Compartmentation and glycoprotein substrates of calpain in the developing rat brain.
An activated form of calpain I associates with telencephalic membranes in a developmentally regulated fashion during early postnatal ontogeny. During this period, the cytoskeletal component spectrin is available and appears to be differentially susceptible to calpain-mediated cleavage. Lectin blotting techniques demonstrated that the leupeptin-sensitive action of calpain is primarily directed toward large proteins which are glycoconjugate in nature; neuronal cell adhesion molecules are among the glycoproteins whose associations with the telencephalic membranes decrease due to calpain activity. These data suggest that cytoplasmic calpain is translocated to the membrane during early brain development in order to act on the cytoskeletal and adhesive structures responsible in part for neuronal shape and function.
Sheppard
A
A
Center for the Neurobiology of Learning and Memory, University of California, Irvine 92717-3800.
Wu
J
J
Bahr
B A
BA
Lynch
G
G
D000818:Animals; D000831:Animals, Newborn / Q000254:growth & development / Q000378:metabolism*; D001921:Brain / Q000254:growth & development / Q000378:metabolism*; D002154:Calpain / Q000737:chemistry / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D007158:Immunologic Techniques; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility; D013687:Telencephalon / Q000378:metabolism
D006023:Glycoproteins; D002154:Calpain