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Surfactant protein A (SP-A) is the most abundant protein
associated with phospholipids in pulmonary surfactant. There are
several lines of evidence that pulmonary and gastrointestinal
epithelium produce closely related surface-active materials, although
the presence of SP-A in gastrointestinal tract has so far not been
reported. Indirect immunofluorescence experiments using different
antibodies raised against rat pulmonary SP-A showed that some jejunal
and colonic but not gastric epithelial cells positively stained for
SP-A. Analysis of the proteins in cell lysates from rat small intestine
and colon studied by Western blot revealed several immunoreactive
bands, including the characteristic triplet of 26-, 32-, and 38-kDa
monomeric proteins, less strongly labeled than in lung cells, and
higher molecular mass forms of 66 and 120 kDa also present in lung
cells. The 66- and 120-kDa bands displayed the expected isoelectric pH
of SP-A after two-dimensional electrophoresis. Alkylation induced
conversion of the 120-kDa form (almost completely) and the 66-kDa form
(partly) into the 26-38-kDa monomeric species. The presence of
SP-A mRNA in rat stomach, small intestine, and colon was then searched
for by conventional cDNA/reverse transcriptase-polymerase chain
reaction. Products of appropriate size (372 base pairs) identical to
that of pulmonary tissue were amplified in small intestine and colon
but not in stomach or in other tissues used as controls. Cloning and
sequencing of rat colon SP-A cDNA revealed the same sequence as the one
reported for rat lung SP-A. Furthermore, analysis of the
transcriptional initiation site of SP-A gene in colon by
anchored-polymerase chain reaction showed that transcription was
initiated at the same site in both colon and lung. These data, which
demonstrate that small intestine and colon express SP-A constitutively
and that this protein is present in some epithelial cells, extend the
concept of intestinal surfactant and underline its close relationships
to pulmonary surfactant.
Volume 270,
Number 20,
Issue of May 19, pp. 12162-12169, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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