Role of fluorine-18 fluoro-deoxyglucose positron emission tomography scan in the evaluation and follow-up of patients with low-grade lymphomas.

BACKGROUND: Fluorine-18 fluoro-deoxyglucose positron emission tomography (FDG-PET) scanning has excellent sensitivity and specificity for staging non-Hodgkin lymphomas, but to the authors' knowledge few studies to date have evaluated FDG-PET in low-grade lymphomas only. METHODS: A retrospective study was performed on patients with biopsy-proven nontransformed and transformed follicular lymphoma (FL), B-cell small-cell lymphocytic lymphoma (SLL/CLL), or marginal zone lymphoma (MZL) who underwent PET and computed tomography (CT) scans within 3 weeks. Standard uptake values (SUV) of all abnormal foci were measured. RESULTS: In FL, PET demonstrated 94% sensitivity and 100% specificity for staging. PET was more specific than CT for detecting recurrence or assessing therapeutic responses (91% vs. 50%). FDG avidity among patients with WHO Grades 1, 2, and 3 disease was not significantly different (analysis of variance [ANOVA]). For MZL staging, PET had moderate sensitivity (71%) and outperformed CT alone in the depiction of extranodal sites (85% vs. 57% sensitivity). In SLL/CLL, PET sensitivity was 53% and underestimated disease extent in 5 of 19 patients (26%) compared with CT. PET did not affect initial management but confirmed suspected recurrences in 75% of patients. Nontransformed FL had a higher SUV (ANOVA, P < .05) compared with MZL and SLL/CLL. SUV was higher in transformed than in nontransformed tumors (P < .001, Student t test). CONCLUSIONS: PET usefulness in staging low-grade lymphomas varies depending on histology. PET sensitivity is excellent in FL and moderate in MZL. PET is more specific than CT for follow-up in all types. PET has limited usefulness for SLL/CLL staging. However, a suggestive pattern of hazy and mild uptake was often noted in positive scans. In all low-grade lymphomas, the emergence of foci of intense uptake should raise suspicion of conversion to high-grade disease.

Regulation of calcium homeostasis by S100RVP, an androgen-regulated S100 protein in the rat ventral prostate.

BACKGROUND: S100RVP was previously identified as an androgen-response gene in the rat ventral prostate (RVP). Characterization of S100RVP is important for elucidating the function of S100 proteins in androgen action. METHODS: The expression and subcellular localization of S100RVP were determined by Northern blot, in situ hybridization, and fluorescent microscopy. Calcium overlay and calcium ionophore sensitivity assays were performed to investigate the calcium binding and function of S100RVP. RESULTS: S100RVP is abundantly expressed in the RVP epithelial cells. A green fluorescent protein(GFP)-S100RVP fusion protein is present in both the cytoplasm and nucleus of transfected cells. A GST-S100RVP fusion protein bound calcium in vitro at levels similar to known S100 proteins. Furthermore, GFP-S100RVP transfected LNCaP and PC3 cells exhibited reduced sensitivity to calcium ionophore-induced cell death, but not to UV-induced cell death. CONCLUSION: The results of this study argue for a role of S100RVP in calcium homeostasis in the prostate.

Androgen regulation of spermidine synthase expression in the rat prostate.

BACKGROUND: Spermidine synthase, an essential enzyme in the polyamine synthesis pathway, was identified as one of the androgen-response genes in the rat ventral prostate. Characterization of androgen regulation of spermidine synthase is important to the understanding of androgenic regulation of polyamine synthesis. METHODS: Full-length cDNA encoding rat spermidine synthase was isolated from a lambdaZAP cDNA phage library. Young male adult Sprague-Dawley rats were used for castration and androgen replacement. Northern blot and in situ hybridization were used to characterize gene expression. RESULTS: The amino acid sequence of rat spermidine synthase shares 99% and 94% identity with that of mouse and human spermidine synthase, respectively. Spermidine synthase gene is abundantly expressed and regulated by androgens in the ventral, dorsal, and lateral lobes of the rat prostate, and its expression is localized to the epithelial cells. Spermidine synthase also is regulated by androgens in the seminal vesicles but not in the muscle, brain, kidney, thymus, heart, or liver, suggesting that this enzyme is responsive to androgen in the male sex accessory organs only. The expression of spermidine synthase and two other enzymes involved in polyamine synthesis, S-adenosylmethionine decarboxylase and ornithine decarboxylase, are regulated by androgens coordinately. CONCLUSIONS: Spermidine synthase is most abundantly expressed and regulated by androgens in the prostatic epithelial cells, suggesting that regulation of spermidine synthase is likely a key step in coordinated androgen regulation of polyamine synthesis in the prostate.