Insertion Of Mutant Lamin Proteins In Sw480 Colon Adenocarcinoma

Essentially, the nucleus is vital for the cell’s survival. The nucleus controls and gives instructions to all organelles and inhabitants of the cell(Doc. 2). It is a dense, ball shaped configuration that contains the DNA of the cell.

Duchenne Muscular Dystrophy is a sex-linked disease, which is inherited in a recessive fashion (National Human Genome Research Institute, 2013). Over thirty similar genetic disorders exist (Duchenne Foundation Australia, 2015). All types of muscular dystrophy are considered to be a rare disorder (Duchenne Foundation Australia, 2015). Duchenne Muscular Dystrophy is most common in children and causes muscle weakness and wasting, which commonly begins in the lower limbs (Duchenne Foundation Australia, 2015; National Human Genome Research Institute, 2013). The disease itself is caused by changes to the DMD gene, which is responsible for providing instructions regarding the creation of the dystrophin protein in one’s muscles (Duchenne Foundation Australia, 2015). This protein is responsible for protecting muscles from damage, and without it the cells of a person’s muscles deteriorate and symptoms of Duchenne Muscular Dystrophy are exhibited (Duchenne Foundation Australia, 2015). The disease results from changes in the DMD gene, or other genetic changes in a child (Duchenne Foundation Australia, 2015).

The LMNA gene was first mapped using in situ hybridization. The gene was detected using clone LA-6, while the hybridization signals were detected using rhodamine-anti-digoxigenin. The samples were analyzed and photographed using a fluorescence microscope. Metaphase figures obtained from the photographs were observed to determine the amount of figures that probed for LMNA. The results showed that 90% of the metaphase figures probed for lamin A/C (Wydner et al. 1996). After analyzing the bands, LMNA was localized to chromosome 1q21.3, giving the chromosomal position of the LMNA gene.

Duchenne Muscular Dystrophy is a sex-linked disease, which is inherited in a recessive fashion (National Human Genome Research Institute, 2013). Over thirty similar genetic disorders exist (Duchenne Foundation Australia, 2015). All types of muscular dystrophy are considered to be a rare disorder (Duchenne Foundation Australia, 2015). Duchenne Muscular Dystrophy is most common in children and causes muscle weakness and wasting, which commonly begins in the lower limbs (Duchenne Foundation Australia, 2015; National Human Genome Research Institute, 2013). The disease itself is caused by changes to the DMD gene, which is responsible for providing instructions regarding the creation of the dystrophin protein in one’s muscles (Duchenne Foundation Australia, 2015). This protein is responsible for protecting muscles from damage, and without it the cells of a person’s muscles deteriorate and symptoms of Duchenne Muscular Dystrophy are exhibited (Duchenne Foundation Australia, 2015). The disease results from changes in the DMD gene, or other genetic changes in a child (Duchenne Foundation Australia, 2015).

A normal cell will use the genetic information that is found in its DNA, following it’s directions to build proteins. Cells will splice together segments of genetic information, called exons which contain the directions for building proteins. The cells also remove any letters of unused genetic information, called introns. This process is called RNA splicing and it appears to be altered by telomere shortening and this in turn negatively affects the building of proteins that are important in a cell’s cytoskeleton. The cytoskeleton is the internal framework, or scaffolding of a cell, which keeps the cell from collapsing.

The cause of Duchenne Muscular Dystrophy is the occurrence of mutations in the Dystrophin (DMD) gene. The cytogenetic location off the DMD gene is Xp21.2; meaning at location 21.2 on the short arm of the X chromosome from base pair 31,119,219 to base pair 33,339,609. DMD is the biggest human gene currently known and instructs for the production of a 427 kDa protein by the same name. The dystrophin protein is part of the dystrophin associated protein complex which is expressed at the sarcolema and anchors muscle cellcytoskeletons to the extracellular matrix in skeletal and cardiac muscle,

DMD is an X-linked recessive chromosomal that affects 1 in 5,000 males (Yiu and Kornberg). DMD rarely affects females and when they are affected the severity of the disease is much milder than the male cases (Bushby, Finkel and Birnkrant). The mother is the carrier of the DMD gene in 2/3 of cases and can be genetic. The remaining 1/3 of cases are spontaneous mutations that occur in the mother’s egg (Wong, McClaren and Dalton). Males have a 50% chance of inheriting the mutated gene from their mother and presenting with DMD, daughters have 50% chance of inheriting the gene and being a carrier (carriers may not show symptoms but can pass the mutated gene on to their offspring). Fathers cannot pass the gene on to their sons but will pass it on to their daughters (The Muscular Dystrophy Association). The mutation in the DMD gene disrupts dystrophin production. Dystrophin is a protein that is responsible

