We have isolated and sequenced a
cDNA clone encoding the mouse LAMP-1 (mLAMP-1) major
lysosomal membrane glycoprotein. The deduced
protein sequence, which included the NH2-terminal portion of the mLAMP-1 molecule, consisted of 382
amino acids (Mr 41,509). The predicted structure of this
protein included an NH2-terminal intralumenal domain consisting of two homology units of approximately 160 residues each separated by a
proline-rich hinge region. Each homology unit contained four
cysteine residues with two intercysteine intervals of 36-38 residues and one of 68 or 76 residues. The molecule also contained 20
asparagine-linked glycosylation sites within residues 1-287, a membrane-spanning region from residues 347 to 370, and a carboxyl-terminal cytoplasmic domain of 12 residues. The biochemical properties and amino acid sequence of mLAMP-1 were highly similar to those of two other molecules that have been studied as cell surface onco-
differentiation antigens: a highly sialylated
polylactosaminoglycan-containing
glycoprotein isolated from human
chronic myelogenous leukemia cells (Viitala, J., Carlsson, S. R., Siebert, P. D., and Fukuda, M. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, in press) and the mouse gp130 (P2B)
glycoprotein, in which an increase in beta 1-6 branching of
asparagine-linked
oligosaccharides has been correlated with metastatic potential in certain
tumor cells (Dennis, J.W., Laferte, S., Waghorne, C., Breitman, M.L., and Kerbel, R.S. (1987) Science 236, 582-585).