Molecular cloning of complementary DNA for human medullasin: an inflammatory serine protease in bone marrow cells.

Article Details

Citation

Okano K, Aoki Y, Sakurai T, Kajitani M, Kanai S, Shimazu T, Shimizu H, Naruto M

Molecular cloning of complementary DNA for human medullasin: an inflammatory serine protease in bone marrow cells.

J Biochem. 1987 Jul;102(1):13-6.

PubMed ID
2822677 [ View in PubMed
]
Abstract

Medullasin, an inflammatory serine protease in bone marrow cells, modifies the functions of natural killer cells, monocytes, and granulocytes. We have cloned a medullasin cDNA from a human acute promyelocytic cell (ML3) cDNA library using oligonucleotide probes synthesized from the information of N-terminal amino acid sequence of natural medullasin. The cDNA contained a long open reading frame encoding 237 amino acid residues beginning from the second amino acid of natural meduallasin. The deduced amino acid sequence of medullasin shows a typical serine protease structure, with 41% homology with pig elastase 1.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Neutrophil elastaseP08246Details