LMNA
LMNA (lamin A/C) encodes prelamin-A/C, an intermediate filament protein that forms part of the nuclear lamina beside the inner nuclear membrane. It is also known as HGPS, MADA, LMN1, CMD1A, LGMD1B, PRO1 and LMNL1. Browse Assay Genie's current range of LMNA research reagents below, or read on for the biology behind the target.
The LMNA gene product is part of the nuclear lamina, a two-dimensional matrix of proteins located next to the inner nuclear membrane. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. During mitosis the lamina matrix is reversibly disassembled as lamin proteins are phosphorylated. UniProt also reports that prelamin-A/C can accelerate smooth muscle cell senescence: in vascular smooth muscle cells it disrupts mitosis and induces DNA damage, leading to mitotic failure, genomic instability and premature senescence.
Prelamin-A/C belongs to the intermediate filament family and is assigned to the lamins gene group. The lamin family is highly conserved in evolution, and vertebrate lamins fall into two types, A and B. Alternative splicing of the LMNA gene results in multiple transcript variants. UniProt records the protein in several nuclear compartments: the nuclear lamina, nuclear envelope, nucleoplasm, nuclear matrix and nuclear speckles. Mouse and rat each carry an ortholog named Lmna.
The LMNA gene is best known for its disease associations. Mutations lead to several disorders: Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease and Hutchinson-Gilford progeria syndrome. This history is reflected in the aliases and former gene names, which include cardiomyopathy, dilated 1A, limb girdle muscular dystrophy 1B, progeria 1 (Hutchinson-Gilford type) and lamin A/C-like 1.
Lamins are thought to contribute to nuclear stability, chromatin structure and gene expression, making LMNA central to studies of nuclear lamina organisation.
Mutations in LMNA cause Hutchinson-Gilford progeria syndrome, and prelamin-A/C can accelerate smooth muscle cell senescence.
LMNA mutations are linked to dilated cardiomyopathy, Emery-Dreifuss muscular dystrophy and limb girdle muscular dystrophy.
The lamina is reversibly disassembled by phosphorylation in mitosis, and prelamin-A/C can disrupt mitosis and induce DNA damage in vascular smooth muscle cells.
LMNA encodes lamin A/C, a component of the nuclear lamina next to the inner nuclear membrane. Lamins are thought to be involved in nuclear stability, chromatin structure and gene expression. The lamina is reversibly disassembled during mitosis as lamin proteins are phosphorylated.
Alternative splicing produces multiple transcript variants. The aliases HGPS, MADA, LMN1, CMD1A, LGMD1B, PRO1 and LMNL1 reflect earlier names, many tied to diseases such as progeria, dilated cardiomyopathy and limb girdle muscular dystrophy. UniProt names the protein prelamin-A/C.
Lamins are highly conserved in evolution, and mouse and rat both have an ortholog called Lmna. Human LMNA mutations lead to Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease and Hutchinson-Gilford progeria syndrome. Check the datasheet of any product for its validated reactivity.
Other lamins, nuclear envelope proteins and markers of nuclear lamina biology and senescence with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P02545; product specifications from Assay Genie datasheets.