The 21-base pair deletion mutant Calpain3 does not inhibit wild-type Calpain3 activity  

作　　者：Swati Maitra Seungjae Oh Yun-Jeong Choe JiHye Kim Nam Chul Kim 

机构地区：[1]Department of Pharmacy Practice and Pharmaceutical Sciences,College of Pharmacy,University of Minnesota,Duluth,MN 55812,USA

出　　处：《Genes & Diseases》2025年第1期52-55,共4页基因与疾病(英文)

基　　金：supported by grants from the Muscular Dystrophy Association and the Wallin Neuroscience Discovery Fund and the Engebretson Drug Design and Discovery Fund(to Nam Chul Kim).

摘　　要：Calpain3 is one of the calpain protease family members that are predominantly expressed in skeletal muscle.Lossof-function mutations in Calpain3 have been related to autosomal recessive limb-girdle muscular dystrophy 1(LGMDR1),a common form of muscular dystrophy.Recently,the heterozygous 21-bp deletion mutation of the Calpain3 gene has been reported to cause autosomal dominant limb-girdle muscular dystrophy 4(LGMDD4)which suggests that the mutant proteins act in a dominant-negative manner.Therefore,we examined whether the mutant protein could suppress the activity of wild-type Calpain3 using a cell culture model and a Drosophila model.The mutant Calpain3 resulted in catalytic inactivation,which did not inhibit wild-type Calpain3 autolytic and catalytic activities in HeLa cells.

关 键 词：CATALYTIC BASE function 

分 类 号：R394[医药卫生—医学遗传学]