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PubMed1993

[Amyloidosis and hepatic amyloidosis].

The classification of amyloid and amyloidosis has undergone several revisions. The 1990 revision of the nomenclature at the 6th Internal Symposium on Amyloidosis in Oslo has been widely accepted and the basis for nomenclature and classification is the fibril protein making up the amyloid deposits. The liver is a major site of amyloid deposition in the disseminated form of the disease. Many studies have shown that the morphologic distribution of amyloid within the liver is not a reliable method for distinguishing AA from AL amyloidosis.

Amyloid↗
PubMed1997

Bilateral plantar amyloidosis: a unique presentation of localized cutaneous amyloidosis.

Nodular amyloidosis is uncommon and is due to a local production of amyloid by aberrant plasma cells. Localized bosselated plantar amyloidosis has been reported before but we present the first case to our knowledge of bilateral plantar amyloidosis. The clinical presentation as well as therapeutic options for this uncommon entity are reviewed.

Amyloidosis↗
PubMed1979

Amyloidosis of the skin: a comparison between localized and systemic amyloidosis.

Skin biopsies from patients with different forms of localized and systemic amyloidoses were studied. Subepidermal deposits, typical of lichen amyloidosus, were also seen in other types of amyloidosis, least frequent in the secondary systemic form. Amyloid within the epidermis and especially the horny layer as well as pigmented cells close to the deposits were found in all cases of lichen amyloidosus but in no other specimens. Plasma cells, on the other hand, were numerous in nodular amyloidosis but were not found in any other cases. It is concluded that in the pathogenesis of lichen amyloidosus the epidermis and perhaps dermal melanocytes are involved. In the pathogenesis of localized nocular amyloidosis the plasma cells might be of importance.

Amyloidosis↗
PubMed1997

Visceral organ involvement and extracellular matrix changes in beta 2-microglobulin amyloidosis--a comparative study with systemic AA and AL amyloidosis.

Patterns of amyloid distribution and extracellular matrix changes in the heart and gastrointestinal tract were compared among beta 2-microglobulin (B2M), AA (secondary), and AL (primary and multiple myeloma-associated) amyloidosis cases. B2M amyloid was found to be mainly distributed in the small arterioles, venules, endocardium and muscularis propria of these organs, the deposits characteristically forming subendothelial nodular lesions in the vessels. A marked increase of chondroitin sulfate (CS) was consistently detected in B2M amyloid. Heparan sulfate (HS) also showed an increase in amyloid deposits, but with less reactivity than CS in the small arterioles or venules. Basement membrane structures stained positively for laminin and collagen type IV were replaced by negative amyloid deposits. In the AL cases, the muscularis propria of the gastrointestinal tract was involved in amyloid deposits, as seen for the B2M type, but the vascular amyloid deposits were localized in the media and adventitia of larger vessels. Immunoreactivity for HS was more intense than that for CS, and no increase in laminin or collagen type IV was observed. In the AA cases, amyloid deposits were distributed in the capillaries, small arterioles, interstitium of the myocardium and mucosa. Immunoreactivity for laminin and collagen type IV was marked, and more intense than that for HS and CS. Although the existence of a direct relationship between increase in extracellular matrix material and amyloidogenesis remains to be proven, the observed variation in extracellular matrix changes in the background of each type of amyloidosis may indicate different binding sites of the amyloid precursor proteins, resulting in the specific histological features and distribution.

Adult↗
PubMed2000

Danish type gelsolin related amyloidosis: 654G-T mutation is associated with a disease pathogenetically and clinically similar to that caused by the 654G-A mutation (familial amyloidosis of the Finnish type).

