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Biomedical subjects

E F Osserman

Publications and source records attributed to E F Osserman.

At least 55 records · Page 3Linked to original sources
PubMed1976

Experimental Bence Jones cast nephropathy.

C3H mice received intraperitoneal injections of a single dose of 50 to 200 mg. of purified lambda Bence Jones protein. Control animals received injections of comparable amounts of ovalbumin. The mice which received 200 mg. of lambda Bence Jones protein developed extensive cast formation in the distal renal tubules. By electron microscopy, the casts were found to contain elongated crystalloid structures. In some areas, these crystalloids appeared to penetrate into or be engulfed by tubular epithelial cells. By immunofluorescence, only lambda Bence Jones protein was detectable in the casts during the first 5 days. Thereafter, Tamm-Horsfall protein was also found in increasing amounts. The casts induced an inflammatory response characterized by the sequential appearance of polymorphonuclear leukocytes and mononuclear cells. The secondary tubular cell changes included atrophy, degeneration, and regeneration. Giant cells were present around many casts, but it could not be determined whether these derived from tubular epithelial or mononuclear inflammatory cells. Elevated blood urea nitrogen was found terminally in most animals. Smaller doses of the same protein as well as preliminary studies with two other lambda Bence Jones proteins failed to produce comparable changes. This experimental model of Bence Jones nephropathy closely resembles the morphologic features of so-called "myeloma kidney" in man.

Animals↗
PubMed1975

IgA heavy chain disease. A case detected in the western hemisphere.

IgA heavy chain disease (alpha chain disease) was detected in a 46 year old South American (Colombian) of mixed Spanish and Indian (Mestizo) descent. The clinical course was characterized by severe malabsorption, initially thought to be a variant of tropical sprue. Jejunal mucosal biopsy revealed marked villous atrophy with heavy infiltration of the lamina propria by a single monotonous cell type which, by light microscopy, had the appearance of either a large, abnormal plasma cell or a small histiocyte. Electron microscopy of the biopsy specimen demonstrated the presence of abnormal plasma cells, lymphatic distention and abnormalities of surface epithelial cells. At autopsy a 6 by 3 cm mass was found in the right para-aortic area along with many firm 2 cm mesenteric and para-aortic lymph nodes. Histologic examination revealed the presence of a monotonous cell type similar to that found in the jejunal mucosal biopsy specimen.

Abdomen↗
PubMed1975

Primary structure of a deleted human lambda type immunoglobulin light chain containing carbohydrate: protein Sm lambda.

An internal molecular deletion occurring in a human lambda type immunoglobulin light (L)-chain (Sm lambda) has been defined by sequence analysis. The Sm protein was isolated from the urine of a patient with a plasma cell dyscrasia involving the synthesis of an IgG molecule with both deleted gamma and lambda subunits. The Sm lambda polypeptide chain has an approximate molecular weight of 15,000 and contains 135 amino-acid residues. The constant (C) region is fully intact, comprising 105 residues, whereas the variable region (V) has only 30 residues. The V-region segment represents residues 1 through 30 of normal lambda chains and possesses considerable homology (87%) to lambda chains of subgroup II. Since lambdaII proteins normally contain 216 amino-acid residues, the defect represents an intramolecular deletion of 81 residues, which is entirely confined to the carboxyterminal three-quarters segment of the V-region, with a resumption of normal synthesis at a glutaminyl residue at position 110, the initiation point of the C-region. Carbohydrate is attached to an Asx residue at position 25, in the first hypervariable region, associated with the sequence triplet Asx-Ser-Ser, which is postulated to be a common recognition site for glycosylation of immunoglobulins. The carbohydrate moiety is a complex oligosaccharide with a branched chain structure containing sialic acid, fucose, mannose, N-acetylglucosamine, and galactose. These structural studies and other findings suggest that restricted areas in the DNA of immunoglobulin genes, such as the hinge regions of heavy (H) and light (L) chains and the hypervariable regions, are particularly susceptible to breakage and reunion. We postulate that the genetic defect of protein Sm could have originated from a somatic mutational event in the plasmacyte precursor during or after the integration of the V and C genes. These studies provide additional support for the hypothesis and two distinct structural genes encode a single immunoglobulin polypeptide chain.

Amino Acid Sequence↗
PubMed1973

Structural identity of Bence Jones and amyloid fibril proteins in a patient with plasma cell dyscrasia and amyloidosis.

The partial amino acid sequence of the amyloid fibril protein isolated from the small intestine of a patient with plasma cell dyscrasia and associated amyloidosis has been determined and compared with the sequence of the kappa-type Bence Jones protein isolated from the urine of the same patient. Identical sequences were observed for the 27 amino-terminal residues that could be compared. The C-terminal tryptic peptide of the amyloid protein was identical with that of the Bence Jones protein. Apparent molecular weights and amino acid compositions of the Bence Jones and amyloid proteins were similar. It appears, therefore, that the predominant protein present in the amyloid deposits in this patient was an intact kappa-type light polypeptide chain that was identical with the urinary Bence Jones protein.

Amino Acid Sequence↗