Med. Genet 2009. 46, 825–833; Cardoso, C., Leventer, R.J., Ward, H.L., Toyo-Oka, K., Chung, J., Gross, A., Martin, C.L., Allanson, J., Pilz, D.T., Olney, A.H., et al. (2003). Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3. Am. J. Hum. Genet. 72, 918–930). MDS is caused by a heterozygous deletion of chromosome 17p13.3, involving several genes including PAFH1B1 and YWHAE coding for LIS1 and 14-3-3 proteins, respectively. This deletion induces malformations during cortical development (Dobyns, W.B., Stratton, R.F., Parke, J.T., Greenberg, F., Nussbaum, R.L., and Ledbetter, D.H. (1983). Miller-Dieker syndrome: Lissencephaly and monosomy 17p. J. Pedod. 102, 552–558; Chong, S.S., Pack, S.D., Roschke, A.V., Tanigami, A., Carrozzo, R., Smith, A.C.M., Dobyns, W.B., and Ledbetter, D.H. (1997). A revision of the lissencephaly and Miller-Dieker syndrome critical regions in chromosome 17p13.3. Hum.

The malfunction of the protein dystrophin is responsible for the symptoms of DMD. If the dystrophin gene functions correctly, the normal allele codes for the production of the protein dystrophin (“NCBI”). This is a high molecular weight protein, and it is in .002% of the total proteins. Normally, the dystrophin protein functions inside muscle cells, providing structural support. It anchors parts of the internal

DMD is caused by a mutation in the X-linked dystrophin gene, which results in a dysfunctional dystrophin protein. Dystrophin is a cytoskeletal protein that provides mechanical stability to muscle cells by connecting the muscle sarcolemma to the basal lamina of the extracellular matrix (ECM), and without it there, the muscle cells typically undergo a process of degeneration and regeneration. This process is limited by the survival of satellite cells present since satellite cells can only undergo mitosis a limited amount of times. Sarcolemma instability typically results in excess intracellular amounts of both sodium and calcium, which causes ATP depletion and mitochondrial uncoupling (Horn & Schleip, 2012). Satellite cells only have a limited number times they can undergo mitosis, and once a patient can no longer generate healthy muscle cells, the patient will typically experience cell death. This cell death and necrosis usually

They are involved because the LMNA gene produces several slightly different proteins called laminas, of the major ones being Lamin A (also known as progerin) and Lamin C. These proteins are generally made throughout the whole body’s cells. The disease is causes the LMNA gene which to become mutated. Althought, this does not causes any harm to lamin c protein, it causes the lamin A protein to misshape, by missing out on 50 amino acids near one end. This is bad because the lamin A protein is a component the nuclear cell membrane. This misshaped version of lamin A is which is responsible for the disorder; it makes it so that it cannot be processed properly in a cell, which then causes a disrupted shape in the nuclear envelope. All in this mutation damages a cell’s structure and function to a nucleus which in turn causes the cells to die

They went to Washington to get money and help from Congress. While there, they got lucky and met Dr. Francis S. Collins and his wife Diane Baker. They agreed to help Sam and his family. They started at Chromosome 1 for answers. Dr. Brown already treated twin boys with troublesome chromosomes. The chromosomes split, turned over, and reattached themselves. This made them find flaws in skin cells. They narrowed it down to a specific spot on the chromosome. Next, they went online to find what genes were in that spot. They realized it was lamin A. This protein can sometimes lead to rare conditions and other problems. The researchers discussed the results together and tested patients. They came to the conclusion that the lamin A was the problem and named the protein progerin. They looked through reports and realized the protein was found in one of Collins’s own patients, Meg Casey. Collins realized she did not have progeria after all. She had mandibuloacral dysplasia

In each form of muscular dystrophy is caused by a genetic mutation particular to that type of the disease. Many of these actions are inherited but, some occur spontaneously

Pathophysiology: This form of muscular disease is caused by a deficiency in motor neuron proteins called SMN or survival of motor neurons. These proteins are necessary for normal motor neuron function. The deficiency is caused by a mutation on chromosome 5 in the gene called SMN1 most commonly. The adjacent SMN2 genes can sometimes compensate for deficient SMN1 genes. Recent research has found that the lack of SMN may, also, affect muscle tissue directly and not just motor neurons.

Muscular dystrophy is a combination of diseases passed down through genes identified by progressive degeneration of the skeletal or voluntary muscles.(Alicia Foose,PhD, Patricia Ardovino,PhD,2008, p.141). This occurs due to mixture of hypertrophy, atrophy, and necrosis muscle cells. The muscle fibers increase in muscle size and results in muscle weakness while the muscle undergoes necrosis, fat and connective tissue replace the muscle fibers.(Sheila Grossman, Carol Mattson Porth,p.461).There are nine types of muscular dystrophy according to Alicia Foose, and Patricia Ardovino“Duchenne, Becker, Emery-Dreifuss, Limb-girdle, facioscapulohumeral, myotonic, oculopharyngeal distal, and congenital.”Each disease