A sensitive assay of transthyretin (prealbumin) in human cerebrospinal fluid in nanogram amounts by ELISA

Vatassery, Govind T.; Quach, Hung T.; Smith, W. E.; Benson, Barbara A.; Eckfeldt, John H.

doi:10.1016/0009-8981(91)90344-c

Cited by 36 publications

(32 citation statements)

References 12 publications

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“…TTR concentration in CSF ranges from 5 to 20 mg/l (19), representing approximately 25% of the total CSF protein content (20). The choroid plexus has 11 times more mRNA than the liver, normalized for tissue weight, and synthetizes TTR 13 times faster than the liver (21).…”

Section: Expressionmentioning

confidence: 99%

Transthyretin: a multifaceted protein

Vieira¹,

Saraiva²

2014

BioMolecular Concepts

148

120

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Transthyretin is a highly conserved homotetrameric protein, mainly synthetized by the liver and the choroid plexus of brain. The carrier role of TTR is well-known; however, many other functions have emerged, namely in the nervous system. Behavior, cognition, neuropeptide amidation, neurogenesis, nerve regeneration, axonal growth and 14-3-3ζ metabolism are some of the processes where TTR has an important role. TTR aggregates are responsible for many amyloidosis such as familial amyloidotic polyneuropathy and cardiomyopathy. Normal TTR can also aggregate and deposit in the heart of old people and in preeclampsia placental tissue. Differences in TTR levels have been found in several neuropathologies, but its neuroprotective role, until now, was described in ischemia and Alzheimer's disease. The aim of this review is to stress the relevance of TTR, besides its well-known role on transport of thyroxine and retinol-binding protein.

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Section: Expressionmentioning

confidence: 99%

Transthyretin: a multifaceted protein

Vieira¹,

Saraiva²

2014

BioMolecular Concepts

148

120

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“…That will be close to the clinical setting. At physiological condition in human, TTR is abundant (5–20 μg/mL or 0.1–0.36 μmol/L) while Aβ concentration in CSF is relatively low (3 nmol/L or less) . The effects of TTR on Aβ neurotoxicity have also been demonstrated in in vivo experiments.…”

Section: Discussionmentioning

confidence: 97%

“…That will be close to the clinical setting. At physiological condition in human, TTR is abundant (5-20 μg/mL or 0.1-0.36 μmol/L) 38 while Aβ concentration in CSF is relatively low (3 nmol/L or less). 39,40 The effects of TTR on Aβ neurotoxicity have also been demonstrat- TTR concentration in the CSF was found to negatively correlate with AD patients, 43 as well as the degree of dementia in patients with AD.…”

Section: Effects Of Ttr On 125 I-t 4 / 125 I-aβ40 In the Brainmentioning

confidence: 99%

Effects of transthyretin on thyroxine and β‐amyloid removal from cerebrospinal fluid in mice

Chen

Preston

2016

Clin Exp Pharma Physio

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Transthyretin (TTR) is a binding protein for the thyroid hormone thyroxine (T 4 ), retinol and β-amyloid peptide. TTR aids the transfer of T 4 from the blood to the cerebrospinal fluid (CSF), but also prevents T 4 loss from the blood-CSF barrier. It is however, unclear whether TTR affects the clearance of β-amyloid from the CSF. This study aimed to investigate roles of TTR in β-amyloid and T 4 efflux from the CSF.Eight weeks old 129sv male mice were anaesthetized and their lateral ventricles were cannulated. Mice were infused with artificial CSF containing 125

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“…It is made in the liver and choroid plexus; it is abundant in the CSF [5-20 m g/mL (0.1-0.4 mg/mL)] and serum [170-420 m g/mL, (Giunta et al 2005 ) ; see also (Ingenbleek et al 1972;Vatassery et al 1991 ) ]. It binds and transports thyroxine (T4) and the complex of retinol and the retinol-binding protein.…”

Section: Transthyretinmentioning

confidence: 99%

Strategies for Inhibiting Protein Aggregation: Therapeutic Approaches to Protein-Aggregation Diseases

Lanning

Meredith

2011

Non-Fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases

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Self-aggregation of proteins and peptides is at the root of many diseases, especially neurodegenerative diseases. These conditions include Alzheimer's disease, Huntington's disease, Parkinson's disease, type-2 diabetes mellitus, and transmissible spongiform encephalopathies, which are associated with self-aggregation of amyloid b -protein (A b ), huntingtin, a -synuclein, islet amyloid polypeptide, and the prion protein, respectively. The list of diseases for which protein/peptide aggregation is the root cause is ever expanding. There does not appear to be a single biochemical mechanism by which proteins and peptides self-associate, or a single pathogenic mechanism to explain all protein-/peptide-aggregation diseases. Nevertheless, inhibition of protein self-aggregation remains a potential target for therapeutic intervention. Beyond therapy, inhibitors of protein self-aggregation can serve as tools to help us understand the mechanisms by which aggregation occurs and harms cells. In this chapter, we examine select examples of inhibitors of protein aggregation. We have divided aggregating proteins/peptides into two types: (1) Proteins that have an unstable tertiary structure, that unfold under cellular stress, or that fail to fold correctly during biosynthesis. This instability leads to persistence of unfolded domains that can act as a nidus for self-association. (2) Peptides or proteins (or protein domains) that cannot fold at all, or fold only in the presence of a bound ligand. Examples of the fi rst group include transthyretin, the mammalian prion protein, and certain point-mutant forms of lysozyme or a 1-antitrypsin. In general, self-aggregation of these proteins results from exposure of normally buried hydrophobic residues to aqueous media. Examples of the second group include A b , islet amyloid polypeptide, and calcitonin. Within the second group, we also include proteins that are "peptide-like" in having domains with no unique, stable

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A sensitive assay of transthyretin (prealbumin) in human cerebrospinal fluid in nanogram amounts by ELISA

Cited by 36 publications

References 12 publications

Transthyretin: a multifaceted protein

Transthyretin: a multifaceted protein

Effects of transthyretin on thyroxine and β‐amyloid removal from cerebrospinal fluid in mice

Strategies for Inhibiting Protein Aggregation: Therapeutic Approaches to Protein-Aggregation Diseases

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