Molecular cloning of complementary DNA for human medullasin: an inflammatory serine protease in bone marrow cells.
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.
Okano
K
K
Basic Research Laboratories, Toray Industries, Inc., Kanagawa.
Aoki
Y
Y
Sakurai
T
T
Kajitani
M
M
Kanai
S
S
Shimazu
T
T
Shimizu
H
H
Naruto
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D001853:Bone Marrow / Q000201:enzymology*; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism*; D004262:DNA Restriction Enzymes; D006801:Humans; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000235:genetics*
D004247:DNA; D004262:DNA Restriction Enzymes; D012697:Serine Endopeptidases; C034869:medullasin