ISSN:
1432-069X
Keywords:
Calpain
;
Transglutaminase
;
Thrombin
;
Dimethyl sulfoxide
;
Heating
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Summary Two transglutaminases (TGase) with estimated molecular weight of 55,000 (55-K TGase) and 120,000 (120-K TGase) were partially purified from the cytosolic fraction of porcine skin (epidermis-rich preparation) using DEAE-cellulose and gel-filtration chromatographies. The enzyme activities of both trans-glutaminases were enhanced more than 20-fold by treatment with calpain (Ca2+-dependent cysteine proteinase) in the presence of Ca2+, and this enhancement was inhibited by adding EDTA, leupeptin, or an endogenous calpain-specific inhibitor protein (calpastatin). 55-K TGase was effectively activated by a smaller amount of calpain than was 120-K TGase, while known activating reagents such as thrombin and dimethyl sulfoxide or heat treatment preferentially activated 120-K TGase. One of the physiological functions of calpain in the epidermis may be the activation of epidermal transglutaminases.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00426618
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