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Development, Vol 107, Issue 3 643-650, Copyright © 1989 by Company of Biologists
JOURNAL ARTICLES |
JA McMahon and AP McMahon
Department of Cell and Developmental Biology, Roche Institute of Molecular Biology, Nutley, New Jersey 07110.
cDNA clones encoding the murine int-1-related protein (m-irp) were isolated from an 8.5-day mouse embryo library. m-irp and its human counterpart, h-irp, share extensive nucleotide homology in coding (92%) and 3' untranslated (69%) regions. At the amino acid level, m-irp and h-irp share 97% of amino acids including all 24 cysteine residues, which are highly conserved among members of the int-1 family. However, in contrast to h-irp and int-1, the predicted m-irp protein sequence did not contain a signal peptide sequence. Analysis of polymerase chain reaction, amplified cDNA, and genomic sequences strongly suggests that a single-base substitution has created a new 5' splice site 17 bp 5' of a highly conserved splice site. Splicing at this new site generates a mRNA-encoding an amino-terminal truncated protein. Splicing at the conserved splice site generates a mRNA species encoding a protein with a signal peptide sequence similar to h-irp. Close linkage between m-irp and the met oncogene maps m-irp sequences to proximal mouse chromosome 6. Adult and fetal expression of m-irp was examined by RNA blot analysis. Adult expression of m-irp is restricted to lungs and heart, and fetal expression, to placental tissue and to all stages of fetal development examined. In situ hybridization localized early fetal m-irp expression to the pericardium of the heart, to the umbilicus and associated allantoic mesoderm, and to the ventral lateral mesenchyme tissue surrounding the umbilical vein in the fetus. These results suggest a role for m-irp in the development of fetal allantoic communication.
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