Metabolism of the Vitamin A Transporting Protein Complex

Vahlquist, Anders; Peterson, Per A.; Wibell, L

doi:10.1111/j.1365-2362.1973.tb00362.x

Cited by 134 publications

(26 citation statements)

References 32 publications

(18 reference statements)

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“…TTR is a very prominent plasma protein (20 -40 mg/dl) and it has a plasma residence time of only 1-2 days. 5,72 It must represent a significant burden to the catabolic mechanisms of plasma protein turnover. Much is known about the synthesis of transthyretin by the liver, but the sites of catabolic processing have not been well defined.…”

mentioning

confidence: 99%

The molecular biology and clinical features of amyloid neuropathy

Benson¹,

Kincaid²

2007

Muscle and Nerve

399

312

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Neuropathy is often a major manifestation of systemic amyloidosis. It is most frequently seen in patients with hereditary transthyretin (TTR) amyloidosis, but is also present in 20% of patients with systemic immunoglobulin light chain (primary) amyloidosis. Familial amyloid polyneuropathy (FAP) is the most common form of inherited amyloidotic polyneuropathy, with clinical and electrophysiologic findings similar to neuropathies with differing etiologies (e.g., diabetes mellitus). Hereditary amyloidosis is an adult-onset autosomal-dominant disease with varying degrees of penetrance. It is caused by specific gene mutations, but demonstration that a patient has one such mutation does not confirm the diagnosis of amyloidosis. Diagnosis requires tissue biopsy with demonstration of amyloid deposits either by special histochemical stains or electron microscopy. Transthyretin amyloidosis is treated by liver transplantation, which eliminates the mutated transthyretin from the blood, but for some patients continued amyloid deposition can occur from wild-type (normal) transthyretin. Presently, a study is ongoing to determine whether amyloid deposition can be inhibited by small organic molecules that are hypothesized to affect the fibril-forming ability of transthyretin. Proposed gene therapy with antisense oligonucleotides (ASOs) to suppress hepatic transthyretin synthesis is effective in a transgenic mouse model but has not yet been tested in humans.

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mentioning

confidence: 99%

The molecular biology and clinical features of amyloid neuropathy

Benson¹,

Kincaid²

2007

Muscle and Nerve

399

312

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“…The protein binds the complex retinol-retinol binding protein, preventing its glomerular filtration (4), thyroxin and related compounds, and also polyhalogenated biphenyl compounds (5). The half-life of TTR is 2-3 days in humans (6), and the major site of TTR degradation is the liver followed by the muscle and skin.…”

Section: Transthyretin (Ttr)mentioning

confidence: 99%

The Crystal Structure of Amyloidogenic Leu55→ Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid Fibrils

Sebastião¹,

Saraiva²,

Damas³

1998

Journal of Biological Chemistry

120

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“…Intestine epithelial cells were isolated from Sprague-Dawley rats essentially as described (11 (17). RBP was purified from human serum (18).…”

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confidence: 99%

Use of anti-idiotypic antibodies as cell-surface receptor probes

Sege

Peterson

1978

Proc. Natl. Acad. Sci. U.S.A.

317

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Anti-idiotypic antibodies have been raised against antibodies to retinol-binding protein (RBP) and to insulin. After absorption the anti-idiotypic antibodies recognized the antigen-combining sites of the antibodies used as the immunogen but of no other antibodies. Some of the anti-idiotypic antibodies raised against antibodies to RBP bound specificanly to rat intestine epithelial cells, which have a physiological cell-surface receptor for RBP. The RBP receptor mediates the uptake of retinol from RBP to the cells. This uptake was abolished in a concentration-dependent manner by the anti-idiotypic antibodies, which obviously competed with RBP for binding to the receptor.Anti-idiotypic antibodies against antibodies to insulin inhibited the binding of "25I-labeled insulin to isolated rat epididymal fat cells, whereas anti-idiotypic antibodies raised against antibodies to RBP had no effect. Furthermore, on interacting with young rat thymocytes, anti-idiotypic antibodies against antibodies to insulin stimulated the uptake by the cells of aaminoisobutyric acid, thereby mimicking the effect of insulin.These results suggest that in some cases anti-idiotypic antibodies may be useful tools in elucidating structure-function relationships for cell-membrane receptors. The immune system recognizes foreign substances by generation of antibodies that display an almost endless variety of combining sites. Thus, even a small, chemically well-defined molecule may, on immunization, give rise to stimulation of about 100 antibody-forming clones. Each clone produces a specific antibody with a unique amino acid sequence in the variable region (1). Due to the enormous variability in the antibody population, it seemed possible that among all the different antibodies that are elicited as a result of the immunization with, e.g., a hormone, a few antibodies might recognize that hormone in a fashion that mimics the way a physiological receptor recognizes the hormone. If so, the combining sites of such receptor-like antibodies might display structural features in common with the hormone-binding part of the receptor. Consequently, a few of a second set of antibodies raised against the combining sites, the idiotopes, of the "receptor-like" antibodies may, in their variable portions, be similar to those structures of the hormone that bind to the physiological receptor. Among such second sets of antibodies, anti-idiotypic antibodies, some would presumably interact with the hormone receptor in a hormone-like fashion.To test the above reasoning we have raised anti-idiotypic antibodies against antibodies to retinol-binding protein (RBP) and to insulin. Since cell-surface receptors for RBP (2) and insulin (for a review, see ref. 3) exist, the possible binding of the anti-idiotypic antibodies to these receptors has been explored. This communication presents data that demonstrate that such anti-idiotypic antibodies may become useful tools in elucidating the structure and function of cell-surface receptors.The costs of publication of this article...

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Metabolism of the Vitamin A Transporting Protein Complex

Cited by 134 publications

References 32 publications

The molecular biology and clinical features of amyloid neuropathy

The molecular biology and clinical features of amyloid neuropathy

The Crystal Structure of Amyloidogenic Leu55→ Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid Fibrils

Use of anti-idiotypic antibodies as cell-surface receptor probes

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