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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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 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.

Detaljer

Författare
Externa organisationer
  • External Organization - Unknown
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Medicinsk genetik

Nyckelord

Originalspråkengelska
Sidor (från-till)329-335
TidskriftEuropean Journal of Biochemistry
Volym255
Utgåva nummer2
StatusPublished - 1998
PublikationskategoriForskning
Peer review utfördJa
Externt publiceradJa