Lamin

Hutchinson-Gilford Progeria Syndrome other wise known as “Progeria”, or “HGPS”, is a very rare, and fatal genetic disorder characterized by an appearance of accelerated aging in young children. The rate of aging is accelerated up to seven times that of a normal life span in first 13 years of life. Progeria comes from the Greek word (πρό), “pro” meaning premature and (γῆρας), “gerias” meaning old age. While there are different forms of Progeria, the most sever form of progeria is formally known

Progeria What is Progeria? Progeria, also known as Hutchinson-Gilford Progeria Syndrome is a rare genetic condition in which a child prematurely ages. It is a form of progeroid syndromes which is a general term for disorders that causes physiological aging. In simple terms, progeria can be referred to as the aging disorder. Effects of Progeria The primary effect of progeria is failure of growth, as one would start to lose hair and have wrinkled skin at a young age. Although, they do not grow or

Insertion of Mutant Lamin Proteins in SW480 colon adenocarcinoma cells Abstract Nuclear Lamina is a mesh like network that lines the nuclear membrane and provides architectural support 2. Lamin proteins are important for cellular structure as well as cellular organization and because of this, functioning lamin proteins are vital in proper expression of genes 1. When mutated, lamin proteins lead to multiple degenerative diseases related to premature aging and diseases like progeria and muscular dystrophy

to death at an average age of about 13 years. Death is usually caused by some form of cardiovascular disease, usually induced by atherosclerosis (Wuyts et al. 2005). Most cases of HGPS are due to de novo autosomal dominant point mutations in the lamin A/C gene (LMNA). There are some reported cases suggesting autosomal recessive inheritance, but further testing needs to be performed. Mapping The LMNA gene was first mapped using in situ hybridization. The gene was detected using clone LA-6, while

The LMNA gene produces two major proteins called lamin A and lamin C and is localized at 1q22. The two proteins are structural proteins found in the nuclear envelope in majority body cells and surrounds and provides support to nucleus. The mutation is autosomal recessive and rarely inherited due to affected

Human Genome Research Institute, 2013). It was discovered that Progeria is caused by a single gene called LMNA. The LMNA gene produces a protein called lamin A and lamin C. Both help to stabilize the inner membrane of the cell’s nucleus. In Progeria, the LMNA mutation causes the gene to produce an abnormal lamin A protein called progerin. Lamin A “is an essential scaffolding component of the nuclear envelope, which is the membrane that surrounds the nucleus” (Genetics

Also, due to the presence of the LID in all INGs, we will study if ING5 and ING4 are capable of interacting with Lamin A in differentiating stem cells and the importance of this interaction to stem cell differentiation. To achieve these objectives, we will use three different mouse embryonic stem (ES) cell lines (R1, D3, E14), already present in the lab. In ongoing

LMNA Gene: The LMNA gene is a member of the intermediate filaments type V, lamins. It is placed at chromosome 1, position 22. The LMNA gene codes for two proteins, lamin A and lamin B. These two protein are similar in amino acid sequences, but a slight difference make lamin A longer than lamin C. These proteins main function is to support the shape of the nuclear lamina (envelope), the fibrous structure surrounding the nucleus. The nuclear membrane regulates the the exchange of molecules through

thereby removing the farnesyl group along with a few adjacent amino acids. Failure to remove this farnesyl group permanently affixes the protein to the nuclear rim. After cleavage by the protease, prelamin A is referred to as lamin A. Lamin A, along with lamin B and lamin C, makes up the nuclear lamina, which provides structural support to the

point mutation in LMNfA gene which encodes the filament protein lamin A, a major component of the nuclear lamina1. The mutation leads to a series of aberrations in splicing of LMNA mRNA which instead produces a truncated version of lamin A protein, called “progerine”1. Lamin A protein itself undergoes posttranslational processing which converts farnesyl-prelamin A to mature lamin A3. One of the crucial stages in processing of lamin A is endoproteolytic processing mediated by the