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Amyloidosis is a group of diseases in which abnormal proteins, known as amyloid fibrils, build up in tissue. There are several non-specific and vague signs and symptoms associated with amyloidosis. These include fatigue, peripheral edema, weight loss, shortness of breath, palpitations, and feeling faint with standing. In AL amyloidosis, specific indicators can include enlargement of the tongue and periorbital purpura. In wild-type ATTR amyloidosis, non-cardiac symptoms include: bilateral carpal tunnel syndrome, lumbar spinal stenosis, biceps tendon rupture, small fiber neuropathy, and autonomic dysfunction.
Transthyretin (TTR or TBPA) is a transport protein in the plasma and cerebrospinal fluid that transports the thyroid hormone thyroxine (T4) and retinol to the liver. This is how transthyretin gained its name: transports thyroxine and retinol. The liver secretes TTR into the blood, and the choroid plexus secretes TTR into the cerebrospinal fluid.
The serum amyloid P component (SAP) is the identical serum form of the amyloid P component (AP), a 25 kDa pentameric protein first identified as the pentagonal constituent of in vivo pathological deposits called "amyloid". APCS is its human gene.
Familial amyloid polyneuropathy, also called transthyretin-related hereditary amyloidosis, transthyretin amyloidosis abbreviated also as ATTR, or Corino de Andrade's disease, is an autosomal dominant neurodegenerative disease. It is a form of amyloidosis, and was first identified and described by Portuguese neurologist Mário Corino da Costa Andrade, in 1952. FAP is distinct from senile systemic amyloidosis (SSA), which is not inherited, and which was determined to be the primary cause of death for 70% of supercentenarians who have been autopsied. FAP can be ameliorated by liver transplantation.
Pentraxins (PTX), also known as pentaxins, are an evolutionary conserved family of proteins characterised by containing a pentraxin protein domain. Proteins of the pentraxin family are involved in acute immunological responses. They are a class of pattern recognition receptors (PRRs). They are a superfamily of multifunctional conserved proteins, some of which are components of the humoral arm of innate immunity and behave as functional ancestors of antibodies (Abs). They are known as classical acute phase proteins (APP), known for over a century.
Cardiac amyloidosis is a subcategory of amyloidosis where there is depositing of the protein amyloid in the cardiac muscle and surrounding tissues. Amyloid, a misfolded and insoluble protein, can become a deposit in the heart's atria, valves, or ventricles. These deposits can cause thickening of different sections of the heart, leading to decreased cardiac function. The overall decrease in cardiac function leads to a plethora of symptoms. This multisystem disease was often misdiagnosed, with a corrected analysis only during autopsy. Advancements of technologies have increased earlier accuracy of diagnosis. Cardiac amyloidosis has multiple sub-types including light chain, familial, and senile. One of the most studied types is light chain cardiac amyloidosis. Prognosis depends on the extent of the deposits in the body and the type of amyloidosis. New treatment methods are actively being researched in regards to the treatment of heart failure and specific cardiac amyloidosis problems.
In medicine, proteinopathy, or proteopathy, protein conformational disorder, or protein misfolding disease, is a class of diseases in which certain proteins become structurally abnormal, and thereby disrupt the function of cells, tissues and organs of the body.
Pentraxin-related protein PTX3 also known as TNF-inducible gene 14 protein (TSG-14) is a protein that in humans is encoded by the PTX3 gene.
Amyloid light-chain (AL) amyloidosis, also known as primary amyloidosis, is the most common form of systemic amyloidosis. The disease is caused when a person's antibody-producing cells do not function properly and produce abnormal protein fibers made of components of antibodies called light chains. These light chains come together to form amyloid deposits which can cause serious damage to different organs. An abnormal light chain in urine is known as Bence Jones protein.
The familial amyloid neuropathies are a rare group of autosomal dominant diseases wherein the autonomic nervous system and/or other nerves are compromised by protein aggregation and/or amyloid fibril formation.
CPHPC ((R)-1-{6-[(R)-2-carboxypyrrolidin-1-yl]-6-oxohexanoyl}pyrrolidine-2-carboxylic acid) is a proline-derived small molecule able to strip amyloid P (AP) from deposits by reducing levels of circulating serum amyloid P (SAP). The SAP-amyloid association has also been identified as a possible drug target for anti-amyloid therapy, with the recent development and first stage clinical trials of CPHPC for amyloidosis.
Sir Christopher Martin Dobson was a British chemist, who was the John Humphrey Plummer Professor of Chemical and Structural Biology in the Department of Chemistry at the University of Cambridge, and Master of St John's College, Cambridge.
Samuel E. Gandy, is a neurologist, cell biologist, Alzheimer's disease (AD) researcher and expert in the metabolism of the sticky substance called amyloid that clogs the brain in patients with Alzheimer's. His team discovered the first drugs that could lower the formation of amyloid.
