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Biomedical subjects

C K Liu

Publications and source records attributed to C K Liu.

At least 55 records · Page 3Linked to original sources
PubMed1984

Abnormal isoelectric focusing patterns of serum galactosyltransferase activity in patients with liver neoplasia.

Serum galactosyltransferase activity (GT) has been studied using isoelectric focusing chromatography in normal subjects, in patients with non-neoplastic liver diseases, and patients with liver neoplastic diseases (hepatoma and liver metastases) using isoelectric focusing chromatography. Freshly obtained serum was applied to an isoelectric focusing column containing Ampholine (pH 4-6) and the fractions were assayed using asialo-agalactofetuin as the galactose acceptor. Three peaks of GT activity were found in sera from normal subjects at pH 4.8, 4.95, and 5.1. In contrast, sera from patients with hepatoma or with gastrointestinal adenocarcinoma with liver metastases contained only two peaks of GT activity (pI 4.75 and 4.95). Sera from patients with non-neoplastic liver diseases had similar GT isoelectric focusing patterns as those from normal subjects. These results suggest that the isoelectric focusing patterns of serum GT activity may be useful in characterizing human liver neoplasia.

Adenocarcinoma↗
PubMed1983

Glycosyltransferase alterations are cell type related when human promyelocytic leukemia (HL-60) cells are treated with various inducers of differentiation.

We have assayed glycosyltransferase activities during the granulocytic and macrophage-like differentiation of human promyelocytic leukemia (HL-60) cells. Functional granulocytic differentiation was assayed by the decarboxylation of 2-deoxyglucose in addition to nitroblue tetrazolium reduction. Dimethylsulfoxide (DMSO) treated HL-60 cells, induced to granulocytic differentiation, had higher 2-deoxy-glucose decarboxylation activity, and contained less sialyltransferase (ST), more fucosyltransferase (FT), and more N-acetylglucosaminyltransferase (NGT) activities than untreated cells. HL-60 cells treated with another granulocytic differentiator, retinoic acid, also had higher 2-deoxyglucose decarboxylation activity, and contained less ST, more FT, and more NGT activities than untreated cells. In contrast, cells treated with 12-O-tetradecanoyl-phorbol-13-acetate (TPA) reported to differentiate HL-60 to macrophage-like cells, but did not show an increased level of 2-deoxyglucose decarboxylation activity, but contained more galactosyltransferase (GT) and FT activities as compared to untreated cells. These findings suggest that the alterations of glycosyltransferase levels during the differentiation of precursor cells may not depend upon different inducers, but are characteristic of the phenotypic expression of the mature cell type.

Cell Line↗
PubMed1982

Characterization of galactosyltransferase released from human hepatoma cells.

A human hepatoma cell line (SK-H-MA) released a large amount of sialyltransferase (ST) and galactosyltransferase (GT) into the culture medium, whereas cells derived from normal human liver (Chang) released a large amount of GT but very little ST. The characteristics of hepatoma GT were studied since an abnormal GT isoenzyme has been associated with human gastrointestinal neoplasms. Both hepatoma and Chang medium GT activities had an absolute requirement for MnCl2 (25 mmol/l) and a broad optimal pH between 6.5 and 7.0, and were not affected by 0.1% Triton X-100. These two enzyme preparations were inhibited to the same extent by N-acetylglucosamine and N-acetylgalactosamine, while N-acetylglucosamine was 100 times more potent than N-acetylgalactosamine. Various nucleotides inhibited both enzyme activities equally well. Uracil-containing nucleotides were better inhibitors than thymine-containing nucleotides, and other nucleotides were only slightly inhibitory. The most effective inhibitor was UDP. More of the GT activity in hepatoma medium (65%) as compared to Chang medium (35%) bound to concanavalin A-Sepharose, and was eluted with 2.5% alpha-methylmannoside. These results suggest that the GTs from hepatoma and Chang media are not different in their enzymatic activity but may differ in their carbohydrate contents, which may be another manifestation of the neoplastic nature of the hepatoma cell line.

