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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1983-12-17
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pubmed:abstractText |
This report describes the conversion of a murine pituitary thyrotropic tumor (MGH 101) to a pure alpha-subunit-secreting tumor (MGH 101A) during a 6-yr period of serial transplantation. MGH 101 was a thyrotropic tumor originating from a hypothyroid mouse pituitary, growing only in hypothyroid hosts, and secreting large quantities of intact TSH and free alpha-subunit. Between the fourth and ninth transplantation generations, tumor TSH secretion declined progressively by at least 500-fold, to undetectable levels. In contrast, tumor secretion of free alpha-subunit decreased only 10-fold, and has since remained stable for nine transplantation generations. During the conversion to pure alpha-subunit secretion, MGH 101A exhibited growth in euthyroid as well as hypothyroid hosts, and increased its growth rate 2 to 3-fold. In contrast, the conventional thyrotropic tumor TtT 97 has maintained its secretion of both intact TSH and free alpha-subunit, its dependence on a hypothyroid environment, and its slower growth rate for nine generations. Gel chromatography of the media from tumor cell cultures confirmed that MGH 101A secreted only the free alpha-subunit, whereas TtT 97 secreted immunoactive TSH, TSH beta, and free alpha-subunit which eluted as separate peaks. We conclude that a dependent thyrotropic tumor has spontaneously developed into a pure alpha-subunit-secreting tumor which is independent of host thyroid function for its growth and alpha-subunit production.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoprotein Hormones, alpha Subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Pituitary Hormones, Anterior,
http://linkedlifedata.com/resource/pubmed/chemical/Thyrotropin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0013-7227
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
113
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1587-91
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6194976-Animals,
pubmed-meshheading:6194976-Cell Line,
pubmed-meshheading:6194976-Chromatography, Gel,
pubmed-meshheading:6194976-Culture Media,
pubmed-meshheading:6194976-Glycoprotein Hormones, alpha Subunit,
pubmed-meshheading:6194976-Male,
pubmed-meshheading:6194976-Mice,
pubmed-meshheading:6194976-Neoplasm Transplantation,
pubmed-meshheading:6194976-Peptide Fragments,
pubmed-meshheading:6194976-Pituitary Hormones, Anterior,
pubmed-meshheading:6194976-Pituitary Neoplasms,
pubmed-meshheading:6194976-Thyrotropin,
pubmed-meshheading:6194976-Time Factors
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pubmed:year |
1983
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pubmed:articleTitle |
Mouse pituitary tumor line secreting only the alpha-subunit of the glycoprotein hormones: development from a thyrotropic tumor.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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