Open AccessCloning and sequence analysis of cDNA clones for bovine aortic‐endothelial‐cell transglutaminase
Author(s) -
NAKANISHI Kazuo,
NARA Kiyomitsu,
HAGIWARA Hiromi,
AOYAMA Yasunori,
UENO Hiroshi,
HIROSE Shigehisa
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16338.x
Subject(s) - complementary dna , microbiology and biotechnology , cdna library , biology , northern blot , tissue transglutaminase , messenger rna , peptide sequence , biochemistry , enzyme , gene
A cDNA clone encoding transglutaminase was isolated from a bovine‐endothelial‐cell cDNA library using oligonucleotide probes designed based on partial amino acid sequences of the purified protein. Sequencing of the cDNA insert revealed an open reading frame of 2061 bp coding for a protein of 687 amino acids. The sequence of bovine endothelial‐cell transglutaminase was 88, 82, 80, 37, 37 and 37% identical with that of human endothelial, rat macrophage, guinea‐pig liver, human and rat keratinocyte transglutaminases, and the human blood‐coagulation factor XIIIa subunit, respectively. The cDNA clone was hybridized to a single mRNA species of 3.9 kb in the liver, lung, spleen and heart but not hybridized to RNA from the brain. Northern‐blot analysis of mRNA from retinoid‐treated cultured vascular endothelial cells revealed that retinoids were able to induce a large increase in the transglutaminase mRNA levels.