Sandbox GGC12: Difference between revisions

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== Disease ==

HSA is involved in two important diseases, Hyperthyroxinemia, familial dysalbuminemic (FDAH) and Analbuminemia (ANALBA).

First, FDAH is a condition based on the genetic composition of the individual. It is caused by a mutation in the ALB gene, which corresponds to an increased affinity of the protein HSA for thyroxine. In detail, this autosomal dominant genetic disorder is characterized by the mutation of HSA causing the assembly of thyroxine in a higher proportion. There are two positions with three natural variants identified on the HSA that mutate to cause this disorder. The first position is at 90 amino acid, where leucine is replaced by a proline. The second position at 242 amino acid, where arginine is substituted by histidine or proline. This disorder could lead to confusion and several misdiagnoses of hyperthyroidism because it is difficult to detect it due to the normal TSH and free thyroxine levels but with an elevated total of thyroxine <ref>PMID: 32665066</ref>.

Second, ANALBA is an uncommon autosomal recessive genetic mutation characterized by the identification of very low levels of HSA circulating in the bloodstream <ref>PMID: 8134387</ref>. The affected individuals have symptoms corresponding to mild edema, hypotension, fatigue, and lower body lipodystrophy in females. The mutagenesis is located in the position 91 where histidine is replaced by alanine impairing metal binding <ref>PMID: 28567254</ref>. The complications of this disorder could lead to early atherosclerosis and heart problems.

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@@ Line 7: / Line 7: @@
 == Disease ==
+HSA is involved in two important diseases, Hyperthyroxinemia, familial dysalbuminemic (FDAH) and Analbuminemia (ANALBA).
+First, FDAH is a condition based on the genetic composition of the individual. It is caused by a mutation in the ALB gene, which corresponds to an increased affinity of the protein HSA for thyroxine. In detail, this autosomal dominant genetic disorder is characterized by the mutation of HSA causing the assembly of thyroxine in a higher proportion. There are two positions with three natural variants identified on the HSA that mutate to cause this disorder. The first position is at 90 amino acid, where leucine is replaced by a proline. The second position at 242 amino acid, where arginine is substituted by histidine or proline. This disorder could lead to confusion and several misdiagnoses of hyperthyroidism because it is difficult to detect it due to the normal TSH and free thyroxine levels but with an elevated total of thyroxine <ref>PMID: 32665066</ref>.
+Second, ANALBA is an uncommon autosomal recessive genetic mutation characterized by the identification of very low levels of HSA circulating in the bloodstream <ref>PMID: 8134387</ref>. The affected individuals have symptoms corresponding to mild edema, hypotension, fatigue, and lower body lipodystrophy in females. The mutagenesis is located in the position 91 where histidine is replaced by alanine impairing metal binding <ref>PMID: 28567254</ref>. The complications of this disorder could lead to early atherosclerosis and heart problems.
 == Relevance ==