Distribution of calcium-activated neutral protease inhibitor in the central nervous system of the rat.
The ubiquitous existence of calcium-activated neutral protease (CANP, calpain), an enzyme whose activity is regulated by calcium ions and a specific endogenous CANP inhibitor (calpastatin), is well known. Although there has been much investigation concerning the distribution and role of CANP, investigations of the distribution of the CANP inhibitor using immunohistochemical techniques are rare. We made antiserum against a 40K fragment of cDNA corresponding to two C-terminal repeats of rat liver CANP inhibitor expressed in Escherichia coli. Using this antiserum, we examined the distribution of CANP inhibitor in the rat central nervous system by the ABC technique and compared it with the distribution of CANP. Neurons and glias were stained, with the cytosol stained diffusely and the cell membranes stained clearly and strongly. Axons and myelin were stained faintly, but nuclei and vessels were not stained. The distribution of CANP inhibitor was thus found to be similar to that of CANP.
Kamakura
K
K
Third Department of Internal Medicine, National Defence Medical College, Saitama, Japan.
Ishiura
S
S
Imajoh
S
S
Nagata
N
N
Sugita
H
H
D000818:Animals; D001360:Avidin; D001710:Biotin; D001921:Brain / Q000033:anatomy & histology / Q000378:metabolism; D002490:Central Nervous System / Q000033:anatomy & histology / Q000378:metabolism*; D002848:Chromatography, DEAE-Cellulose; D006023:Glycoproteins / Q000378:metabolism*; D006168:Guinea Pigs; D007150:Immunohistochemistry; D051381:Rats; D013116:Spinal Cord / Q000033:anatomy & histology / Q000378:metabolism
D006023:Glycoproteins; C039304:calpain inhibitors; D001360:Avidin; D001710:Biotin