Neutrophil chemotactic activity of N-terminal peptides from the calpain small subunit.
On the basis of previous findings that N-acetyl nonapeptide from the human calpain I large subunit has chemotactic activity for neutrophils, a series of peptides with the N-terminal sequence of the calpain small subunit were synthesized and their chemotactic activity was examined. Potent activity was found in N-acetyl tetra, hepta, octa, nona and a larger peptide of 13 residues, although N-acetyl tripeptide showed only weak activity and N-acetyl penta and hexa peptides showed almost no activity. Since the small subunit is identical in calpains I and II, the results indicate that both calpains could be precursor proteins of chemotactic factors for neutrophils.
Kunimatsu
M
M
Department of Biochemistry, Nagoya City University Medical School, Japan.
Ma
X J
XJ
Nishimura
J
J
Baba
S
S
Hamada
Y
Y
Shioiri
T
T
Sasaki
M
M
D000595:Amino Acid Sequence; D002154:Calpain; D002630:Chemotactic Factors; D002634:Chemotaxis, Leukocyte; D004305:Dose-Response Relationship, Drug; D006801:Humans; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000502:physiology*; D010446:Peptide Fragments / Q000138:chemical synthesis
D002630:Chemotactic Factors; D010446:Peptide Fragments; D002154:Calpain