Hyper-Ige Syndrome

Hutchinson-Gilford Progeria syndrome, also known as HGPS, or Progeria, is a very rare genetic disease caused by a mutation in the cell. In 1886, Jonathan Hutchinson first reported case of a 3 ½ year old boy who had the appearance of an old man. In 1897 Hastings Gilford reported a second case with similar features. However, this mystery disease didn’t have a name until 1904, when it was named after the two men. People who have HGPS usually star showing symptoms by the age of 2, and only live to be a teen-mid-20s.

This syndrome is from a mutation of a gene on chromosome 15 and this causes problems in the production of fibrillin-1 which is a protein that is an important part of connective tissue. The name for the gene is FBN1. Basically, it is the “glue” that helps to support the tissues in the human body. A child born to a parent with this syndrome has a 50% of having it. However, in the remaining 25%, neither parent has the disease which gives them a 1 in 10,000 chance of having a child with this disorder. When a child of two unaffected parents is born with it then the genetic mutation occurs in either the egg or sperm cell at the time of conception.

Hutchinson-Gilford Progeria Syndrome (HGPS) affects approximately 1 in 4-8 million newborns. It is characterized by rapid aging, but no symptoms are seen at birth. Within a year, infected children start showing symptoms such as a receding jaw, pointy nose, partial to total hair loss (alopecia), fat loss, bone disfigurements, a short stature and skin problems (Pollex 2004). The disease progresses with time, and eventually leads 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.

The goal: To identify the difference in severity of FH for the homozygous and heterozygous genotypes. Also, to learn about statins.

Hutchinson Gilford Syndrome or otherwise commonly known as Progeria; is a fatal disease. Sadly, death occurs in every case. This disease is a fast spreading disease in the body, it affects the body almost instantaneously.This disease is a rapid aging disorder caused by a LMNA anomaly. This anomaly release progerin, a mutant lamin. The lamin A/C is the official name of the gene more widely known as LMNA. The gene gives out a designated list of tasks to making different proteins called lamins. The infected cells show a decrease in heterochromatin, a increased amount a deoxyribonucleic acid, and cell cycle changes. Hutchinson-Gilford progeria syndrome (HGPS) is an extremely rare hereditary disease that affects the skin, musculoskeletal system, and vasculature. HGPS is characterized by signs of premature aging(Kara N Shah,HGPS, MedScape)

chemotherapy, or have a rapid proliferative rate. The signs and symptoms to look for include hyperuricemia, hypocalcemia, hyperphosphatemia, and hyperkalemia and with children flank pain, lethargy, nausea, vomiting, muscle cramps, pruritus, tetany, and seizures . With hyperuricemia more complications can occur such as the crystallization of uric acid which can cause obstructive nephropathy, tubular injury, acute renal failure and death. Because tumor lysis syndrome can be lethal the important teaching for management of it would be prevention measures, early identification, and putting in place interventions early on.

caused by an overacting immune system and is actually an autoimmune where the immune system mistakenly attacks the body’s own tissue.

Since the most commonly documented associated condition with AIWS is infection, much of the recent literature has focused on the associated effects of infection resulting from Lyme disease and Epstein-Barr virus (EBV). The following three instances of AIWS episodes are case studies of children with AIWS associated with various forms of infection:

For the genetic abnormality at the root of this disease, it is an X-linked inborn error of the glycosphingolipid metabolic pathway. Typically it is an X linked inheritance pattern that is neither recessive or dominant, and is x linked in this family history as well. The metabolic defect is in in the lysosomal hydrolase alpha-galactosidase A (alpha-Gal A), which catalyzes the hydrolytic cleavage of the terminal galactose from globotriaosylceramide (Gb3). This results in accumulation of globotriaosylceramide within lysosomes in cells, in the vascular

ABSTRACT: Mutations in the MED12 gene are associated with X-linked intellectual disability (ID) which present phenotypically as FG syndrome or Lujan syndrome. The two disorders have overlapping features of ID, hypotonia, and corpus callosum abnormalities but physical features differ . Carrier females are typically unaffected. Mitochondrial dysfunction has not been previously described. Herein, we report a 7 year old male with features of FG syndrome, hypogammoglobulinemia, mitochondrial dysfunction, and normal IQ found to have a de novo deleterious MED12 mutation on whole exome sequencing. This case expands the phenotype of MED12-related disorders. In addition, hypogammoglobulinemia documented in this patient may explain the frequent infections reported in other patients with MED12 mutations.

In their paper, Essential Lymphocytophthisis; New Clinical Aspect of Infant Pathology, the authors observed that Swiss infants who were diagnosed with the condition were profoundly lympopenic and would usually die before they reached their second birthday. Subsequent research on this condition was focused on identifying its inheritance patterns. The research identified two main inheritance patterns, namely, an X-linked recessive mode of inheritance and an autosomal recessive mode of inheritance. Giblett were the first to discover the molecular cause of SDIC, adenosine deaminase deficiency, in 1972 (Giblett, et al., 1972). However, it took researchers almost 21 years to determine the second cause of SCID, that is, X-linked SCID (Puck, et al., 1993). Since then, advances in molecular biology have led to a much wider understanding of SDIC and its other causes. It is now known that the disease can be caused by mutations in more than 10 genes in the human body as well as some other causes that have not yet been identified (Russell, et al., 1995). Thus, the gene products of these mutations are components of cytokine receptors like IL-2, IL-4R, IL-7R, IL-9R, IL-15R, and IL-21R. However, mutations of the IL-2RG receptor accounts for more than 46% of all cases of X-linked SCID. Adenosine deaminase deficiency, on the other hand, is responsible for 16% of all SCID cases, while

Stevens-Johnson syndrome has been associated with various bacterial, viral, mycotic, and protozoal infections. Vaccines, collagen diseases, and many drugs have also been implicated

The biochemical pathways involved in IDH mutant forms (IDH1m, IDH2m) reveal that a substitution of the arginine residue 132 with histidine is responsible for the pathogenic changes due to IDH1 mutations (6) (Figure 1).

Zellweger syndrome (ZS), neonatal adrenoleukodystrophy (NALD), X-linked adrenoleukodystrophy (X-ALD), and infantile Refsum disease (IRD) are the four main peroxisomal disorders classified by the absence, or a defect in, specific peroxisomal proteins. Zellweger syndrome is considered the most severe of the four most studied peroxisomal disorders, causing a faster and earlier death. Lacking or having defective peroxisomal proteins is especially problematic due to the many functions specific to this organelle such as the breakdown of fatty acids, production of lipids for the nervous system and digestion, and functioning in development of the brain. Peroxisomes contain no DNA, causing all of its defects to be mutations of nuclear genes. This is significant because, as we’ll learn later in this class, nuclear genes code for peroxisomal proteins which are synthesized on cytoplasmic ribosomes to later be imported into the peroxisome. Without proper formation, these proteins will not enter the peroxisomes and remain functionless in the cytosol. Some individuals can still have peroxisomes detected in their cells, but they are non-functional--or cannot properly carry out their duties--without the assistance

From research on Medline, I learn that Transverse myelitis is a neurological disorder caused by inflammation