Androgen‐sensitive human prostate cancer cells, LNCaP, produce both N‐terminally mature and truncated prostate‐specific antigen isoforms
Open Access
- 15 July 1998
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 255 (2) , 329-335
- https://doi.org/10.1046/j.1432-1327.1998.2550329.x
Abstract
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 non‐reducing 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/(min×mg). All the pools formed stable complexes with α1‐antichymotrypsin and α2‐macroglobulin. The pools 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.Keywords
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