Liddle's Syndrome

Cotard's Syndrome is an uncommon emotional instability which exists in patients with depression, schizophrenia, and psychotic disorder created by a general restorative condition, and it is frequently connected with dementia. Patients denies their existence, the presence of a specific body part, or the presence of a bit of their body. Delusion and hallucinations are the primary manifestations, yet others, for example, depression and anxiety happen by and large.

Six year old Eric is continuously brought to a local clinic by his mother Monica for treatment of abdominal cramps or according to the mother, appendicitis. Eric is the only son and lives with his mother. With each appointment, Eric symptoms become more progressive, resulting in his hospitalization. As his length of stay increases, Eric’s doctor, Dr. Spencer begins to suspect that something is wrong and suspects Munchausen’s syndrome by proxy, however, none of the other hospital staff members believes Dr. Spencer. As Eric remains hospitalized, his hospital roommate, Ben, begins to develop similar symptoms Eric has been presenting. Dr. Spencer would like to monitor Eric’s mother without her knowledge, but the

mutation is phenylalanine 508 known as delta F508. Delta F508 is a deletion of 3 nucleotides

Lysosomal storage diseases form due to the modification of lysosomal enzymes. The diseases can be metabolically inherited through gene mutation. In “Lysosomal Storage Disease”, Michael Kruer (2) claims that,

Lamentably, down syndrome and autism are the only brain disorders that come in mind to many people when the word syndrome is spoken. However, there are other rare types of disorders that are now increasing dramatically that many are not aware of. Capgras syndrome is a disorder that is not acknowledged by the majority. This psychological issue has been discovered in the 80s by a French psychiatrist named Jean Marie Joseph Capgras where the disorder has been named after her name. This syndrome is a rare delusion disorder where the ill goes through the illusion of seeing the double of a beloved friend, family, pet or even a thing while strongly believing that they are not the same person anymore but are different individuals or things that has

The LOX mutation was discovered by using whole-genome sequencing in a family exhibiting autosomal dominant TAAD. Two individuals from this family affected with TAAD were analyzed, and researchers were able to identify a missense mutation in the lysyl oxidase (LOX) gene,

A delusion where the person is alive but is firmly convinced they are dead. This is called Cotard delusion or walking corpse syndrome.

Chloride channels are a structurally diverse superfamily of transmembrane proteins that facilitate the transport of negative anions across the cell membrane. These channels are involved in a plethora of physiological processes such as neurotransmission, excitation of skeletal, cardiac, and smooth muscle, salt transport, cell volume regulation, and acid production in internal and external compartments. Families of these channels include the voltage-gated CLC family, calcium-activated CaCC family, GABAA receptors, glycine receptors, and the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is an ATP-binding cassette (ABC) transporter that is responsible for proper fluid transport across the epithelial membrane of various cells within body tissues such as the lungs, liver, digestive tract, and reproductive tract. Mutations in the protein sequence of CFTR are characteristic of the disease cystic fibrosis, a disease where improper or absent ion movement decreases the flow of water across exocrine epithelial cells causing mucus and other secretions to be unusually thick.

Bell's palsy befalls when there is a malfunction in the facial nerve (the 7th cranial nerve that is accountable for facial movement), occasioning in feebleness or paralysis of the facial muscles (normally on one side). When the facial nerve is inflamed or compressed, signals directed from the brain to the facial muscles become interrupted occasioning in restricted facial movement or sagging on one side of the face, often accompanied by pain and common uneasiness. Generally, patients are under fifteen or over sixty. Occasionally pregnant women can develop the ailment. Folks become insecure when they have Bell's palsy since it alters the appearance of their face.

As mentioned before, TRPML1 is the transient receptor protein affected by the mutation that causes MLIV. The TRP gene family are not yet well characterized, but are known to localize in late endosomes and have associations with lysosomes. It is required for proper and efficient fusion of late endosomes and autophagosomes with lysosomes (6). There were debates regarding what sort of channel TRMPL1 was, with some stating that it was a proton channel rather than an ion channel (2). However, it seems widely accepted that it is an ion channel capable permeable to ions such as Ca2+ and Fe2+. There has also been recent research that further support TRPML1 as an ion channel. Regardless, the precise role of TRPML1 is largely

Mucolipidosis type IV (MLIV) is a human lysosomal storage disorder characterized early in life by neurodegeneration, visual impairment, low muscle tone, and impaired secretion of gastric acid1. MLIV is caused by loss-of-function mutations or deletions in the Mucolipin-1 gene2 resulting in the absence or a dysfunctional protein product called transient receptor potential mucolipin-1 (TRPML1) ion channel. TRPML1 consists of six predicted transmembrane (TM) domains with channel features showing inward rectification, and non-selective permeability to calcium (Ca2+), zinc (Zn2+), iron (Fe2+), and manganese (Mn2+) 3. Some of the cellular phenotypic characteristics of TRPML1 dysfunction include hyperacidic lysosomes, lysosomal swelling, and lipid accumulation. More recently, irregular levels of specific trace metals have been suggested to contribute to the abnormal cellular phenotype, as well as the progressive cell degeneration associated with TRPML1 dysfunction4.

NGLY1 deficiency is a rare genetic disorder that was first discovered in 2012 and has been diagnosed in less than 100 individuals worldwide. This disease is caused by a lack of the enzyme N-glycanase 1, which helps break down defective proteins, explained by Clement Y. Chow, PhD, Assistant Professor in the Department of Human Genetics at the University of Utah. People with this disease tend to experience global developmental delays, seizures, difficulty with movement, problems with liver function, and the difficulty to produce tears. The symptoms of this disease can vary since not all the information has been gathered about NGLY1 deficiency.

The disease does not a have a very long or varied history. The first description of generalized RTA was made by Reginald Lightwood an English pediatrician. He first described RTA as Lightwood Syndrome, in 1936 in an abstract as a “calcium infarction of the kidneys” and did not mention the term acidosis. Lightwood first described this in infants who died of dehydration and a salt wasting disease. Later that year Lightwood, Payne, and Black who are doctors in pediatrics at Massachusetts General Hospital added to the syndrome describing dehydration and acidosis with calcification of renal tubules. Cases concerning Lightwood syndrome seemed to disappear between the 1950’s - 1960’s, as did the urinary acidification defect. This lead many to believe

This rare disease has an incidence of 1 in 36,000 live births [1] worldwide and a very high penetrance rate of more than 90% of mutation carriers by the age of 65 years. Causative gene VHL (NCBI Genebank gene ID: 608537), was located at Chr 3p25.3 and was found by positional cloning techniques in

Moreover, SERCA2b is the only SERCA isoform expressed in astrocytes, as shown by recent immunoblotting data using astrocytes isolated from the rat cerebral cortex (Morita & Kudo, 2010). Of note, the universal expression of the SERCA2b in mammalian cells has led to considering this SERCA isoform as an ER housekeeping protein (Burk, Lytton, MacLennan, & Shull, 1989; Lytton & MacLennan, 1988; Lytton, Zarain-Herzberg, Periasamy, & MacLennan, 1989). Last but not least, recent immunoblotting data suggest that the SERCA2c isoform is also expressed at low levels in the brain, but it is more widely expressed in epithelial, mesenchymal and hematopoietic cells (Dally et al., 2006; Dally et al., 2010; Gelebart et al., 2003).