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Books > Science & Mathematics > Biology, life sciences > Biochemistry > Proteins
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Recent Advances in Transthyretin Evolution, Structure and Biological Functions (Paperback, 2009 ed.)
Loot Price: R6,549
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Recent Advances in Transthyretin Evolution, Structure and Biological Functions (Paperback, 2009 ed.)
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Since its ?rst description in 1942 in both serum and cerebrospinal
?uid, transthyretin (TTR) has had an eventful history, including
changes in name from "prealbumin" to "thyroxine-binding prealbumin"
to "transthyretin" as knowledge increased about its functions. TTR
is synthesised in a wide range of tissues in humans and other
eutherian mammals: the liver, choroid plexus (blood- cerebrospinal
?uid barrier), retinal pigment epithelium of the eye, pancreas,
intestine and meninges. However, its sites of synthesis are more
restricted in other vertebrates. This implies that the number of
tissues synthesising TTR during vertebrate evolution has increased,
and raises questions about the selection pressures governing TTR
synthesis. TTR is most widely known as a distributor of thyroid
hormones. In addition, TTR binds retinol-binding protein, which
binds retinol. In this way, TTR is also involved with retinoid
distribution. More recently, TTR has been demonstrated to bind a
wide variety of endocrine disruptors including drugs, pollutants,
industrial compounds, heavy metals, and some naturally occurring
plant ?avonoids. These not only interfere with thyroid hormone
delivery in the body, but also transport such endocrine disruptors
into the brain, where they have the potential to accumulate.
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