Stephen Craig West FRS is a British biochemist and molecular biologist specialising in research on DNA recombination and repair. He is known for pioneering studies on genome instability diseases including cancer. West obtained his BSc in 1974, and his PhD in 1977, both from Newcastle University. He is currently a Principal Group Leader at the Francis Crick Institute in London. He is an honorary Professor at University College London, and at Imperial College London. In recognition of his work he was awarded the Louis-Jeantet Prize for Medicine in 2007, is a fellow of the Royal Society, the Academy of Medical Sciences, an International Member of the National Academy of Sciences, and an International Honorary Member of the American Academy of Arts and Sciences. He received the 2022 Royal Medal for 'discovering and determining the functions of key enzymes that are essential for DNA recombination, repair and the maintenance of genomes'.
Sheena Elizabeth Radford is a British biophysicist, and Astbury Professor of Biophysics and a Royal Society Research Professor in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds. Radford is the Associate Editor of the Journal of Molecular Biology.
Gideon John Davies is a professor of chemistry in the Structural Biology Laboratory (YSBL) at the University of York, UK. Davies is best known for his ground-breaking studies into carbohydrate-active enzymes, notably analysing the conformational and mechanistic basis for catalysis and applying this for societal benefit. In 2016 Davies was appointed the Royal Society Ken Murray Research Professor at the University of York. Gideon Davies has recently been elected to the Council of the Royal Society.
LECT2 Amyloidosis (ALECT2) is a form of amyloidosis caused by the LECT2 protein. It was found to be the third most common cause of amyloidosis in a set of more than 4,000 individuals studied at the Mayo Clinic; the first and second most common forms the disorder were AL amyloidosis and AA amyloidosis, respectively. Amyloidosis is a disorder in which the abnormal deposition of a protein in organs and/or tissues gradually leads to organ failure and/or tissue injury.
Wild-type transthyretin amyloid (WTTA), also known as senile systemic amyloidosis (SSA), is a disease that typically affects the heart and tendons of elderly people. It is caused by the accumulation of a wild-type protein called transthyretin. This is in contrast to a related condition called transthyretin-related hereditary amyloidosis where a genetically mutated transthyretin protein tends to deposit much earlier than in WTTA due to abnormal conformation and bioprocessing. It belongs to a group of diseases called amyloidosis, chronic progressive conditions linked to abnormal deposition of normal or abnormal proteins, because these proteins are misshapen and cannot be properly degraded and eliminated by the cell metabolism.
Nicholas John White is a British medical doctor and researcher, specializing in tropical medicine in developing countries. He is known for his work on tropical diseases, especially malaria using artemisinin-based combination therapy.
Monoclonal gammopathy of renal significance (MGRS) are a group of kidney disorders that present with kidney damage due to nephrotoxic monoclonal immunoglobulins secreted by clonal plasma cells or B cells. By definition, people with MGRS do not meet criteria for multiple myeloma or other hematologic malignancies. The term MGRS was introduced in 2012 by the International Kidney and Monoclonal Gammopathy Research Group (IKMG). MGRS is associated with monoclonal gammopathy of undetermined significance (MGUS). People with MGUS have a monoclonal gammopathy but does not meet the criteria for the clonal burden nor the presence of end organ damage seen in hematologic malignancies. In a population based study based on the NHANES III health survey; 6% of patients with MGUS were subsequently classified as having MGRS. The prevalence and incidence of MGRS in the general population or in specific populations is not known but it is more prevalent in those over the age of 50 as there is a monoclonal protein (M-protein) present in 3% of those 50 and years older and 5% of those 70 years and older, placing those 50 and older at increased risk of MGRS.
References
- ↑ "Pepys, Prof. Mark Brian". Who's Who. doi:10.1093/ww/9780199540884.013.U30545. ISBN 978-0-19-954088-4 . Retrieved 28 April 2019.
- 1 2 "EC/1998/26: Pepys, Mark Brian". London: The Royal Society. Archived from the original on 13 July 2015.
- ↑ Booth, D. R.; Sunde, M; Bellotti, V; Robinson, C. V.; Hutchinson, W. L.; Fraser, P. E.; Hawkins, P. N.; Dobson, C. M.; Radford, S. E.; Blake, C. C.; Pepys, M. B. (1997). "Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis". Nature. 385 (6619): 787–93. Bibcode:1997Natur.385..787B. doi:10.1038/385787a0. PMID 9039909. S2CID 4347837.
- ↑ "Prof Sir Mark Pepys". Institutional Research Information Service. Retrieved 28 April 2019.
- ↑ "The Royal Society GlaxoSmithKline Prize and Lecture (1976) (2002)". royalsociety.org. Archived from the original on 9 June 2008. Retrieved 3 April 2009.
- ↑ "Mark Pepys". royalsociety.org. Retrieved 13 December 2017.
- ↑ "No. 60009". The London Gazette (Supplement). 31 December 2011. p. 1.
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