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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0006141,
umls-concept:C0007634,
umls-concept:C0014597,
umls-concept:C0017968,
umls-concept:C0029205,
umls-concept:C0030685,
umls-concept:C0033572,
umls-concept:C0086418,
umls-concept:C0220781,
umls-concept:C0391871,
umls-concept:C0449830,
umls-concept:C0542341,
umls-concept:C0596625,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1963578
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pubmed:issue |
3-4
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pubmed:dateCreated |
1978-11-18
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pubmed:abstractText |
We demonstrate that a technique is available to investigate glycoprotein synthesis in organ cultures of human breast and prostate surgical specimens where the 3-dimensional epithelial cell arrangement remains intact. Malignant breast and prostate epithelium maintained their capacity to synthesize glycoproteins for at least 3 days as followed by the incorporation of [3H]glucosamine into macromolecules. Over 70% of incorporation was by malignant cells as judged by autoradiography. Labeled glycoproteins were released into glandular lumina and consequently into the culture fluid. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed predominantly one group of macrmolecules released with an apparent molecular weight of 48,000 +/- 6,000 daltons. This glycoprotein was found in all of the breast specimens studied, which included 1 medullary, 1 infiltrating lobular, and 8 infiltrating duct carcinomas. The pattern was independent of the availability of estrogen receptors. A similar glycoprotein was also observed in the culture media from a Grade I and a Grade II well-differentiated infiltrating prostate carcinoma. Incorporation was below the level of detection in 4 of 6 cases of benign prostatic hyperplasia. A more complex pattern of labeled glycoproteins was found in the media of a Grade II and a Grade III poorly-differentiated prostate carcinoma. The established human mammary carcinoma cell line MCF-7 synthesized and released a similar 48,000 molecular weight glycoprotein but additional components with larger molecular weights were also released. An intriguing interpretation that 3-dimensional tissue integrity restricts some glycoprotein synthesis is discussed. Cells grown in 2-dimensional monolayers could escape from such a topographic restriction and express additional families of glycoproteins.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0091-7419
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
515-30
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:211350-Adenocarcinoma,
pubmed-meshheading:211350-Breast,
pubmed-meshheading:211350-Breast Neoplasms,
pubmed-meshheading:211350-Carcinoma, Intraductal, Noninfiltrating,
pubmed-meshheading:211350-Cell Line,
pubmed-meshheading:211350-Epithelium,
pubmed-meshheading:211350-Female,
pubmed-meshheading:211350-Glycoproteins,
pubmed-meshheading:211350-Humans,
pubmed-meshheading:211350-Male,
pubmed-meshheading:211350-Organ Culture Techniques,
pubmed-meshheading:211350-Prostate,
pubmed-meshheading:211350-Prostatic Neoplasms
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pubmed:year |
1977
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pubmed:articleTitle |
Glycoprotein synthesis as a function of epithelial cell arrangement: biosynthesis and release of glycoproteins by human breast and prostate cells in organ culture.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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