BACKGROUND: Familial amyloidosis of the Finnish type (FAF, Finnish hereditary amyloidosis) is caused by a 654G-A mutation in the gelsolin gene on chromosome 9 resulting in the expression of mutant Asn-187 gelsolin which is abnormally proteolytically processed generating amyloidogenic fragments that polymerize into amyloid fibrils. We have recently shown that in a Danish and a Czech family with a clinical syndrome similar to FAF, including corneal lattice dystrophy, cranial neuropathy and skin changes, the disease is caused by another mutation at the same position, namely 654G-T predicting a Try-for-Asp substitution at 187 in secreted gelsolin. AIM: To undertake a closer examination of the Danish subtype of FAF and report immunohistochemical and biochemical findings. RESULTS: Immunostaining of plasma gelsolin isolated from heterozygous FAF of the Danish subtype revealed a pattern similar to that found in FAF-Asn 187. The > 60 kDa gelsolin species contain an epitope characteristic of the amyloid forming region as revealed by an amyloid specific antibody, whereas the approximately 50 kDa fragments are devoid of it. Compared with the wild-type gelsolin peptide (Asp-187), the corresponding mutant peptide (Tyr-187) showed dramatically increased fibrillogenicity as revealed by quantitative thioflavine-T based fluorimetry; ultrastructurally, amyloid-like fibrils were formed by the mutant peptide. Immunohistochemistry showed that antibodies directed against residues 231-242 of secreted gelsolin, representing the carboxy terminus of the sequence forming the amyloid protein (residues 173-243) laid down in the tissues in a fibrillar form in FAF, specifically labelled the amyloid deposited in rectum and skin in the Danish (654G-T) subtype. CONCLUSIONS: The 654G-T mutation in the gelsolin gene gives rise to an amyloid disease clinically and pathogenetically similar to that caused by the 654G-A mutation.

Amyloid↗
PubMedDate not supplied

[Primary localized cutaneous amyloidosis--lichen amyloidosis].

This case report presented a female patient with primary-localized-cutaneous-amyloidosis in the form of lichen amyloidosus. Primary-localized-cutaneous-amyloidosis is a rare idiopathic dermatosis caused by abnormal deposition of amyloid composed primarily of degenerated keratin filaments. In order to establish the final diagnosis, detailed clinical and laboratory investigations were performed, with a particular emphasis on pathohistological analysis of skin specimens, special stains, and electron microscopy.

Adult↗
PubMedDate not supplied

Friction melanosis, friction amyloidosis, macular amyloidosis, towel melanosis: many names for the same clinical entity.

Macular or friction amyloidosis is a cutaneous entity characterized by a brownish pigmentation distributed on the skin over bony regions of the trunk and limbs after the use, for many years, of a nylon towel or scrub brush to clean the skin. Electron microscopy is necessary for the diagnosis of this dermatosis and reveals deposits of amyloid in the papillary dermis. This condition is relatively unknown in Western countries. In this report, we describe 24 Italian patients affected by friction amyloidosis which was caused by the use of cotton towels, horse-hair gloves or artificial and rough sponges to clean their skin.

Adult↗
PubMed1978

Partial characterization of amyloid proteins in inherited amyloidosis with lattice corneal dystrophy and in secondary amyloidosis.

Amyloid fibrils isolated from two patients, one with inherited systemic amyloidosis and lattice corneal dystrophy, and the other with secondary amyloidosis due to chronic glomerulonephritis, were studied using immunologic, electrophoretic and chromatographic techniques. Amino acid hydrolysates of both amyloid types showed a high proportion of acidic and aliphatic amino acid residues but were non-identical in the overall amino acid composition. The preparations also contained 12--16% lipids. Guanidine hydrochloride denaturated amyloid fibrils of both types were resolved into four fractions in Sepharose 6B chromatography with molecular weights of ca. 160 000, 45 000, 20 000 and 8 000. The 160 000 mol. wt. fraction predominated in the chromatograms of inherited amyloid protein and was further resolved into two main fractions of 17 000 and 15 000 mol. wt. in sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. None of these fractions from inherited amyloid protein showed immunologic identity with tissue-derived amyloid protein A (AA) whereas all four fractions from secondary amyloid reacted against anti-AA antiserum. The three major Sepharose 6B fractions of secondary amyloid fibrils were resolved into a 25 000 mol. wt. fraction in SDS-polyacrylamide gel electrophoresis without urea but into a 12 000 mol. wt. fraction in gels containing 8M urea after more drastic dissolving conditions of the fibrils.

