Calcium dependent cysteine proteinase is a precursor of a chemotactic factor for neutrophils.
A new chemotactic factor for neutrophils is generated from calcium dependent cysteine proteinase (calpain) I by autodigestion. An active peptide was isolated from the autodigest and its structure was determined to be an acetylated nonapeptide with the sequence: N-acetyl Ser-Glu-Glu-Ile-Ile-Thr-Pro-Val-Tyr. Compared with the entire sequence of human calpain I, the peptide was identical with the N-terminal amino acid sequence of the large subunit deduced from the cDNA sequence, except that the peptide was devoid of a methionine residue and acetylated at the N-terminus. The acetyl nonapeptide was synthesized and its chemotactic activity was reconfirmed. The biological significance and possible role of this calpain derived chemotactic factor in inflammation are discussed.
Kunimatsu
M
M
Department of Biochemistry, Nagoya City University Medical School, Japan.
Higashiyama
S
S
Sato
K
K
Ohkubo
I
I
Sasaki
M
M
D000595:Amino Acid Sequence; D002154:Calpain / Q000097:blood* / Q000235:genetics; D002630:Chemotactic Factors / Q000096:biosynthesis / Q000097:blood* / Q000302:isolation & purification; D002634:Chemotaxis, Leukocyte; D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009504:Neutrophils / Q000502:physiology*; D010196:Pancreatic Elastase / Q000097:blood
D002630:Chemotactic Factors; D010196:Pancreatic Elastase; D002154:Calpain