Evaluation of systemic amyloidosis by scintigraphy with 123-I-labeled serum amyloid p component

Article Abstract:

Systemic amyloidosis, a metabolic disorder, is characterized by the deposition of a waxy compound called amyloid that interferes with the function of vital body organs. There are two forms of the disease that have been recognized: AL amyloidosis, which is found in patients with pathologic development of cells which produce antibodies, and AA (also called reactive) amyloidosis, which is found in patients with chronic inflammatory conditions. Both of these subtypes of amyloidosis are serious and often fatal. The usual means of diagnosing the condition is to obtain biopsy specimens in order to detect the accumulation of amyloid within the organs. But this method gives little information concerning the spread of the condition and its progress. Certain patients have recently been found to be greatly improved by the administration of colchicine, but without a clear marker to follow the progress or improvement of the condition it is difficult to control therapy. Serum amyloid P (SAP) is a normal protein present in the blood. This blood protein binds strongly with the amyloid fibers which are present in the diseased tissues in amyloidosis. The present study used SAP which had been labelled with radioactive iodine (123-I) to identify the sites, and to some degree the level, of amyloid deposition in patients with amyloidosis. Accompanying nuclear camera plates (scintigrams) clearly showed the accumulation of the radioactive iodine within the tissues of living patients. One patient who had received the radioactive SAP died. This allowed organs obtained at autopsy to be measured and the distribution of SAP in the body to be calculated. The study includes data from scintigrams obtained from 25 amyloidosis patients and 50 patients with other diagnoses (controls). Control patients failed to show uptake of 123-I, but a diagnostic pattern of amyloid deposition was found in patients with AA and AL types of amyloidosis. This method appears to be highly useful for diagnosing, classifying and following the progression of amyloidosis. (Consumer Summary produced by Reliance Medical Information, Inc.)

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New frontiers in the study of amyloidosis

Article Abstract:

The August 23, 1990 issue of The New England Journal of Medicine includes an article about a new and powerful assay for the diagnosis of amyloidosis. Systemic amyloidosis, a metabolic disorder, is characterized by the deposition of a waxy compound called amyloid that interferes with the function of vital body organs. There are two forms of the disease that have been recognized: AL amyloidosis, which is found in patients with pathologic development of cells which produce antibodies; and AA (also called reactive) amyloidosis, which is found in patients with chronic inflammatory conditions. Both of these subgroups of the disease are serious and often fatal. The usual means of diagnosing the condition is to obtain biopsy specimens and measure the accumulation of amyloid within the organs. The amyloid fibers stain red with standard stains used in the preparation of microscopic slides. When the tissues are stained with the dye Congo red, they appear apple-green, and when examined in polarized light they appear as bright filaments. The new technique involves the use of serum amyloid P (SAP), a normal component of the blood. This blood protein is attracted to and binds strongly with the amyloid fibers which are present in the diseased tissues in amyloidosis. This study used SAP which had been labelled with radioactive iodine (123-I) to identify the locations and the amount of amyloid deposition in patients. While it is likely that microscopic examination of biopsy samples will remain the 'gold standard' of diagnosis for some time (in part because of its low cost), this new test appears to be a valuable addition to the physician's diagnostic arsenal. (Consumer Summary produced by Reliance Medical Information, Inc.)

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Amyloidosis

Article Abstract:

A study is conducted on amyloidosis, which is a clinical disorder caused by extra cellular deposition of insoluble abnormal fibrils, derived from aggregation of misfolded, normally soluble, protein. It is seen that though the diagnosis of the disease remains a considerable clinical challenge, specialist centers are having greatly improved outputs for the patients.

United States, Causes of, Disease/Disorder overview

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