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Structure of the guinea pig neutrophil cationic peptide gene
Author(s) -
Nagaoka Isao,
Someya Akimasa,
Iwabuchi Kazuhisa,
Yamashita Tatsuhisa
Publication year - 1992
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(92)80471-r
Subject(s) - guinea pig , cationic polymerization , peptide , chemistry , gene , microbiology and biotechnology , biology , biochemistry , genetics , organic chemistry
Guinea pig neutrophils contain the antimicrobial cationic peptides GNCP‐1 and GNCP‐2 in the granules. In this study, the GNCP gene was isolated, and the structure was characterized. Using cDNA probes, one phage clone was isolated from a guinea pig genomic library. The gene spanned > 3 kb, and comprised three exons and two introns. Sequence analysis revealed that the gene encoded GNCP‐2. Exon 1 mainly coded for the 5′ untranslated region, exon 2 coded for the prepro‐peptide region of GNCP‐2, and exon 3 coded for the mature peptide region of GNCP‐2 and the 3′ untranslated region. Primer extension analysis indicated that the transcription initiation site was located to a thymidine residue, 93 bp upstream of the ATG initiation codon or GNCP‐2 mRNA. A possible TATA box was located 24 bp upstream or the transcription start site. Interestingly, the pyrimidine‐rich sequences identified in the promoter regions of the human neutrophil elastase and myeloperoxidase genes were also found in the 5′ flanking region of the GNCP‐2 gene.