Nuclear shape and nuclear matrix protein composition in prostate and seminal vesicles

Citation
J. Pannek et al., Nuclear shape and nuclear matrix protein composition in prostate and seminal vesicles, UROLOGY, 54(5), 1999, pp. 934-939
Citations number
32
Categorie Soggetti
Urology & Nephrology
Journal title
UROLOGY
ISSN journal
00904295 → ACNP
Volume
54
Issue
5
Year of publication
1999
Pages
934 - 939
Database
ISI
SICI code
0090-4295(199911)54:5<934:NSANMP>2.0.ZU;2-K
Abstract
Objectives. The nucleus controls cell function and behavior. The nuclear ma trix determines internal nuclear changes. Two-dimensional gel electrophores is is the reference standard for the analysis of nuclear matrix protein (NM P) composition. Differences in NMP composition should therefore be reflecte d by changes in nuclear shape. We investigated the differences in NMP compo sition and nuclear morphometry of the prostate and seminal vesicles. Both t issues are androgen-dependent sex accessory organs with completely differen t biologic behavior. Methods. High-resolution two-dimensional gel electrophoresis and silver sta ining were used to evaluate NMP composition from histologically normal pros tate and seminal vesicle epithelial cells. Nuclear morphometry, performed u sing a computer-assisted image analysis system, described the distribution, variability, and extremes of nuclear shape. Results, NMP composition analysis demonstrated that both tissues have a sim ilar NMP composition, and tissue-specific NMPs that were consistently prese nt in all specimens of each tissue could not be demonstrated. Nuclear morph ometry showed a significantly greater heterogeneity in nuclear shape in the seminal vesicles than in the prostate. Conclusions. The striking similarity of the NMP composition demonstrates th e close biologic relationship between prostate and seminal vesicle tissue. The similar NMP composition does not correlate with the marked alterations in nuclear shape and structure between these tissues. Therefore, nuclear mo rphometry may depict differences in the functional state of a similar set o f NMPs, shown by two-dimensional gel electrophoresis, which may be responsi ble for the different biologic behavior of these tissues. UROLOGY 54: 934-9 39, 1999. (C) 1999, Elsevier Science Inc.