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Amyloidotic polyneuropathy in a Jewish family. Evidence for the genetic heterogeneity of the lower limb familial amyloidotic neuropathies.

https://arctichealth.org/en/permalink/ahliterature51402
Source
Q J Med. 1985 Apr;55(216):33-44
Publication Type
Article
Date
Apr-1985
Author
J. Gafni
B. Fischel
R. Reif
M. Yaron
M. Pras
Source
Q J Med. 1985 Apr;55(216):33-44
Date
Apr-1985
Language
English
Publication Type
Article
Keywords
Adult
Amino Acid Sequence
Amyloid - analysis
Amyloidosis - genetics - metabolism
Eye Diseases - genetics
Hereditary Sensory and Autonomic Neuropathies - genetics - metabolism
Humans
Israel
Jews
Leg
Male
Poland
Research Support, Non-U.S. Gov't
Vitreous Body
Abstract
The first instance of familial amyloidotic polyneuropathy affecting a Jewish family is reported. Vitreous opacities were its presenting feature in the father at age 30 and the son at 25. Severe autonomic dysfunction and progressive peripheral neuropathy affecting initially the lower extremities soon followed. Death, suicidal in the son, occurred after seven and four years of illness. Their amyloid contained three proteins-an entire variant monomer of prealbumin, glycine replacing threonine as residue 49, and both products of its cleavage at the point of substitution. Lower limb familial amyloidotic polyneuropathy has been recorded in many families in Portugal, Sweden and Japan and occasionally in families of various ethnic stocks. This ethnic diversity prompts consideration of genetic heterogeneity. Differentiation on a genetic basis is forestalled since all pedigrees are compatible with autosomal dominant transmission and clinical data are marred by observer variance, even regarding vitreous opacities. Notwithstanding, an isolated British family is unique in the frequent occurrence of intractable peptic ulceration, cataracts, deafness and renal disease not attributable to amyloidosis and a striking predominance of males afflicted. Biochemically, monomeric prealbumin has been demonstrated by electrophoretic and immunologic techniques as the single protein constituent of amyloids isolated from Portuguese, Japanese and Swedish patients. The variant prealbumin of Japanese amyloid is characterised by methionine replacing valine as residue 30 and is identical to that found in plasma (but not as yet in amyloid) of affected Swedes. These limited data suggest that: (a) derivation of their amyloids from prealbumin is the biochemical common denominator of lower limb familial amyloidotic neuropathies regardless of the ethnic derivation of the afflicted; (b) to the extent that ethnic diversity reflects genetic heterogeneity, this will be demonstrable in the amyloid (and hopefully in the plasma) of the afflicted as entity-specific variant prealbumin monomers distinguished by different single amino acid substitutions; (c) on clinical and biochemical grounds, lower limb familial amyloidotic neuropathies include at least three genetic entities. In the upper limb and facial forms of familial amyloidotic polyneuropathy first recorded in Swiss and Finns respectively, the differences in their patterns of neurological disease and ocular lesions could be the result of their amyloids deriving from proteins other than prealbumin.
PubMed ID
3859886 View in PubMed
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Association of C3 and C4A complement types with familial amyloidotic polyneuropathy.

https://arctichealth.org/en/permalink/ahliterature103549
Source
Hum Hered. 1990;40(5):272-7
Publication Type
Article
Date
1990
Author
P O Nylander
L. Beckman
G. Holmgren
L. Steen
Author Affiliation
Department of Medical Genetics, University of Umeå, Sweden.
Source
Hum Hered. 1990;40(5):272-7
Date
1990
Language
English
Publication Type
Article
Keywords
Age Factors
Amyloidosis - genetics - metabolism
Biological Markers
Complement C3 - genetics
Complement C4a - genetics
Female
Gene Frequency
Hereditary Sensory and Autonomic Neuropathies - genetics - metabolism
Humans
Male
Middle Aged
Sex Factors
Sweden
Abstract
A mutant variant of the serum protein transthyretin (TTR-met30) appears to be a necessary but not sufficient condition for the development of familial amyloidotic polyneuropathy (FAP). We have studied a number of serum protein markers (alpha 1-antitrypsin, properdin factor B, C3, C4A, C4B, haptoglobin, transferrin and group-specific component) in FAP patients and healthy controls in an attempt to identify additional pathogenic factors which may influence the risk for developing FAP in male and female patients as well as the age of onset of the disease. Statistically significant associations were found in the complement systems C3 and C4A. The C3F variant was significantly increased in all FAP patients with a relative risk (RR) of 2.0, more pronounced in female patients (RR = 2.6) and patients with an early onset of the disease (RR = 4.5). In the FAP patients only the variants A3 and A4 were found in the C4A system. C4A3 was found in all patients, which was significantly higher than in the controls. The remaining serum protein systems showed no statistically significant associations with FAP. The results suggest that genetic variants of complement factors C3 and C4A may interact with the mutant TTR-met30 by modifying the expression and onset of FAP.
PubMed ID
2265853 View in PubMed
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Immunohistochemical localization of amyloid in Finnish hereditary amyloidosis with antibodies to gelsolin peptides.

