Renal complications of B-cell dyscrasias

Article Abstract:

The kidneys are often the organ in which disease first becomes apparent. Albumin in the urine is frequently the first sign of abnormal protein deposits from systemic diseases, among them, B cell dyscrasias. Light-chain (part of the immunoglobulin molecule) amyloid is a starch-like protein-polysaccharide produced and deposited in the tissues during certain chronic diseases. B cell dyscrasia, or disease of the lymphocyte cells in the bone marrow, is present in most patients with light-chain amyloid disease, but may not be apparent. Light-chain deposition may show up in one of two ways: moderate amounts of protein in the urine, or acute kidney failure, myeloma, and the classic features of Bence Jones cast nephropathy (deposits causing hardening of kidney tissues). The least common form of this type of disorder, light- and heavy-chain deposition disease, usually begins with albumin in the urine and occult (hidden) B cell dyscrasia. With the development of modern methods of testing, the chemical composition of different amyloid proteins has been documented, and diagnosis has become more precise. Light-chain deposition disease was only recognized 15 years ago, and since then reports of over 150 cases indicate that the disease is not rare. Alan Solomon and his colleagues add to the knowledge of this disease in the June 27, 1991 issue of The New England Journal of Medicine with an experimental model of the importance of the Bence Jones protein in kidney disease. (Consumer Summary produced by Reliance Medical Information, Inc.)

Abnormalities, B cells, editorial

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Nephrotoxic potential of Bence Jones proteins

Article Abstract:

Bence Jones proteins are light chains that are part of the immunoglobulin molecule. They are associated with several diseases in which the build-up of light chains in the tissues and bones causes impairment and toxic effects. These diseases include myeloma nephropathy, light-chain deposition disease, and amyloidosis, all of which involve a build-up of light chains and subsequent kidney deterioration. Many factors may be involved in kidney damage among these patients, but it is likely that differences in the physical and chemical properties of the proteins determine whether they are harmful or not. Forty patients with multiple myeloma or amyloidosis AL and Bence Jones proteinuria were examined, most at autopsy, to demonstrate the applicability of a mouse model in distinguishing malignant from benign Bence Jones proteins. The results implicate the protein as the factor responsible for the pathological changes in the kidneys. How the protein is deposited in the kidney is determined by structurally distinctive, and still unknown, aspects of individual proteins. (Consumer Summary produced by Reliance Medical Information, Inc.)

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Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans

Article Abstract:

A gene mutation in the transthyretin protein may be responsible for the increased incidence of amyloidosis in the hearts of blacks with unexplained heart disease. Amyloidosis is caused by abnormal deposits of the protein amyloid in various tissues. Researchers tested samples of heart tissue taken at autopsy from 32 blacks and 20 whites with cardiac amyloidosis and 228 people who died of other causes. Twenty-three percent of the blacks had a gene mutation called Ile 122 in the transthyretin protein compared to none of the white patients.

Health aspects, Diagnosis, Gene mutations, Gene mutation, African Americans, Genetic aspects, Cardiomyopathy, Myocardial diseases

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