Murine expressed sequence tags (EST) showing homology with chondromodulin-I
(ChM-I) were identified. Cloning of the full-length cDNA revealed a novel
protein (317 amino acid residues) having a domain homologous to ChM-I, and
we termed it tenodmoulin (TeM), The predicted amino acid sequence revealed
33% overall identity with mouse ChM-I precursor. Overall structural feature
s were conserved well in TeM, including a single transmembrane domain at th
e N-terminal region and the putative antiangiogenic domain with eight cyste
ine residues. However, TeM lacked a hormone-processing signal present in th
e ChM-I precursor, suggesting that it may function as a type II transmembra
ne protein on cell surface. TeM transcript (1.4 kb in size) was detected in
skeletal muscle by Northern blot analysis. In situ hybridization analysis
revealed that the expression of TeM mRNA was not associated with muscle fib
ers, but was tightly associated with epimysium and tendon, both of which ar
e classified as dense connective tissue having little vascularity. (C) 2001
Academic Press.