The influence of the choroid plexus on the concentration of prealbumin in CSF

“…TTR plasma concentration is age dependent and in healthy newborns it is about half of that in adults (Stabilini, et al 1968;Vahlquist, et al 1975), varying from 20 to 40 mg/ dL. In spite of the low TTR levels in CSF (~2 mg/ dL), the choroid plexus is presented as the major site of TTR expression, expressed as a ratio of tissue/mass, corresponding to a 30-fold higher than that found in plasma and represents 20% of the total CSF proteins (Weisner and Kauerz 1983). Over a hundred TTR mutations have been associated with Familial Amyloid Polyneuropathy (FAP), some of which are very common in Portuguese patients, such as the valine at position 30 substituted by a methionine (TTR V30M) (Saraiva, et al 1984), others provide a very aggressive phenotype, such as the TTR L55P (Jacobson, et al 1992).…”

Section: Transthyretinmentioning

confidence: 99%

Key Enzymes and Proteins in Amyloid-Beta Production and Clearance

Santos¹,

Cardoso²,

Gonçalves³

2011

Alzheimer's Disease Pathogenesis-Core Concepts, Shifting Paradigms and Therapeutic Targets

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“…Human TTR (in association with thyroxine-binding globulin) and serum albumin distribute thyroid hormones in the intravascular and interstitial compartment and control thyroid hormone metabolism and activity [14]. TTR is also secreted by the choroid plexus toward the brain and represents the main thyroid hormone-binding protein in the cerebrospinal fluid [15]. TTR also transports retinol from the liver to target cells in a complex with retinol-binding protein [16].…”

Section: Transthyretinmentioning

confidence: 99%

Biological activity and pathological implications of misfolded proteins

Bellotti¹,

Mangione²,

Stoppini³

1999

CMLS, Cell. Mol. Life Sci.

115

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The physiological metabolism of proteins guarantees that different cellular compartments contain the appropriate concentration of proteins to perform their biological functions and, after a variable period of wear and tear, mediates their natural catabolism. The equilibrium between protein synthesis and catabolism ensures an effective turnover, but hereditary or acquired abnormalities of protein structure can provoke a premature loss of biological function, an accelerated catabolism and diseases caused by the loss of an irreplaceable function. In certain proteins, abnormal structure and metabolism are associated with a strong tendency to self-aggregation into a polymeric fibrillar structure, and in these cases the disease is not principally caused by the loss of an irreplaceable function but by the action of this new biological entity. Amyloid fibrils are an apparently inert, insoluble, mainly extracellular protein polymer that kills the cell without tissue necrosis but by activation of the apoptotic mechanism. We analyzed the data reported so far on the structural and functional properties of four prototypic proteins with well-known biological functions (lysozyme, transthyretin, beta 2-microglobulin and apolipoprotein AI) that are able to create amyloid fibrils under certain conditions, with the perspective of evaluating whether the achievement of biological function favors or inhibits the process of fibril formation. Furthermore, studying the biological functions carried out by amyloid fibrils reveals new types of protein-protein interactions in the transmission of messages to cells and may provide new ideas for effective therapeutic strategies.

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The influence of the choroid plexus on the concentration of prealbumin in CSF

Cited by 25 publications

References 13 publications

Nonimmunoglobulin Proteins in Human Cerebrospinal Fluid

Nonimmunoglobulin Proteins in Human Cerebrospinal Fluid

Key Enzymes and Proteins in Amyloid-Beta Production and Clearance

Biological activity and pathological implications of misfolded proteins

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