Metaplasia of the duodenum shows a Helicobacter pylori-correlated differentiation into gastric-type protein expression.
The origin of gastric metaplasia of the duodenum (GMD) remains enigmatic. We studied expression of mucins and trefoil peptides in GMD to gain insight into its phenotype and origin. We examined duodenal tissue of 95 patients (0 to 83 years old, 26 with gastric Helicobacter pylori infection) for the presence of GMD. Expression was examined immunohistochemically of secretory mucins (MUC2, MUC5AC, MUC5B, and MUC6), trefoil peptides (TFF1, TFF2, and TFF3), and sucrase-isomaltase (SI). GMD, found in 37 patients, correlated positively to gastric H. pylori infection, age, and villus atrophy. MUC2 and TFF3, expressed in normal goblet cells, were absent from 100% and 87% of GMD, respectively. GMD ubiquitously expressed MUC5AC, whereas MUC5AC expression in adjacent goblet cells was closely correlated with the extent of GMD. TFF1, TFF2, and MUC6 were found in 84%, 92%, and 65% of GMD, respectively. MUC5B was absent from epithelium and GMD. SI, expressed by villus enterocytes, was absent from GMD. Brunner's glands ubiquitously expressed MUC5B, MUC6, and TFF2. GMD was characterized by the expression of gastric-type proteins MUC5AC, MUC6, TFF1, and TFF2 and the absence of intestinal markers MUC2, TFF3, and SI. In terms of the location of metaplastic cells, our results suggest that epithelial cells migrating toward villus tips switch to gastric-type secretory cells. Positive correlation with infection suggests an inductive role H. pylori in the development of GMD.
Van De Bovenkamp
Jeroen H B
JH
Laboratory of Pediatrics, Erasmus MC/Sophia Children's Hospital, Rotterdam, The Netherlands.
Korteland-Van Male
Anita M
AM
Büller
Hans A
HA
Einerhand
Alexandra W C
AW
Dekker
Jan
J
D000293:Adolescent; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000375:Aging; D002011:Brunner Glands / Q000737:chemistry; D002454:Cell Differentiation; D002648:Child; D002675:Child, Preschool; D004386:Duodenum / Q000737:chemistry* / Q000473:pathology*; D005753:Gastric Mucosa / Q000473:pathology*; D020397:Goblet Cells / Q000737:chemistry; D006133:Growth Substances / Q000032:analysis; D016481:Helicobacter Infections / Q000473:pathology*; D016480:Helicobacter pylori; D006801:Humans; D007223:Infant; D008679:Metaplasia; D008875:Middle Aged; D055271:Mucin 5AC; D055262:Mucin-2; D055257:Mucin-5B; D055272:Mucin-6; D009077:Mucins / Q000032:analysis*; D009124:Muscle Proteins; D009479:Neuropeptides; D010455:Peptides / Q000032:analysis*; D011506:Proteins / Q000032:analysis; D013272:Stomach Diseases / Q000382:microbiology / Q000473:pathology; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins
D006133:Growth Substances; C524625:MUC2 protein, human; C524678:MUC5AC protein, human; C524578:MUC5B protein, human; C524734:MUC6 protein, human; C524628:Muc2 protein, rat; C524680:Muc5ac protein, rat; C524736:Muc6 protein, rat; D055271:Mucin 5AC; D055262:Mucin-2; D055257:Mucin-5B; D055272:Mucin-6; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D010455:Peptides; D011506:Proteins; C051838:TFF1 protein, human; C000604007:TFF2 protein, human; C082495:TFF3 protein, human; C099037:TFF3 protein, rat; C000604008:Tff2 protein, rat; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins