Compartmentation and glycoprotein substrates of calpain in the developing rat brain

✍ Scribed by Allan Sheppard; Justina Wu; Ben A. Bahr; Gary Lynch

• Book ID: 104600397
• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: English
• Weight: 948 KB
• Volume: 9
• Category: Article
• ISSN: 0887-4476
• DOI: 10.1002/syn.890090310

✦ Synopsis

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 duringearly brain development in order to act on the cytoskeletal and adhesive structures responsible in part for neuronal shape and function.