Trefoil peptide gene expression in gastrointestinal epithelial cells in inflammatory bowel disease.
BACKGROUND
This work expands on recent observations that the trefoil peptides pS2 and human spasmolytic polypeptide (hSP) are expressed in the ulceration-associated cell lineage (UACL) glands developing in chronic ulcerative conditions.


METHODS
Trefoil peptide expression in small intestinal Crohn's disease was examined by in situ hybridization to reveal sites of expression of the messenger RNAs encoding pS2 and hSP and by immunohistochemistry and immunoelectron microscopy to localize the peptides in the UACL and adjacent goblet and neuroendocrine cells.


RESULTS
Goblet cells near the UACL expressed pS2 messenger RNA and peptide; ultrastructural immunolocalization revealed pS2 copackaged within mucous cell granules. Neuroendocrine cell hyperplasia was marked in crypts near the UACL; pS2 was copackaged with the neuroendocrine granules.


CONCLUSIONS
Copackaging of a secretory protein, pS2, in both mucous and neuroendocrine granules, which have different functions, is unusual and indicates an important role for pS2 in the secretory process itself or as a ligand delivered to its receptors via different routes. It is concluded that trefoil peptides are of considerable potential functional importance in inflammatory bowel disease.
Wright
N A
NA
Department of Histopathology, Royal Postgraduate Medical School, London, England.
Poulsom
R
R
Stamp
G
G
Van Noorden
S
S
Sarraf
C
C
Elia
G
G
Ahnen
D
D
Jeffery
R
R
Longcroft
J
J
Pike
C
C
D002460:Cell Line; D004064:Digestive System / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology*; D004848:Epithelium / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology; D066246:ErbB Receptors / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D015212:Inflammatory Bowel Diseases / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins / Q000235:genetics*; D009479:Neuropeptides; D009490:Neurosecretory Systems / Q000378:metabolism / Q000473:pathology; D010455:Peptides / Q000235:genetics*; D011506:Proteins; D012333:RNA, Messenger / Q000378:metabolism; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins
D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins; D009479:Neuropeptides; D010455:Peptides; D011506:Proteins; D012333:RNA, Messenger; C051838:TFF1 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; C034407:pancreatic spasmolytic polypeptide; D066246:ErbB Receptors