Animals↗
PubMed1980

12-O-tetradecanoyl-phorbol-13-acetate release of glycosyltransferases from human blood cells.

The mononuclear cells separated from human blood by Ficoll-Hypaque centrifugation contained and released sialyltransferase, galactosyltransferase, and fucosyltransferase. Granulocytes contained and released lesser amounts of glycosyltransferases, whereas platelets released more fucosyltransferase than sialyltransferase or galactosyltransferase. When mononuclear cells were incubated with 12-O-tetradecanoyl-phorbol-13-acetate (TPA), the release of these three glycosyltransferases increased two- to six-fold, and cell suspension glycosyltransferase activities decreased 10-50%. Mononuclear cells were fractionated into lymphocytes and monocytes using baby hamster kidney cells microexudate-coated flasks. TPA stimulated the release of glycosyltransferases from lymphocytes but not from monocytes. The release of glycosyltransferases by TPA-treated mononuclear cells was not further stimulated by reincubation with TPA and was not affected by puromycin, cAMP, or cGMP. Concanavalin A, a mitogenic stimulator of lymphocytes, also stimulated the release of glycosyltransferases from mononuclear cells, but to a lesser extent. TPA did not stimulate the release of 5'-nucleotidase or decrease its activity on the cell pellet. Triton X-100 (0.2%) stimulated the release of glycosyltransferases to the same extent as TPA, but also caused the release of 5'-nucleotidase. [(3)H]TPA bound specifically and reversibly to mononuclear cells. The possible relationship between glycosyltransferase release and TPA effect on the plasma membrane is discussed.

Cell Separation↗
PubMed1979

The specific release of sialytransferase activity by human hepatoma cell lines.

Sialyltransferase (EC 2.4.99.1) is released in large amounts by two hepatoma cell lines (SK-H-MA and CLH) established from patients with hepatocellular carcinoma (hepatoma). This release requires protein synthesis and glycoprotein synthesis, but not cell division. In contrast, sialyltransferase is released in minimal amounts by a cell line derived from normal human liver (Chang). The hepatoma cells also contain more surface and cellular sialyltransferase activity than Change cells. Hepatoma sialyltransferase has properties similar to other sialyltransferases. Using a calibrated Sephadex G-200 column, it is resolved into two forms with molecular weights of 65 000 and 80 000.

Carcinoma, Hepatocellular↗
PubMed1977

The clinical and physiological implications of hepatoma B12-binding proteins.

A serum B12-binding protein with increased sialic acid content (termed hepatoma B12-binding protein) that causes elevations of serum B12 and unsaturated B12-binding capacity has been found in some patients with hepatocellular carcinoma (hepatoma). We now report another patient with hepatoma with initial near-normal, unsaturated B12-binding capacity that increased 400-fold as the disease progressed and then fell 50% with response to chemotherapy. A perfusate of the tumor in the liver had 5 times more B12-binding protein than did the serum and was immunologically the same as the serum hepatoma B12-binding protein isolated from previous cases. A cell line derived from hepatoma produced significant amounts of B12-binding protein similar to hepatoma B12-binding protein, whereas cell lines from normal liver and other neoplasia did not. The hepatoma sera, perfusate, and media from the hepatoma cell line contained elevated sialyltransferase activity. These data suggest that some hepatomas produce increased hypersialylated B12-binding protein that is cleared slowly from the plasma and accumulates there as hepatoma B12-binding protein.

Adolescent↗
PubMed1974

Role of phospholipids in the multiple forms of mammalian elongation factor 1.

Evidence is presented that high-molecular-weight aggregates of elongation factor 1 from calf brain and liver contain phospholipids. Sucrose gradient analysis has shown that these high-molecular-weight species can be converted to a low-molecular-weight form after incubation with different phospholipase preparations. In addition, a partially purified elongation factor 1 from rabbit reticulocytes is also converted to a low-molecular-weight species by phospholipase treatment. These data indicate that phospholipids are involved in maintaining the integrity of the high-molecular-weight species and support the view that this species is an aggregate of the low-molecular-weight elongation factor 1.

Animals↗