Lamin A and lamin C are members of the intermediate filament protein family and are located in the nucleus where they function as skeletal components of the inner nuclear membrane (1). The two proteins are generated by alternate transcription from the single LMNA gene. Lamin A has a molecular weight of about 74kDa while lamin C is 65kDa. The lamin A protein includes a C-terminal segment of 98 amino acids missing from lamin C, while lamin C has a unique C-terminal 6 amino acid peptide not present in lamin A. As a result antibodies raised against lamin A are almost certain bind
to lamin C. During cell division the nuclear lamina breaks down and lamin A/C containing filaments depolymerize, this being regulated by phosphorylation by cyclin dependent protein kinase 1. Mutations in the lamin A/C gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, Hutchinson-Gilford progeria syndrome and Hutchinson-Gilford progeria syndrome.