title: Reduction of QM protein expression correlates with tumor grade in prostatic adenocarcinoma.
abstract: The QM protein is a transcription cofactor inhibiting the activity of AP-1 transcription factors and is also a ribosomal protein participating in protein synthesis. While protein synthesis is known to be increased in many cancers, inhibition of AP-1 activity presumably suppresses development and growth of sex-hormone-regulated tumor cells. The present study is the first report on immunohistochemical data of QM in human prostatic tissues. Paraffin sections of human prostate cancer samples were immunohistochemically stained for QM. The staining scores were analyzed with the clinicopathologic data of the patients. QM protein expression was found in all normal prostate glands adjacent to prostate cancer and in various intraepithelial neoplasia (PIN). In prostate cancer, the staining intensity and stained areas were decreased, compared to the normal glands and PIN lesions; in high-grade tumors only some patches of tumor cells showed positivity. Intense (3+) staining was mostly observed in the Gleason grade three areas (48%) compared to grade 4 and 5 areas (22%), although both low and high-grade tumors showed similar percentages of weakly stained areas. Moreover, staining in prostatic adenocarcinoma was often topographically patchy and varied from negative or weak (1+) to intense (3+). There was an inverse correlation from normal to low-grade tumors and then to high-grade tumors. However, in high-grade tumors, the positive areas were mostly confined to peripheral aspects of tumors and were particularly strong in foci of perineural invasion. This preliminary study suggests that decreased QM expression may be associated with early development of prostate cancer, but later a high level of QM may facilitate progression of the tumors to a more aggressive phenotype.
authors.affiliation: Department of Pathology, Harper University Hospital and Wayne State University, and Karmanos Cancer Institute, Detroit, MI, USA.
authors.forename: G
authors.initials: G
authors.lastname: Altinok
authors.forename: I J
authors.initials: IJ
authors.lastname: Powell
authors.forename: M
authors.initials: M
authors.lastname: Che
authors.forename: K
authors.initials: K
authors.lastname: Hormont
authors.forename: F H
authors.initials: FH
authors.lastname: Sarkar
authors.forename: W A
authors.initials: WA
authors.lastname: Sakr
authors.forename: D
authors.initials: D
authors.lastname: Grignon
authors.forename: D J
authors.initials: DJ
authors.lastname: Liao
mesh_terms: D000230:Adenocarcinoma / Q000378:metabolism* / Q000473:pathology; D000328:Adult; D000368:Aged; D006801:Humans; D008297:Male; D008875:Middle Aged; D009361:Neoplasm Invasiveness / Q000473:pathology; D009367:Neoplasm Staging; D019048:Prostatic Intraepithelial Neoplasia / Q000378:metabolism* / Q000473:pathology; D011471:Prostatic Neoplasms / Q000378:metabolism* / Q000473:pathology; D000080882:Ribosomal Protein L10; D012269:Ribosomal Proteins / Q000378:metabolism*; D025521:Tumor Suppressor Proteins / Q000378:metabolism*
chemical_list: C000630686:RPL10 protein, human; D012269:Ribosomal Proteins; D025521:Tumor Suppressor Proteins