Sandbox Reserved 1105: Difference between revisions
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Identified on 1942, Human transthyretin (TTR) ([[1dvq]]) is a transport protein encoded by the TTR gene, located on chromosome 18 <ref> Wallace MR, Naylor SL, Kluve-Beckerman B, Long GL, McDonald L, Shows TB, Benson MD, Localization of the human prealbumin gene to chromosome 18 [archive], Biochem Biophys Res Commun, 1985;129:753–758</ref>. It was originally called prealbumin as it runs faster than albumin ([[1bm0]]) during SDS-PAGE <ref> Seibert FB, Nelson JW. Electrophoretic study of the blood protein response in tuberculosis. J Biol Chem 1942; 143: 29–38. </ref>. After discovering its binding and transport ability to | Identified on 1942, Human transthyretin (TTR) ([[1dvq]]) is a transport protein encoded by the TTR gene, located on chromosome 18 <ref> Wallace MR, Naylor SL, Kluve-Beckerman B, Long GL, McDonald L, Shows TB, Benson MD, Localization of the human prealbumin gene to chromosome 18 [archive], Biochem Biophys Res Commun, 1985;129:753–758</ref>. It is mainly present in the plasma and synthetized by the liver, but also in the cerebrospinal fluid produced by the choroid plexus of the brain, and in retinal pigment epithelium. This protein was originally called prealbumin as it runs faster than albumin ([[1bm0]]) during SDS-PAGE <ref> Seibert FB, Nelson JW. Electrophoretic study of the blood protein response in tuberculosis. J Biol Chem 1942; 143: 29–38. </ref>. After discovering its binding and transport ability to thyroxine (T4), it was given the name of “thyroxine-binding prealbumin” (TBPA). Indeed, its role is crucial as it allows essential thyroid hormones, implied in cell differenciation, growth and metabolic regulation<ref> Wikipedia contributors. "Thyroid hormones." Wikipedia, The Free Encyclopedia. Wikipedia, The Free Encyclopedia, 10 Jan. 2020. Web. 16 Jan. 2020.</ref>, to pass through the bloodstream. Finally, its actual name refers to an additional carrier function: '''trans'''ports '''thyr'''oxine and '''retin'''ol (one form of vitamin A). Recently, it has been found that TTR also has a role in proteolysis, and in the nervous system, implicated axonal growth, neurogenesis, and nerve regeneration<ref name= "Vieira">Vieira M, Saraiva MJ, Transthyretin: a multifaceted protein [archive], Biomol Concepts, 2014;5:45–54</ref>. | ||
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== Disease == | == Disease == | ||
Abnormal TTR levels are found in neuropathologies such as Guillain-Barré syndrome (GBS), frontotemporal dementia (FTD), amyotrophic lateral sclerosis (ALS), amd Parkinson’s disease (PD)<ref name= "Vieira" />. | |||
The most known defect related to TTR is the formation of amyloid fibrils, which can engender several diseases such as familial amyloid polyneuropathy (FAP), familial amyloid cardiomyopathy (FAC), and senile systemic amyloidosis (SSA) also called wild-type transthyretin amyloid (WTTA or ATTR)<ref> Faria TQ, Almeida ZL, Cruz PF, Jesus CS, Castanheira P, Brito RM. A look into amyloid formation by transthyretin: aggregation pathway and a novel kinetic model. Phys Chem Chem Phys. 2015 Mar 4;17(11):7255-63. PMID:25694367 doi:http://dx.doi.org/10.1039/c4cp04549a </ref>. Another type of disease possibly engendered due to TTR amyloid fibrils is the central nervous system selective amyloidosis (CNSA) including familial oculoleptomeningeal amyloidosis characterized by an eye injury, or meningocerebrovascular amyloidosis if the eye is not affected. <ref> P.Gambetti, C. Russo. Human brain amyloidoses. Neuphrol Dial Transplant. 1998; 13 [Suppl 7] : 33-40</ref> | The most known defect related to TTR is the formation of amyloid fibrils, which can engender several diseases such as familial amyloid polyneuropathy (FAP), familial amyloid cardiomyopathy (FAC), and senile systemic amyloidosis (SSA) also called wild-type transthyretin amyloid (WTTA or ATTR)<ref> Faria TQ, Almeida ZL, Cruz PF, Jesus CS, Castanheira P, Brito RM. A look into amyloid formation by transthyretin: aggregation pathway and a novel kinetic model. Phys Chem Chem Phys. 2015 Mar 4;17(11):7255-63. PMID:25694367 doi:http://dx.doi.org/10.1039/c4cp04549a </ref>. Another type of disease possibly engendered due to TTR amyloid fibrils is the central nervous system selective amyloidosis (CNSA) including familial oculoleptomeningeal amyloidosis characterized by an eye injury, or meningocerebrovascular amyloidosis if the eye is not affected. <ref> P.Gambetti, C. Russo. Human brain amyloidoses. Neuphrol Dial Transplant. 1998; 13 [Suppl 7] : 33-40</ref> | ||