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P Westermark

Publications and source records attributed to P Westermark.

At least 163 records · Page 9Linked to original sources
PubMed1985

Systemic amyloidosis: a review with emphasis on pathogenesis.

Our knowledge about the composition of the deposits in amyloidosis has increased considerably during the last decade. Three different protein groups have been shown to form fibrils in systemic amyloidosis, namely monoclonal immunoglobulin light chains in primary and myeloma-associated amyloidosis, protein AA in secondary amyloidosis and prealbumin in the familial and senile forms of systemic amyloidosis. This review deals with known and postulated pathogenetic mechanisms involved in the creation of fibrils from these proteins.

Aging↗
PubMed1985

Serum prealbumin and retinol-binding protein in the prealbumin-related senile and familial forms of systemic amyloidosis.

In a series of 13 elderly patients with proven prealbumin-related senile systemic amyloidosis (SSA), depressed serum prealbumin values (110.7 +/- 14.1 micrograms/ml) were found as compared to an age-matched control group (175.1 +/- 20.3 micrograms/ml). As expected, there was a significant correlation between serum prealbumin and serum retinol-binding proteins in both groups of patients. Patients with reactive amyloid protein AA amyloidosis had slightly depressed serum prealbumin concentrations, whereas patients with prealbumin-related familial amyloidosis of Swedish type had prealbumin values within normal limits. Since the serum levels of the acute phase reactants, haptoglobin and amyloid-related serum protein AA, were higher in the group of patients with reactive amyloidosis than in patients with SSA, the depression of the prealbumin levels in SSA is not a result of inflammation. Since SSA is known to contain prealbumin, it is possible that a disturbed prealbumin metabolism in old age results in low prealbumin serum values and deposition of amyloid.

Adult↗
PubMed1984

Demonstration of amyloid protein AA in old museum specimens.

Three amyloid-infiltrated organs, which had been stored in fixative for 65 to 83 years, were obtained from a collection of pathologic tissues. All the tissues originated from persons with pulmonary tuberculosis. Amyloid fibril protein AA, typical of secondary systemic amyloidosis, was demonstrated in all the tissues by the peroxidase-antiperoxidase method. Protein AA was also extracted and purified from the tissues in spite of the long period in fixative.

Adult↗
PubMed1984

Senile systemic amyloidosis.

The senile amyloidoses comprise a heterogeneous group of disorders with deposition of amyloid in a variety of tissues. Most of these amyloidoses are localized to one tissue. It has been shown previously that the amyloid fibrils in one form of senile amyloidosis affecting the heart contains a prealbumin-related protein, ASc1. It is shown in this paper by immunohistochemical study using a specific anti-protein ASc1 antiserum that this type of amyloidosis, previously called senile cardiac amyloidosis, is a systemic disease with amyloid deposits in many organs. The designation senile systemic amyloidosis is proposed for this disease, which differs from other systemic amyloidoses in distribution of amyloid deposits.

Aged↗
PubMed1983

Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin.

Amyloid deposition is the most typical islet alteration in Type 2 (non-insulin-dependent) diabetes. In the present study we show by immunohistochemistry that the amyloid reacts with an antiserum against insulin B chain. Islet amyloid was also purified, dissolved in guanidine-HCl and gel filtered on a Sepharose 6B column. Immunization of a guinea pig with a high molecular weight fraction from this gel filtration resulted in an antiserum with insulin-binding capacity. This binding was partially blocked with pure insulin B chain. The results indicate that islet amyloid contains insulin B chain and that the amyloid is a product of the islet B cells. Thus the study support previous morphological studies.

Aged↗
PubMed1983

Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation.

