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Androgen-sensitive human prostate cancer cells, LNCaP, produce both N-terminally mature and truncated prostate-specific antigen isoforms

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Author

Summary, in English

To characterize prostate-specific antigen (PSA) produced by cancer cells, different isoforms of PSA secreted by the human prostate cancer cells, LNCaP, were purified. LNCaP-PSA production was induced by synthetic androgen, R1881. LNCaP-PSA was separated into four pools. The molecular mass of LNCaP-PSA isoforms in these pools was 34 kDa under reducing conditions and 29 kDa under nonreducing conditions on SDS/PAGE. pI of LNCaP-PSA isoforms varied from 6.8 to 8.2. Pool A had the highest specific activity, 37 nmol/(minxmg). All the pools formed stable complexes with alpha 1-antichymotrypsin and alpha 2-macroglobulin. The Fools contained 10-60% of N-terminally correctly processed LNCaP-PSA isoforms. According to the molecular modelling, the addition or deletion of two or four N-terminal amino acids could affect the three-dimensional structure and thereby remarkably reduce the enzyme activity of LNCaP-PSA.

Publishing year

1998

Language

English

Pages

329-335

Publication/Series

European Journal of Biochemistry

Volume

255

Issue

2

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Medical Genetics

Keywords

  • prostate cancer
  • N-terminal sequencing
  • molecular modeling
  • standardization
  • enzyme activity

Status

Published

ISBN/ISSN/Other

  • ISSN: 0014-2956