Adult↗
PubMed1987

A molecular-pathologic approach to murine senile amyloidosis. Serum precursor-apolipoprotein A-II variant (Pro5----Gln) presents only in the senile amyloidosis-prone SAM-P/1 and SAM-P/2 mice.

Murine apolipoprotein (apo) A-II is a serum precursor of murine senile amyloid protein. We determined the primary structures of apo A-II in accelerated senescence-prone mice (SAM-P) characterized by a high frequency of age-associated systemic amyloidosis and accelerated senescence-resistance mice (SAM-R) in which senile amyloidosis occurred with a low incidence. Apo-A-II variant (Pro5----Gln) was found to be present only in the serum of SAM-P and not in that of SAM-R or other random bred slc:ICR mice. The apo A-II variant in the serum of SAM-P is identical to the murine senile amyloid fibril protein (ASSAM) derived from amyloid-deposited tissues of SAM-P. These findings proved that apo A-II deposits in tissues without degradation and this mutation (Pro5----Gln) probably have significant effects on the structure and function of apo A-II and would play a critical role in murine senile amyloidogenesis.

Aging↗
PubMed1971

Transfer amyloidosis. I. Studies on the transfer of various lymphoid cells from amyloidotic mice to syngeneic nonamyloidotic recipients. II. Induction of amyloidosis in mice with spleen, thymus and lymph node tissue from casein-sensitized syngeneic donors.

Lymphoid cells from various lymphoid organs were transferred from amyloidotic mice to normal syngeneic recipients. The recipients were treated with nitrogen mustard. Only the recipients of spleen cells developed amyloidosis. Furthermore, slices of spleen, thymus and lymph node from casein-sensitized mice were transplanted to kidneys of normal syngeneic mice. The recipients were treated with ten casein injections, and they all developed amyloidosis. The results from both experiments indicate that amyloid is formed by macrophages due to a stimulation of these cells with both antigen and an amyloid-inducing factor released from the pyroninophilic lymphoid cells.

Amyloidosis↗
PubMed1996

[Cardiac involvement in amyloidosis. Apropos of a case of hereditary amyloidosis of neurologic expression].

The authors report a case of hereditary amyloidosis in a 54-year old patient with an essentially neurological clinical expression. The cardiovascular assessment, consisting of echocardiography performed systematically while the patient was free of any cardiac symptoms, revealed typical amyloid infiltration with a hyperechoic, shiny appearance of the myocardium and significant parietal hypertrophy. Systolic function was preserved, in contrast with impairment of diastolic function, revealed by the presence of Appleton type I mitral blood and decreased propagation velocity of the transmitral flow on colour TM. The authors stress the importance of ultrasonographic examination in all patients with suspected cardiac amyloidosis, even in the absence of clinical or electrical signs.

Amyloidosis↗
PubMed1997

Familial subepithelial corneal amyloidosis--a lactoferrin-related amyloidosis.

PURPOSE: To isolate the protein that collects in increased amounts beneath the corneal epithelium in familial subepithelial corneal amyloidosis (FSCA), also known as gelatinous droplike corneal dystrophy, and to identify it by N-terminal amino acid sequencing. METHODS: Peptides resulting from pepsin digestion of a unique protein isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis from frozen tissue from two corneas with FSCA were purified by high-pressure liquid chromatography followed by protein sequence analysis. The protein was identified by amino acid sequencing, Western blotting, and immunohistochemistry. RESULTS: A protein was identified in two corneas with FSCA that was not present in normal corneas or in corneas with other disorders. The amino acid sequences of two peptides derived from this protein were identical to portions of lactoferrin. The unique protein reacted with rabbit antihuman lactoferrin after Western blotting. The presence of lactoferrin in the amyloid within affected corneas was confirmed using the immunoperoxidase method on formalin-fixed, paraffin-embedded tissue sections and lactoferrin antiserum. CONCLUSIONS: Corneal tissue with FSCA contains lactoferrin, and this is the first form of amyloidosis found to be associated with this protein. Because lactoferrin is a product of lacrimal glands, the corneal lactoferrin may be derived from the tears. Because the gene for lactoferrin is on chromosome 3 (3q21-q23), this locus is a potential site for the FSCA gene.