Atrium, ventricle, aorta, lung, kidney, and rectum were removed at autopsy from 85 consecutive elderly patients (aged 80 years or older) and examined for amyloid with Congo red. All tissues containing amyloid were counterstained with an antiserum specific for amyloid fibril protein ASc1 and studied by immunofluorescence. Three distinct forms of amyloid were found: (1) all patients had senile aortic amyloid; (2) 78 percent of patients had isolated atrial amyloid; and (3) 25 percent of patients had senile cardiac amyloid of the ASc1 type. The cardiac amyloid deposits were small and widely scattered in more than 80 percent of patients with isolated atrial amyloid and in more than 50 percent of patients with ASc1-type amyloid. Of 21 patients with ASc1 amyloid, 19 had extracardiac involvement (lung in 81 percent of cases and rectum in 57 percent of cases). The kidney was not involved in any patient. The mean heart weight, frequency of atrial fibrillation, percentage of patients with heart failure, and frequency of myocardial infarction were increased in patients with cardiac amyloid, but these differences failed to reach statistical significance. There was no difference in the mean left ventricular wall thickness or degree of coronary atherosclerosis.

Aged↗
PubMed1983

Immunofluorescence and histochemical studies of localized cutaneous amyloidosis.

Lichen amyloidosus (LA) and macular amyloidosis (MA) are two forms of localized cutaneous amyloidosis in which the amyloid occurs as larger and smaller deposits respectively in the papillary dermis. The histogenesis of the amyloid of these conditions is unknown. By using an indirect immunofluorescence technique we showed that LA and MA do not react with antibodies against different previously characterized amyloid fibril proteins. These results indicate that the amyloid of LA and MA is different from other known types of amyloid. Protein AP, which was demonstrated in amyloid of MA and LA, is known to be present in all forms of amyloid and is of unknown significance. Antiserum against keratin did not react with the larger homogeneous amyloid bodies, but showed a weak reaction with some small deposits. Histochemical staining failed to show keratin in any of the tissues containing LA or MA.

Adult↗
PubMed1983

Amino acid sequences in amyloid proteins of kappa III immunoglobulin light-chain origin.

The main amyloid fibril (AL) proteins extracted from the spleen of Patient So 124 with systemic amyloidosis and from a skin nodule of Patient KSA with localized amyloidosis were studied by partial amino acid sequence analysis and proved to be of kappa III immunoglobulin light-chain origin. The sequences were similar to that of Bence Jones protein V and, which has been reported to have a unique kappa III subset sequence. Thus, except for position 9 in protein AL(KSA), the amino acid sequences were identical to position 25 in AL(So 124) and in AL(KSA). The question is being raised whether this kappa III subset might contain amyloidogenic sequences.

Aged↗
PubMed1983

Protein AA in primary and myeloma associated amyloidosis.

Protein AA, the main fibril constituent in secondary systemic amyloidosis, was demonstrated by the peroxidase-anti-peroxidase method in kidney sections from five out of 14 cases of primary and myeloma associated amyloidosis, all having an immunoglobulin light chain derived protein as a major subunit. In three of these cases, protein AA was also demonstrated in double immunodiffusion of dissolved amyloid preparations. The protein had the characteristics of protein AA in elution position, immunodiffusion and isoelectric focussing pattern. The significance of protein AA in primary and myeloma associated amyloidosis is unknown.

Amyloid↗
PubMed1983

Amyloid of the seminal vesicles. A distinctive and common localized form of senile amyloidosis.

Amyloid deposits were found subepithelially in the seminal vesicles of 34 of 209 consecutively studied men. The incidence increased with age and was found in 21% of men over 75 years. This senile seminal vesicle amyloidosis (SSVA) is a localized disorder, and the amyloid substance has unique histochemical and immunochemical properties not shared with any other amyloid described until now.

Aged↗
PubMed1982

The heterogeneity of protein AA in secondary (reactive)systemic amyloidosis.

In secondary systemtic amyloidosis, amyloid fibrils have protein AA as a main subunit protein. As judged from gel chromatography and electrophoresis, this protein is rather homogeneous. In the present paper it is shown, however, that protein AA is very heterogeneous and composed of many peptides with different isoelectric points. However, their antigenic properties and amino acid compositions vary only little. It is concluded that protein AA is as heterogeneous as its postulated precursor, the acute phase reactant serum AA and that a theory that only one or a few serum protein AA's can give rise to amyloid fibrils, might be wrong.

