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Cancer Metastasis Program, Michigan Cancer Foundation, Detroit, Michigan [A. R.], and the Department of Cell Biology, The Weizmann Institute of Science, Rehovot, Israel [G. P., P. C.]
We report the complete primary and secondary structures of a metastasis-associated Mr 34,000 galactoside-binding lectin. The polypeptide sequence (264 amino acids) was derived from the nucleotide sequence of three overlapping complementary DNA clones isolated from 
gt11 and gt10 phage libraries of UV-induced murine fibrosarcomas. Striking features of the polypeptide sequence are two distinct regions of ß-sheet and globular structures at the amino and carboxy terminals, respectively. Homology search suggests that the polypeptide is a chimeric gene product formed by fusion of the 5'-end of an Mr 
14,000 galactoside-binding lectin with an internal domain of the collagen 
gene. Enzymatic treatment with collagenase confirmed the presence of a collagen-like structure in the polypeptide. Unexpectedly, the entire sequence is >85% homologous to a rat low affinity IgE-binding protein.
1 This work was supported in part by USPHS Grant CA-46120 awarded by the National Cancer Institute, Department of Health and Human Services to A. R., by a grant from the American Cancer Society to A. R., and by the Paul Zuckerman Support Foundation for Cancer Research to A. R.
2 To whom requests for reprints should be addressed, at Michigan Cancer Foundation, 110 E. Warren Ave., Detroit, MI 48201.
Received 1/10/89. Revised 3/22/89. Accepted 3/28/89.
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