https://arctichealth.org/en/permalink/ahliterature226778
Source
Lab Invest. 1991 Mar;64(3):400-4
Publication Type
Article
Date
Mar-1991
Author
C P Maury
Author Affiliation
Fourth Department of Medicine, University of Helsinki, Finland.
Source
Lab Invest. 1991 Mar;64(3):400-4
Date
Mar-1991
Language
English
Publication Type
Article
Keywords
Amyloid - metabolism
Amyloidosis - genetics - metabolism
Antibodies - analysis
Calcium-Binding Proteins - immunology
Child, Preschool
Congo Red - diagnostic use
Enzyme-Linked Immunosorbent Assay
Finland
Gelsolin
Humans
Immunohistochemistry
Microfilament Proteins - immunology
Microscopy, Electron
Nerve Tissue Proteins - immunology
Abstract
The amyloid fibril protein in the Finnish type of familial amyloid polyneuropathy was recently identified as a fragment of gelsolin, a cytoskeletal and plasma protein with actin-modulating properties. Antibodies to three synthetic peptides of various parts of gelsolin were raised in rabbits and used in immunocytochemistry. The P-3 dodecapeptide, corresponding to the C-terminal region of the amyloid protein, elicited the best immunologic response and the P-3 antibodies were found suitable for use in immunohistochemistry and enzyme immunoassay. The P-3 antibodies specifically stained the amyloid deposits in various tissues including the skin, kidney, heart, thyroid gland, salivary gland, and rectum in patients with Finnish familial amyloid polyneuropathy. The staining was completely abolished by absorption of the antiserum with the synthetic dodecapeptide used for immunization, but not by a peptide of another region of the gelsolin molecule. The antibodies did not stain the amyloid of secondary amyloid A or of the myeloma-associated amyloid light chain. The results provide evidence for the relation between the amyloid deposited in the systemic tissues of patients with Finnish familial amyloid polyneuropathy and gelsolin, and demonstrate the utility of these anti-gelsolin antibodies in diagnostic immunohistochemistry.
PubMed ID
1848334 View in PubMed
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Impact of age and amyloidosis on thiol conjugation of transthyretin in hereditary transthyretin amyloidosis.

https://arctichealth.org/en/permalink/ahliterature33111
Source
Amyloid. 1999 Sep;6(3):187-91
Publication Type
Article
Date
Sep-1999
Author
O B Suhr
I H Svendsen
P I Ohlsson
J. Lendoire
P. Trigo
K. Tashima
P J Ranløv
Y. Ando
Author Affiliation
Department of Medicine, Umeå University Hospital, Sweden. ole.suhr@medicin.umu.se
Source
Amyloid. 1999 Sep;6(3):187-91
Date
Sep-1999
Language
English
Publication Type
Article
Keywords
Adolescent
Adult
Aged
Aging - metabolism
Amyloidosis - genetics - metabolism - physiopathology
Child
Female
Humans
Male
Middle Aged
Mutation
Prealbumin - metabolism
Research Support, Non-U.S. Gov't
Sulfhydryl Compounds - metabolism
Abstract
Variant forms and post-translational modifications of transthyretin (TTR) can be identified by electrospray ionisation mass spectrometry (ESI-MS). The aim of the present study was to investigate thiol conjugation of transthyretin and it's relation to age and symptomatic amyloid disease in different populations of variant TTR carriers. Plasma samples from 70 individuals from Denmark, Argentina, Sweden and Japan, with 2 different TTR mutations were analysed. The percentage cysteine (Cys) conjugated wild and variant TTR were calculated from the corresponding peaks of the spectra, and multiple regression analysis was employed to disclose relationships between age, symptomatic amyloid disease and origin. Age, origin and presence of symptomatic disease, were found to be independent factors related to transthyretin conjugation. A higher percentage of conjugated to unconjugated TTR was disclosed in symptomatic, but not in asymptomatic carriers. In summary: Thiol conjugation of TTR is dependent on age and presence of symptomatic amyloid disease. Furthermore, it varies between different populations. Variant TTR is more susceptible to thiol conjugation than the wild type. Post-translational factors may be related to amyloid formation and/or toxicity.
PubMed ID
10524283 View in PubMed
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A new prealbumin variant in familial amyloid cardiomyopathy of Danish origin.

