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Cloning and characterization of the α1-antichymotrypsin produced by human prostate tissue

Wu, Guan ; Lilja, Hans LU orcid ; Cockett, Abraham T.K. and Gershagen, Sten (1998) In Prostate 34(3). p.155-161
Abstract

BACKGROUND. α1-antichymotrypsin (ACT) forms stable complexes with prostate-specific antigen (PSA), a serine protease, and this complex is the major form of PSA in the blood circulation. α1-antichymotrypsin occurs in the blood in approximately 105 molar excess to PSA, mainly due to hepatic production, but local prostatic production of ACT has been demonstrated by immunohistochemistry and in situ hybridization. The present study was performed to further characterize this prostate-produced ACT. METHODS. The nucleotide structure of the prostatic transcript was determined from ACT coding clones isolated from prostatic cDNA. The occurrence of a prostatic ACT transcript was analyzed by Northern blot. RT-PCR was... (More)

BACKGROUND. α1-antichymotrypsin (ACT) forms stable complexes with prostate-specific antigen (PSA), a serine protease, and this complex is the major form of PSA in the blood circulation. α1-antichymotrypsin occurs in the blood in approximately 105 molar excess to PSA, mainly due to hepatic production, but local prostatic production of ACT has been demonstrated by immunohistochemistry and in situ hybridization. The present study was performed to further characterize this prostate-produced ACT. METHODS. The nucleotide structure of the prostatic transcript was determined from ACT coding clones isolated from prostatic cDNA. The occurrence of a prostatic ACT transcript was analyzed by Northern blot. RT-PCR was used to detect ACT transcripts in cultured prostatic cancer cells. RESULTS. Screening of two prostatic cDNA libraries showed the frequency of ACT transcripts to be about 1 clone in 40,000. The cDNA sequence of prostatic ACT is identical to that of the previously published hepatic ACT. Northern blot analysis of mRNA extracted from prostatic tissue showed a single transcript of approximately 1.5 kb. RT-PCR analysis demonstrated an ACT transcript in cultured prostatic cancer cells. CONCLUSIONS. In this study we provide further evidence for a local, prostatic production of ACT. The cDNA sequence data suggest that the peptide backbone of prostatic ACT is identical to the protein derived from the liver, and thus may be functional as a protease inhibitor.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
BPH, Prostate cancer, Protease inhibitors, PSA
in
Prostate
volume
34
issue
3
pages
7 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • pmid:9492842
  • scopus:0031960939
ISSN
0270-4137
DOI
10.1002/(SICI)1097-0045(19980215)34:3<155::AID-PROS1>3.0.CO;2-H
language
English
LU publication?
yes
id
006d164f-1046-4a2a-b66f-5805e8a2571b
date added to LUP
2022-12-06 15:55:29
date last changed
2024-02-02 06:19:38
@article{006d164f-1046-4a2a-b66f-5805e8a2571b,
  abstract     = {{<p>BACKGROUND. α<sub>1</sub>-antichymotrypsin (ACT) forms stable complexes with prostate-specific antigen (PSA), a serine protease, and this complex is the major form of PSA in the blood circulation. α<sub>1</sub>-antichymotrypsin occurs in the blood in approximately 10<sup>5</sup> molar excess to PSA, mainly due to hepatic production, but local prostatic production of ACT has been demonstrated by immunohistochemistry and in situ hybridization. The present study was performed to further characterize this prostate-produced ACT. METHODS. The nucleotide structure of the prostatic transcript was determined from ACT coding clones isolated from prostatic cDNA. The occurrence of a prostatic ACT transcript was analyzed by Northern blot. RT-PCR was used to detect ACT transcripts in cultured prostatic cancer cells. RESULTS. Screening of two prostatic cDNA libraries showed the frequency of ACT transcripts to be about 1 clone in 40,000. The cDNA sequence of prostatic ACT is identical to that of the previously published hepatic ACT. Northern blot analysis of mRNA extracted from prostatic tissue showed a single transcript of approximately 1.5 kb. RT-PCR analysis demonstrated an ACT transcript in cultured prostatic cancer cells. CONCLUSIONS. In this study we provide further evidence for a local, prostatic production of ACT. The cDNA sequence data suggest that the peptide backbone of prostatic ACT is identical to the protein derived from the liver, and thus may be functional as a protease inhibitor.</p>}},
  author       = {{Wu, Guan and Lilja, Hans and Cockett, Abraham T.K. and Gershagen, Sten}},
  issn         = {{0270-4137}},
  keywords     = {{BPH; Prostate cancer; Protease inhibitors; PSA}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{3}},
  pages        = {{155--161}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Prostate}},
  title        = {{Cloning and characterization of the α<sub>1</sub>-antichymotrypsin produced by human prostate tissue}},
  url          = {{http://dx.doi.org/10.1002/(SICI)1097-0045(19980215)34:3<155::AID-PROS1>3.0.CO;2-H}},
  doi          = {{10.1002/(SICI)1097-0045(19980215)34:3<155::AID-PROS1>3.0.CO;2-H}},
  volume       = {{34}},
  year         = {{1998}},
}