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Isolation and sequencing of a cDNA clone encoding 107 kDa sialoglycoprotein in rat liver lysosomal membranes
Author(s) -
Himeno Masaru,
Noguchi Youichiro,
Sasaki Hiroyuki,
Tanaka Yoshitaka,
Furuno Koji,
Kono Akira,
Sakaki Yoshiyuki,
Kato Keitaro
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80561-7
Subject(s) - complementary dna , biology , sialoglycoprotein , microbiology and biotechnology , open reading frame , peptide sequence , northern blot , biochemistry , amino acid , cdna library , glycoprotein , sialoglycoproteins , gene
A cDNA for 107 kDa sialoglycoprotein (LGP 107), the major protein component of rat liver lysosomal membranes, was isolated and sequenced. The 1.8 kbp cDNA contained an open reading frame encoding a polypeptide consisting of 386 amino acid residues ( M r 41914). The deduced NH 2 ‐terminal 10‐residue sequence is identical with that determined for purified LGP 107. The primary structure deduced for LGP 107 contains 20 potential N ‐glycosylation sites and exhibits 82.5, 43 and 60% sequence similarities to mouse LAMP‐1, chicken LEP 100, and a 120‐kDa human lysosomal glycoprotein, respectively. Among these lysosomal glycoproteins, the amino acid sequence of the putative transmembrane segment is highly conserved. Northern blot hybridization analysis identified a single species of LGP 107 mRNA (2.1 kbp in length) in rat liver, kidney, brain, lung, spleen, heart and pancreas, although its level in pancreas was very low.