Description
Antipain is a protease inhibitor originally isolated from actinomycetes. It inhibits thrombokinase, plasmin, trypsin, and papain
in vitro (IC
50s = 20, 93, 0.26, and 0.16 μg/ml, respectively). Antipain (6-600 μg/ml) inhibits the morphological transformation of and increases frequency of chromosomal aberrations in Syrian hamster embryo cells induced by N-methyl-N''-nitro-N-nitroso-guanidine (MNNG).
In vivo, antipain (25-100 mg/kg) suppresses urethan-induced formation of cleft palates and cleft lips in mice.
Uses
Antipain inhibits trypsin, papain, and catherpsins A and B (a reversible inhibitor of cysteine and serine proteases). It is used to evaluate the role of proteases in cell transformations. It is used to help identify new proteases.
Uses
Concentrations for 50% inhibition (μg/ml): papain, 0.16trypsin, 0.26cathepsin A, 1.19cathepsin B, 0.59cathepsin D, 125plasmin, >93chymotrypsin and pepsin, >250It also has been reported to inhibit calpain I, (porcine) with Ki = 1.4 μM
General Description
Antipain is a protease inhibitor isolated from actinomycetes. It inhibits thrombokinase and blood coagulation.
Biochem/physiol Actions
Reversible inhibitor of serine/cysteine proteases and some trypsin-like serine proteases. Its action resembles leupeptin; however, its plasmin inhibition is less and its cathepsin A inhibition is more than that observed with leupeptin. Chronic administration of antipain can reduce the frequency of chemically induced transformation in BALB/c-/3T3 cells.
in vivo
The intact, cycling female mice received subcutaneous injections of Antipain dihydrochloride (3 mg) for 16 days, their uteri shows significant diminution in weight and total DNA when compared to untreated controls[4].
Antipain dihydrochloride (100 μg/g body wt; i.p.; at 12h intervals from 0 to 120 h or 240 to 360 h) shows inhibitory effect on Urethane-induced lung neoplasia in mice[5].
References
[1] UMEZAWA H. Structures and activities of protease inhibitors of microbial origin.[J]. Methods in enzymology, 1976, 45: 678-695. DOI:
10.1016/s0076-6879(76)45058-9[2] T GOTOH. Proteolytic activity and recombinant protein production in virus-infected Sf-9 insect cell cultures supplemented with carboxyl and cysteine protease inhibitors.[J]. Journal of bioscience and bioengineering, 2001, 92 3: 248-255. DOI:
10.1263/jbb.92.248[3] K. HOCKENSMITH. Identification and characterization of a chymotrypsin-like serine protease from periodontal pathogen, Tannerella forsythia[J]. Microbial pathogenesis, 2016, 100: Pages 37-42. DOI:
10.1016/j.micpath.2016.08.041[4] AMIN N M. Proteinases in Naegleria Fowleri (strain NF3), a pathogenic amoeba: a preliminary study.[J]. Tropical biomedicine, 2004, 21 2: 57-60.
[5] YUJI MORIYASU Yuko I. Use of protease inhibitors for detecting autophagy in plants.[J]. Methods in enzymology, 2008, 451: 557-580. DOI:
10.1016/s0076-6879(08)03232-1
