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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1988-6-28
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pubmed:abstractText |
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. G-hPRL appeared fully sensitive to endoglycosidase F digestion, further supporting the presence of a freely accessible N-linked carbohydrate chain. When assayed for their ability to react with polyclonal antibodies directed against hPRL in a competitive RIA, G-hPRL was 3 times less immunoreactive than NG-hPRL. However, both types of hPRL exhibited superimposable displacement curves when tested in an immunoassay using an anti-hPRL monoclonal antibody. In binding studies using crude rabbit mammary gland membranes G-hPRL was half as potent as NG-hPRL. In stimulating the growth of the Nb2 lymphoma cell line, G-hPRL was 50% less active than NG-hPRL. Thus 1) under basal conditions, hPRL undergoes partial and variable glycosylation; 2) glycosylation of the hormone may modulate its immunoreactivity; 3) glycosylation of hPRL not only lowers its mammary gland receptor binding capacity but also its growth-promoting activity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0013-7227
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
122
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2667-74
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3131120-Adenoma,
pubmed-meshheading:3131120-Animals,
pubmed-meshheading:3131120-Cell Division,
pubmed-meshheading:3131120-Chromatography, Affinity,
pubmed-meshheading:3131120-Chromatography, Gel,
pubmed-meshheading:3131120-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3131120-Female,
pubmed-meshheading:3131120-Glycoside Hydrolases,
pubmed-meshheading:3131120-Glycosylation,
pubmed-meshheading:3131120-Humans,
pubmed-meshheading:3131120-Immunoassay,
pubmed-meshheading:3131120-Male,
pubmed-meshheading:3131120-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase,
pubmed-meshheading:3131120-Mice,
pubmed-meshheading:3131120-Molecular Weight,
pubmed-meshheading:3131120-Pituitary Neoplasms,
pubmed-meshheading:3131120-Polymorphism, Genetic,
pubmed-meshheading:3131120-Prolactin,
pubmed-meshheading:3131120-Radioimmunoassay,
pubmed-meshheading:3131120-Radioligand Assay,
pubmed-meshheading:3131120-Receptors, Prolactin,
pubmed-meshheading:3131120-Structure-Activity Relationship,
pubmed-meshheading:3131120-Tumor Cells, Cultured
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pubmed:year |
1988
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pubmed:articleTitle |
Polymorphism of prolactin secreted by human prolactinoma cells: immunological, receptor binding, and biological properties of the glycosylated and nonglycosylated forms.
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pubmed:affiliation |
Laboratoire de Neuroendocrinologie Expérimentale, Faculté de Médecine Nord, INSERM U 297, Marseille, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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