Adolescent↗
PubMed2006

Aging and transthyretin-related amyloidosis: pathologic examinations in pulmonary amyloidosis.

Although aging is closely related with the onset of senile systemic amyloidosis (SSA) caused by wild-type transthyretin (TTR), the effect of aging on amyloid formation has remained unclear in familial amyloidotic polyneuropathy (FAP), caused by variant- and wild-type TTR. The aim of this study was to elucidate the effects of aging and/or other factors in FAP on amyloid formation in the lung, one of the most important target organs of amyloid deposition in SSA. Pulmonary amyloid distribution was determined using 19 autopsied lung samples from patients with FAP amyloidogenic TTR (ATTR) V30M, the most common type of FAP. Amyloid deposition was observed around the walls of the bronchi/ bronchioles, the pulmonary arteries, and the pulmonary veins, while no amyloid deposits could be found around the lymphatics. In addition, amyloid deposition in the alveolar regions was a characteristic finding in aged patients with FAP ATTR V30M (average ages of the patients with amyloid positive vs. negative: 50.55 +/- 8.75 vs. 39.75 +/- 4.17 years old, p < 0.005), similar to the finding in one SSA patient. These results suggest that aging could play an important role in the progression of pulmonary amyloid formation in FAP ATTR V30M.

Adult↗
PubMed1978

Cardiac amyloidosis in hereditary neuropathic amyloidosis diagnosed by endomyocardial biopsy.

A 57 year old male first developed progressive neuropathy of the lower extremities and then similar involvement in the upper extremities. Two years later he developed dyspnea and then complete atrioventricular block requiring the use of a permanent cardiac pacemaker. An older brother had an almost identical clinical course, including the installation of a permanent pacemaker. Both died of left ventricular failure. An endomyocardial biopsy revealed extensive amyloidosis and fibrosis of the myocardium. This is the first report of a myocardial biopsy showing amyloid on electron microscopy.

Amyloidosis↗
PubMed1999

[Amyloidosis: rapid course of AL-amyloidosis in a patient without myelomatosis].

A case of severe AL-amyloidosis in a 72-year-old man is presented. Amyloid was especially deposited in the kidneys and the liver. The patient died one year after diagnosis with impaired kidney function and severe ascites. Despite the type of amyloid (AL-type), multiple myelomata or lymphoproliferative disease could not be demonstrated.

Aged↗
PubMed1988

Plasmacytoma and gastric amyloidosis associated with nodular pulmonary amyloidosis.

The authors report an association of gastric and pulmonary amyloidosis in a 74 year old woman. The patient had had a gastric plasmacytoma for the last 11 years. On autopsy, the stomach was found to contain intramural deposits of amyloid, and was infiltrated by plasma cells secreting monoclonal IgG lambda light chain. In the lungs, the plasma cells in the vicinity of the amyloid deposits proved to be polytypic, suggesting that these deposits originated from circulating precursor proteins.

Amyloidosis↗
PubMed1984

Ultrastructural investigation of amyloidosis. Pathogenesis of systemic amyloidosis.

Three types of ultrastructural changes in the cell membrane observed in the formation and accumulation of amyloid fibrils in systemic amyloidosis were described: in type I change (contact loss type), unusual dilatation of the intercellular gaps accompanied by occasional disappearance of the tight junction and desmosomes appeared. Type II change (indentation or cystic invagination type) showed cone-shaped indentations or cave-like cystic invaginations. Type III change (surface fold type) consisted of newly developed or inherent surface folds. The widened intercellular gaps of type I, advanced indentation or invagination of type II and the disrupted surface folds of type III resulted in atrophy of the cells and final replacement by amyloid. The author believes that amyloid fibrils are produced by many cells, not by a certain specific cell, extracellularly.

Amyloid↗