title: Detection of alkaline sphingomyelinase activity in human stool: proposed role as a new diagnostic and prognostic marker of colorectal cancer.
abstract: OBJECTIVE
  Intestinal alkaline sphingomyelinase, by exerting a major role in dietary sphingomyelin digestion, is responsible for the generation of messengers able to trigger the rapid turnover and apoptosis in intestinal epithelial cells. Markedly reduced mucosal alkaline sphingomyelinase activity has been associated with human colorectal neoplasms. The aim of this study was to analyze the alkaline sphingomyelinase activity in feces from healthy subjects and colorectal adenocarcinoma patients and to correlate it with the enzyme activity in intestinal tissues.
  
  
  METHODS
  The enzyme activity was measured both in the intestinal samples from 12 healthy controls and 51 patients with colorectal adenocarcinoma (tumoral and paratumoral tissue) and in the fecal samples of 34 healthy subjects and 29 patients with adenocarcinoma. The relation between sphingomyelinase activity and Dukes' stage, cell differentiation degree, age, and gender was also analyzed.
  
  
  RESULTS
  Alkaline sphingomyelinase was significantly decreased (P < 0.001; mean reduction >90%) in tumoral intestinal mucosa of patients compared with controls independently of Dukes' stage and tumor differentiation grade. Interestingly, the enzyme activity in histologically normal paratumoral tissues was statistically lower than control samples (P < 0.001). As occurs in neoplastic tissues, a relevant mean reduction (P < 0.0001; almost 90%) of alkaline sphingomyelinase was revealed in stool samples from tumor patients when compared with controls.
  
  
  CONCLUSIONS
  These findings may have implications for cancer biology and perhaps also for the design of clinical test, thus suggesting that the fecal sphingomyelinase activity could really reflect the human intestinal mucosa enzyme level and could represent a new marker for human colorectal adenocarcinoma, mainly taking into account its early appearance in intestinal neoplasms.
authors.affiliation: Department of Drug Science, University of L'Annunzio, Chieti, Italy.
authors.forename: Luisa
authors.initials: L
authors.lastname: Di Marzio
authors.forename: Alfredo
authors.initials: A
authors.lastname: Di Leo
authors.forename: Benedetta
authors.initials: B
authors.lastname: Cinque
authors.forename: Donatella
authors.initials: D
authors.lastname: Fanini
authors.forename: Alessio
authors.initials: A
authors.lastname: Agnifili
authors.forename: Pasquale
authors.initials: P
authors.lastname: Berloco
authors.forename: Michele
authors.initials: M
authors.lastname: Linsalata
authors.forename: Dionigi
authors.initials: D
authors.lastname: Lorusso
authors.forename: Michele
authors.initials: M
authors.lastname: Barone
authors.forename: Claudio
authors.initials: C
authors.lastname: De Simone
authors.forename: Maria Grazia
authors.initials: MG
authors.lastname: Cifone
mesh_terms: D000230:Adenocarcinoma / Q000175:diagnosis / Q000201:enzymology* / Q000473:pathology; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D016022:Case-Control Studies; D015179:Colorectal Neoplasms / Q000175:diagnosis / Q000201:enzymology* / Q000473:pathology; D005243:Feces / Q000201:enzymology*; D005260:Female; D006801:Humans; D008297:Male; D008875:Middle Aged; D013108:Sphingomyelin Phosphodiesterase / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D013108:Sphingomyelin Phosphodiesterase