Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0019204 (hepatocellular carcinoma)
 71,386 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The target antigens for the complement-dependent cytotoxic antibodies in D23 tumour-bearer serum from rats carrying the chemically induced D23 hepatoma were extractable from extranuclear membranes of tumours with chloroform/methanol. The antigenic activity, measured by inhibition of D23 TBS cytotoxicity against D23 cells, was recovered in the phospholipid-containing fraction after silica gel chromatography. Preparative thin-layer chromatography (in chloroform/methanol/0.25% CaCl2) revealed that the antigenic activity migrated similarly to phosphatidylethanolamine and cardiolipin, although these phospholipids did not cause the inhibition seen with the antigenic fractions. Phospholipase A2 digestion of the phospholipid fraction did not affect the antigenic activity nor did it after the mobility of the antigen when analysed with thin-layer chromatography. From these results it was concluded that the antigen extracted from D23 hepatoma may be of phospholipid nature, although its molecular identity remains to be established.
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PMID:The lipid nature of a tumour-associated autoantigen from a chemically induced rat hepatoma. 617 53

3M-KCl extracts of the hepatoma D23 contain antigens that inhibit the complement-dependent cytotoxicity for D23 hepatoma cells of serum from D23 tumour-bearing rats (D23 TBS). Inhibition was not due to a general anticomplementary activity of the extracts. Although a minor part (25%) of the protein of D23-KCl extract was insoluble in PBS, this part contained most of the inhibitory activity. Fractionation of the PBS-soluble material of the extract on Concanavalin A-Sepharose showed that the inhibitory activity did not bind to the lectin. Analysis of D23-KCl extracts on a Sepharose CL-4B column showed that the antigens involved in the cytotoxicity were heterogeneously distributed in the high-mol. wt region (greater than 200,000). Precipitation with 10% trichloroacetic acid (TCA) of D23 KCl extracts revealed that most of the antigenicity was insoluble in TCA. Heating of D23 KCl extracts at 100 degrees C did not affect the antigenicity. Enzyme treatment of D23 extra nuclear membranes (D23 ENP) revealed that the inhibitory activity was not sensitive to proteolytic digestion, while treatment with phospholipase A2, C or D abrogated partly the inhibitory activity. The lipid nature of the antigenicity was indicated by its solubility in organic solvents as chloroform or n-butanol.
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PMID:Tumour-associated antigens reacting with cytotoxic antibodies in serum of hepatoma-bearing rats. 729 8

The immunoglobulin class of the complement-dependent cytotoxic antibodies in serum from D23 hepatoma-bearing rats (D23 TBS) for D23 hepatoma cells was analysed. When studied by affinity chromatography with concanavalin A, protamine, or staphylococcal protein A conjugated to Sepharose, the cytotoxic activity bound to the former two but not protein A. The binding fractions were further characterized by column chromatography on Sepharose CL-4B. The cytotoxic activity was recovered exclusively in the high molecular weight fractions corresponding to human IgM. Monitoring with IgG- or IgM-specific rabbit antibodies indicated that these high molecular weight cytotoxic fractions contained both IgG and IgM. However, fractionation of D23 TBS at low pH suggested that cytotoxicity was due to IgM antibodies rather than to immune-complexed IgG antibodies. This was supported by the findings that rabbit antirat IgM antibodies inhibited the cytotoxicity of TBS completely when added at high dilutions.
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PMID:Determination of the immunoglobulin class of complement-dependent cytotoxic antibodies in serum of D23 hepatoma-bearing rats. 953 53