Open AccessIdentification of calreticulin isoforms in the central nervous system
Author(s) -
Susan Treves,
Francesco Zorzato,
Tullio Pozzan
Publication year - 1992
Publication title -
biochemical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.706
H-Index - 265
eISSN - 1470-8728
pISSN - 0264-6021
DOI - 10.1042/bj2870579
Subject(s) - calreticulin , biology , gene isoform , xenopus , kdel , endoplasmic reticulum , signal peptide , complementary dna , peptide sequence , clone (java method) , microbiology and biotechnology , glycosylation , genetics , gene , golgi apparatus
In the present paper we report the cloning and sequencing of the cDNA encoding two calreticulin isoforms from Xenopus laevis central nervous system. The two isoforms display 93% identity at the amino acid level. The predicted amino acid sequences of the amphibian calreticulins are very similar (76%) to those of mammalian liver and skeletal muscle. Xenopus laevis calreticulins are characterized by a very acidic c-terminal domain endowed with the endoplasmic-reticulum retention signal KDEL. The cDNAs of both clones encode an N-glycosylation consensus sequence. A third clone of calreticulin was also identified. The restriction map of this clone was clearly distinct from that of the two sequenced clones. These results indicate the existence of multiple calreticulin isoforms in the central nervous system and open questions about their functional role in different cells and/or subcellular compartments.