Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0677930 (primary tumor)
 20,210 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Renal carcinoma cells removed surgically from two patients (one primary tumor and one bone metastasis) were maintained in short-term culture. Media conditioned by these cells contained calcium oxalate monohydrate crystal growth inhibitor, a glycoprotein named nephrocalcin (NC). NC was also detected in both cell lines by an enzyme-linked immunosorbent assay using anti-NC antibody raised in rabbits. The glycoprotein was purified from the culture medium and found to have an amino acid composition similar to that of normal human urinary NC. However, NC from the renal carcinoma cells, isolated in multiple forms by DEAE-cellulose column chromatography, contained larger amounts of carbohydrate residues than normal NC. Purified NCs showed a dissociation constant of 10(-6) to 10(-8) M toward calcium oxalate monohydrate crystal. Three renal carcinoma cell lines maintained in long-term culture failed to produce NC. Our study demonstrates that NC is produced by renal cell carcinoma cells (in vitro) from primary and metastatic tumors. Preliminary data suggest that urinary levels of NC corresponded with disease progression in patients with metastatic disease, suggesting that NC may be useful clinically as a tumor marker.
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PMID:Nephrocalcin: biosynthesis by human renal carcinoma cells in vitro and in vivo. 154 Sep 66

Colorectal primary carcinomas and metastases from 20 Dukes' stage C or D patients were examined for the immunohistochemical localization and contents of various fucosylated N-acetyl-lactosamine oligomers by specific monoclonal antibodies (MAbs). MAbs used were SH1, specific for Lewis X antigen; FH4, specific for dimeric Lewis X antigen; FH6, specific for sialyl-dimeric Lewis X antigen; and KH1, specific for Lewis Y-Lewis X antigen. The distribution of the carbohydrate antigens identified by these MAbs was heterogeneous within the primary tumor as well as within the metastatic lesion. Examinations of serial sections indicated that areas within an individual tumor which were stained with one MAb were not always reactive with the other MAbs, although these four MAbs identify closely related structures. The degree of MAb reactivity with carcinoma sections was classified by percentage positive carcinoma cells, and primary tumors and metastases from the same patients were compared. An equivalent or higher proportion of carcinoma cells in the metastatic lesions were reactive with MAb FH6 than in the primary colon carcinomas, but each correlation was not seen with the other MAbs. Electrophoretic separation of tumor tissue extracts followed by staining with these MAbs revealed that a component having an approximate molecular weight of 1,000,000 is the major site for the binding of MAbs, FH6, FH4, and KH1. The electrophoretic mobility of the antigenic molecule on polyacrylamide gels as shown by direct MAb bindings was slightly different from that of a major sialomucin revealed by wheat germ agglutinin in the same tissues. MAb FH6 binding to a high molecular weight component was eliminated by prior treatment of the glycoprotein with mild acid or sialidase to remove sialic acid. Simultaneously, binding of MAb SH2, specific for dimeric Lex antigen, to this component increased. An extract was prepared from a liver metastasis, and high molecular weight components were isolated by gel filtration and then fractionated by DEAE-cellulose ion exchange chromatography. A fraction eluted from DEAE-cellulose between 0.10-0.25 M sodium chloride contained most of the MAb FH6 reactivity, as shown by antibody affinity chromatography. These results support a hypothesis that high molecular weight glycoproteins produced by colorectal carcinoma tissues are heterogeneous with regard to their carbohydrate chains and their antigenic structures may change during tumor progression.
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PMID:Sialyl-dimeric Lewis-X antigen expressed on mucin-like glycoproteins in colorectal cancer metastases. 197 61

Cellular retinol binding protein is present in the cytosol of Lewis lung primary tumor, as detected by DEAE-filter disk method. Gel filtration, followed by non-denaturing polyacrylamide gel electrophoresis, reveals the presence of two binding components. One of them binds retinol specifically as the [3H]retinol can be replaced by unlabeled retinol, but not by unlabeled retinoic acid. In contrast, [3H]retinol radioactivity of the second binding component can be abolished by both unlabeled retinol and unlabeled retinoic acid. SDS polyacrylamide gel electrophoresis shows that the two components have similar migration distances which correspond to an apparent molecular weight of 15,000.
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PMID:Two retinol binding proteins in Lewis lung tumor cytosol. 689 Jul 57

The more differentiated components of a primary tumor may produce substances that reduce the growth rate and metastatic potential of more aggressive components. In the Dunning R-3327 prostatic adenocarcinoma model, cancer cell motility is required for metastatic potential. Medium conditioned by the non-motile, non-metastatic G subline contains proteins of molecular weight 50-100 kDa that inhibited the motility of the highly motile, highly metastatic MAT-LyLu subline. G subline-conditioned medium was separated by DEAE-cellulose chromatography using a linear gradient of 0-0.5 M NaCl in 100 mM Tris at pH 8.3. The motility inhibitory activity of G-conditioned medium was localized to column fractions 51-70 that contained 18% of the applied protein and only 6.5% of the proteins secreted by the G cells. Analysis of pooled fractions 51-60 and 61-70 by two-dimensional gel electrophoresis identified five protein families, with a total of 12 charged proteins of molecular weights approximating 66, 54, 50, 41 and 34 kDa, that were not present or present in reduced quantities in column fractions that did not inhibit motility. Isolation and identification of motility inhibitory protein may prove it the first substance discovered that is produced by a more differentiated component of a neoplasm that directly inhibits a metastasis-associated property.
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PMID:Detection of candidates for cancer cell motility inhibitory protein in the Dunning adenocarcinoma model. 758 5