Biomedical subjects

T M Chu

Publications and source records attributed to T M Chu.

219 records · Page 13Linked to original sources

PubMedDate not supplied

Culture of mammalian prostatic cells.

Preliminary experimental data and concepts oriented toward the achievement of certified primary prostatic cell cultures, normal and/or malignant, for mass distribution are presented. Such monolayer cultures would be established as subcultures from the microcarrier, spin-filter (steady-state) system. The suspension culture of primary cells directly derived from the tissue of origin would be propagated at high cell populations for extended periods of time. The ease of complete monitoring on a sequential basis for conformity to specifications is apparent. The feasibility of the approach appears to have been established. Problems relating to the reduction to practice are detailed.

Acid Phosphatase↗

PubMedDate not supplied

Tumor antigen and acid phosphatase isoenzyme in prostatic cancer.

Plasma and prostatic fluid from man, dog, and baboon were measured for carcinoembryonic antigen (CEA) by a radioimmunoassay technique. No CEA was detected in plasma, prostatic fluid, or seminal fluid in 12 dogs and three baboons. Elevated CEA (less than 2.5 ng/ml) was found in 13 of 20 human prostatic fluids. It was inferred that there was no immunologic cross-reactivity of CEA among man, dog, and baboon. CEA has been isolated and purified from liver tumors. Biochemical studies reveal that CEA consists of 60 percent carbohydrate and 40 percent protein. It contains the following carbohydrates: fucose, mannose, galactose, sialic acid, N-acetylglucosamine, and a small amount of N-acetylgalactosamine. The following amino acids were found in CEA: lysine, histidine, arginine, aspartic acid, threonine, serine, glutamic acid, proline, glycine, alanine, valine, emthionine, isoleucine, leucine, tyrosine, phenylalanine, and cysteine. The amino acid sequence (first 30 amino acids) of the N-terminal has been determined. The N-terminal amino acid was lysine. Using this study as a model, other tumor antigens from prostatic tumor tissues are being investigated. The acid phosphatase isoenzyme from prostatic tissue was also studied. After a series of purifications, two chromatographic fractions were obtained. Treatment with neuraminidase removed the sialic acid content of the molecule, changed the isoelectric focusing patterns, and abolished the chromatographic heterogeneity. Sedimentation studies indicated a molecular weight of about 100,000. Biochemical studies showed that prostatic acid phosphatase isoenzyme is a glycoprotein which consists of 7 percent carbohydrate and 93 percent protein. It contains fucose, galactose, mannose, sialic acid, N-acetylglucosamine, and the following amino acids: aspartic acid, threonine, serine, glutamic acid, proline, glycine, alanine, valine, methionine, isoleucine, leucine, tyrosine, phenylalanine, lysine, histidine, arginine, tryptophan, and cysteine. An antiserum to this purified prostatic acid phosphatase isoenzyme is being prepared in animals.

Acid Phosphatase↗

PubMedDate not supplied

Enzyme markers in human prostatic carcinoma.

In an effort to develop a sensitive and specific method for detecting human prostatic cancer at early stages, we have studied the isoenzyme patterns of acid phosphatase in patients' sera as well as in benign hypertrophic and cancerous prostatic tissues using isoelectric focusing techniques. At least eight acid phosphatase isoenzymes at pI 4.1-5.5 could be observed. The sera with highly elevated acid phosphatase activity generally contained more isoenzymes with pI values of 4.5-5.0. The purified acid phosphatase isolated from benign hypertrophic and malignant prostatic tissues showed no qualitative difference in isoenzyme patterns although quantitative variations were observed. Malignant tissue contained more isoenzymes with pI values of 4.5-4.8. Patients' sera were found to contain isoenzymes of prostate origin. We have also investigated serum ribonuclease (RNase) activity in patients with prostatic cancer. The serum RNase activity of patients was significantly elevated. No significant correlation was observed between serum acid phosphatase and RNase activity. In some instances, where acid phosphatase activity was in the normal range, RNase activity was elevated. These data suggest that simultaneous measurements of RNase and acid phosphatase activities may be of value in the diagnosis of prostatic cancer. The purified RNase has been isolated from human prostatic tissue and its immunologic properties are being studied.

Acid Phosphatase↗