Serum human telomerase reverse transcriptase: a novel biomarker for breast cancer diagnosis.

Background: Telomerase is a ribonucleoprotein complex composed mainly of a reverse transcriptase catalytic subunit, telomerase reverse transcriptase (hTERT). Expression of hTERT confers telomerase activity, indicating that hTERT is the rate-limiting component of human telomerase. The aim of the present study was to investigate the diagnostic implications of hTERT in the serum of breast cancer patients.

Evaluation of serum human telomerase reverse transcriptase as a novel marker for cervical cancer.

Human telomerase reverse transcriptase (hTERT) is the catalytic subunit of human telomerase and its rate-limiting component. The purpose of the present study was to investigate the diagnostic value of hTERT in serum of cervical cancer patients. Preoperative values of hTERT, squamous cell carcinoma antigen (SCC-ag) and cancer antigen 125 (CA 125) were measured by enzyme-linked immunosorbent assay (ELISA) in 192 patients with squamous cell carcinoma or adenocarcinoma of the uterine cervix and 38 healthy controls.

Enhanced xenobiotic-induced hepatotoxicity and Kupffer cell activation by restraint-induced stress.

We tested the hypothesis that environmental stress is a predisposing factor for liver injury by examining the effect of acute restraint on liver injury provoked by carbon tetrachloride (CCl4) and allyl alcohol. Mice were immobilized using Plexiglas restraint cages, producing a form of psychogenic stress, whereas other animals were allowed to roam free. Serum alanine aminotransferase levels were elevated significantly in restrained animals after administration of varying doses of CCl4 or allyl alcohol that did not produce liver injury in unrestrained animals.

Capillary electrophoretic assay of acyl-CoA hydrolase activity.

Acyl-CoA hydrolases catalyze the hydrolysis of fatty acyl CoA thioesters to free fatty acids and coenzyme A. These enzymes play an important role in the maintenance of cellular acyl-CoA and free CoASH pools and in the detoxification of nonphysiological metabolites. The assays most commonly used for acyl-CoA hydrolase quantitation are spectrophotometric and radioisotopic methods, both of which have limitations.

Hepatic enzymatic synthesis and hydrolysis of CoA esters of solvent-derived oxa acids.

Many ethylene glycol-derived solvents are oxidized to xenobiotic alkoxyacetic acids (3-oxa acids) by hepatic enzymes. The toxicity of these ubiquitous solvents has been associated with their oxa acid metabolites. For many xenobiotic carboxylic acids, the toxicity is associated with the CoA ester of the acid.