O. Lefebvre et al., THE MOUSE ONE P-DOMAIN (PS2) AND 2 P-DOMAIN (MSP) GENES EXHIBIT DISTINCT PATTERNS OF EXPRESSION, The Journal of cell biology, 122(1), 1993, pp. 191-198
We have previously shown that the human pS2 gene, which codes for a se
creted peptide of 60 amino acids, is expressed in a number of human ca
rcinomas, including carcinomas of the breast, the pancreas, and the la
rge bowel. Strong pS2 gene expression was also observed in the normal
gastric mucosa and in the regenerative tissues surrounding ulcerous le
sions of the gastrointestinal tract. A number of pS2 similar peptides,
designated as P-domain peptides, have been described, notably the por
cine (PSP), murine (mSP), and human (hSP) spasmolytic polypeptides, wh
ich correspond to duplicated pS2 proteins. We have now cloned a mouse
homolog of the human pS2 cDNA to dispose of an animal model to study t
he pS2 protein function, which remains unknown at the present time. We
show that the mouse putative pS2 protein sequence and the physiologic
al pattern of expression of the mouse pS2 gene are well conserved. The
mouse pS2 gene is highly expressed in the stomach mucosa cells, where
as no pS2 gene expression could be detected in the mouse mammary gland
, even during postnatal development processes dependent on growth fact
ors or hormones. Using in situ hybridization, we show that although co
expressed in the fundus, the antrum and the antrum-pyloric regions of
the stomach, the mouse pS2 and mSP genes exhibit distinct and compleme
ntary cellular patterns of expression.