Cell cycle phases of two human lung tumor cell lines derived from squamous cell carcinoma and pulmonary metastasis of a rhabdomyosarcoma (HS 24 and HS 57) and N-acetylalanine aminopeptidase activity.

Abstract

The cell cycle phase distribution of two human lung cancer cell lines (HS 24 and HS 57) grown both to half-confluency and confluency was determined. Both cell lines were then synchronized by applying a thymidine block forcing them to stay in the S-phase. After removal of the thymidine block, which allows the cells to go then through their cell cycle phases, N-acylamino acylpeptide hydrolase (EC 3.4.19.1) activity was measured using N-acetylalanine-p-nitroanilide as substrate (N-acetylalanine aminopeptidase). At the same times that the enzymatic activity was measured, the cell cycle phase distribution was analyzed, in order to determine the cell cycle phase of N-acetylalanine aminopeptidase synthesis. However, the cell cycle phase of N-acetylalanine aminopeptidase synthesis could not be determined. This result was caused by the fact that the cells remained synchronous only for a short period of time.

• Authors: O L Schoenberger, S Beikirch
• Journal: Cancer biochemistry biophysics (Cancer Biochem Biophys) Vol. 10 Issue 4 Pg. 337-43 (Oct 1989) ISSN: 0305-7232 [Print] England
• PMID: 2695238 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Neoplasm Proteins
• Peptide Hydrolases
• acylaminoacyl-peptidase

Topics

• Carcinoma, Squamous Cell (enzymology, pathology)
• Cell Cycle
• Enzyme Induction
• Gene Expression Regulation, Neoplastic
• Humans
• Lung Neoplasms (enzymology, pathology, secondary)
• Neoplasm Proteins (analysis)
• Peptide Hydrolases (analysis)
• Rhabdomyosarcoma (enzymology, pathology, secondary)
• Tumor Cells, Cultured (enzymology, pathology)