https://arctichealth.org/en/permalink/ahliterature55522
Source
Scand J Immunol. 1988 Jan;27(1):119-22
Publication Type
Article
Date
Jan-1988
Author
M. Nordlie
K. Sletten
G. Husby
P J Ranløv
Author Affiliation
Institute of Biochemistry, University of Oslo, Norway.
Source
Scand J Immunol. 1988 Jan;27(1):119-22
Date
Jan-1988
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Amyloid - genetics - isolation & purification
Amyloidosis - genetics - metabolism
Cardiomyopathies - genetics - metabolism
Denmark - ethnology
Humans
Molecular Sequence Data
Prealbumin - genetics - isolation & purification
Abstract
A C-terminal fragment of a prealbumin variant was isolated from amyloid material obtained from the myocardium of a patient (Han) with familial amyloid cardiomyopathy of Danish origin. The prealbumin variant fragment was shown to have a methionine for leucine substitution in position 111.
PubMed ID
3340821 View in PubMed
Less detail

Ocular amyloid deposition in familial amyloidosis, Finnish: an analysis of native and variant gelsolin in Meretoja's syndrome.

https://arctichealth.org/en/permalink/ahliterature217357
Source
Invest Ophthalmol Vis Sci. 1994 Sep;35(10):3759-69
Publication Type
Article
Date
Sep-1994
Author
T. Kivelä
A. Tarkkanen
B. Frangione
J. Ghiso
M. Haltia
Author Affiliation
Department of Ophthalmology, Helsinki University Central Hospital, Finland.
Source
Invest Ophthalmol Vis Sci. 1994 Sep;35(10):3759-69
Date
Sep-1994
Language
English
Publication Type
Article
Keywords
Aged
Aged, 80 and over
Amyloid - metabolism
Amyloidosis - genetics - metabolism - pathology
Anterior Eye Segment - blood supply - innervation - metabolism - pathology
Choroid - metabolism - pathology
Eye Diseases - genetics - metabolism - pathology
Finland
Gelsolin - metabolism
Humans
Immunoenzyme Techniques
Middle Aged
Optic Nerve - metabolism - pathology
Retina - metabolism - pathology
Syndrome
Abstract
To analyze the deposition of amyloid and its precursors in eyes of patients with familial amyloidosis, Finnish (FAF; Meretoja's syndrome), a hereditary systemic amyloidosis.
Autopsy eyes from three patients with FAF and ten control eyes were studied by Congo red staining and with antibodies to the nonmutated part of gelsolin (GS-2C4), the mutated gelsolin Asn-187 fragment (AGel), and amyloid-P component (AP).
Congo red and antisera to AP and AGel bound to amyloid deposits in the cornea and conjunctiva, the sclera, the perineurium of ciliary nerves, the walls of ciliary vessels, the optic nerve sheaths, the stroma of the ciliary body, and along the choriocapillaris. mAb GS-2C4 bound weakly and focally to most deposits and strongly around the choriocapillaris. It labeled the corneal epithelium and endothelium, keratocytes, scleral fibroblasts, trabecular and lens epithelial cells, the ciliary muscle and epithelium, the iris sphincter and dilator, and stromal cells of the conjunctiva and uveal tract.
Local production, especially in the cornea, conjunctiva, sclera, and ciliary muscle, and systemic deposition, particularly in blood vessles and in the sclera, may contribute to amyloid deposits in FAF. To explain the complex pattern of deposition, microenvironmental factors such as lamellar architecture of the cornea and sclera, altered processing of gelsolin, or blood-tissue barriers must be invoked. In addition to corneal lattice dystrophy type II, the observed deposits help to explain glaucoma in patients with FAF.
PubMed ID
8088963 View in PubMed
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Primary hereditary systemic amyloidosis (Meretoja's syndrome): clinical features and treatment by plastic surgery.

https://arctichealth.org/en/permalink/ahliterature233886
Source
Scand J Plast Reconstr Surg Hand Surg. 1988;22(2):141-5
Publication Type
Article
Date
1988
Author
A E Rintala
A. Alanko
J. Mäkinen
R. Nordström
H. Salo
Author Affiliation
I Department of Surgery, Helsinki University Central Hospital, Finland.
Source
Scand J Plast Reconstr Surg Hand Surg. 1988;22(2):141-5
Date
1988
Language
English
Publication Type
Article
Keywords
Adult
Aged
Amyloid - metabolism
Amyloidosis - genetics - metabolism - pathology - surgery
Corneal Dystrophies, Hereditary - metabolism - pathology - surgery
Cutis Laxa - metabolism - pathology - surgery
Facial Muscles - metabolism - pathology
Facial Paralysis - metabolism - pathology - surgery
Female
Finland
Humans
Male
Middle Aged
Surgery, Plastic
Syndrome
Abstract
The characteristic, bloodhound-like appearance, which degenerates gradually, of patients with primary hereditary systemic amyloidosis, also called Meretoja's syndrome (MS), is attributable to amyloid degeneration of the craniofacial skin and peripheral facial nerves, but apparently also to amyloid deposits in the muscles; a finding not previously described. A material of five patients treated with plastic surgery is presented, and the peculiarities and differences of this rare disease in comparison with other peripheral neuropathies is discussed from a reconstructive viewpoint.
PubMed ID
3263697 View in PubMed
Less detail

7 records – page 1 of 1.