Amino Acids↗
PubMed1982

Localized laryngeal amyloidosis: partial characterization of an amyloid fibril protein AL.

Amyloid fibrils were extracted from a patient Wr with more than 10 yr history of localized laryngeal amyloidosis. Degraded amyloid fibrils reacted in immunodiffusion with an antiserum against an amyloid protein of immunoglobulin kappa light chain origin, showing a line of identity with a kappa I amyloid protein. The protein Wr had a blocked aminoterminal, previously only reported in lambda chains. Amino acid sequence analysis of a fragment of the protein showed it to be an immunoglobulin light chain protein of V kappa I or V kappa III subgroup. The protein had a few unusual amino acid residues as compared to other kappa light chains. The findings support the view that the fibrils in localized, tumour-like amyloidosis are composed by homogeneous immunoglobulin light chain proteins in the same way as is seen in primary and myeloma associated systemic amyloidosis. It is possible that unusual light chains are over-represented in amyloid fibrils.

Amino Acid Sequence↗
PubMed1982

Senile aortic amyloid. A third distinctive type of age-related cardiovascular amyloid.

Aortic tissues from 22 elderly patients were analyzed by Congo red staining for amyloid deposits. All samples contained amyloid, which was resistant to the potassium permanganate reaction. Tryptophan was present in all amyloid deposits. The amyloid failed to react with antiserums to amyloid fibril protein ASc1 or human prealbumin, proteins previous demonstrated in generalized senile cardiac amyloid. It also differed from age-related isolated atrial amyloid, which has been shown to lack tryptophan. Deposits did not react with antiserums specific for amyloid fibril proteins of the A lambda IV, A lambda VI, AA, or AEt types. These results indicate that senile aortic amyloid is distinct from amyloid present in primary and secondary amyloidosis and appears to represent a third form of cardiovascular amyloid associated with the aging process.

Aged↗
PubMed1982

Senile cerebral amyloid. Prealbumin as a common constituent in the neuritic plaque, in the neurofibrillary tangle, and in the microangiopathic lesion.

Three lesions that characterize the nosologic findings in the brain of Alzheimer's presenile dementia and senile dementia of Alzheimer type, ie, neuritic plaque, neurofibrillary tangle, and microangiopathy, all are frequently associated with amyloid deposition. There has been some question, however, as to whether these lesions share the same etiology. Moreover, the specific chemical nature of amyloid associated with these lesions has not yet been determined. In the present study, formalin-fixed paraffin sections of the affected brains were tested immunocytochemically for their reactivity against antiserum to prealbumin (recently disclosed as the major constituent of amyloid associated with familial amyloidotic polyneuropathy as well as senile cardiac amyloid) and known components of other types of amyloid (AA, AP, etc.). The results demonstrated that amyloid deposits in all three lesions reacted with anti-prealbumin, suggesting that it is a common constituent of these lesions. Indeed, it is likely that prealbumin is the major constituent of amyloid associated with neuritic plaque, neurofibrillary tangle, and microangiopathy.

Alzheimer Disease↗
PubMed1982

Immunohistochemical evidence for the lack of amyloid P component in some intracerebral amyloids.

Sections of brain tissue from patients with Alzheimer's disease with amyloid deposits in vessels, in plaques, and within nerve cells were studied by means of an immunoperoxidase method using a specific antiamyloid P component (AP) antiserum. Amyloid deposits in vessels were found to be strongly positive for protein AP, whereas the Alzheimer's plaques and the neurofibrillary tangles were negative or only weakly positive. The absence of protein AP in some intracerebral amyloid deposits might be due to an inability of the protein AP in some intracerebral amyloid deposits might be due to an inability of the protein to penetrate the blood-brain barrier. These findings support the theory that protein AP is absorbed to already formed amyloid fibrils, but the possibility that it may participate in the formation of vascular amyloid cannot be dismissed. The findings also indicate that protein AP is not necessary for the formation of amyloid fibrils at least in some forms of cerebral amyloidosis.

Alzheimer Disease↗