Clinical relapse in systemic lupus erythematosus: correlation with antecedent elevation of urinary free light-chain immunoglobulin.

This paper reports preliminary evidence suggesting that measurements of free light-chain Ig (FLIg) in urine may represent quantitative markers of in vivo polyclonal B-cell activation. Thus, longitudinal levels of urinary FLIg in patients with systemic lupus erythematosus (SLE) may be used to track or monitor the in vivo immunopathologic B-cell activity of SLE and be helpful in predicting a disease relapse. Our findings showed that dramatic rises in urinary FLIg occurred during asymptomatic intervals that preceded by 4-8 weeks the first symptomatic signs of acute SLE relapse.

Restriction of blood and marrow CLL-B cells to free L-chain Ig secretion: implication for normal B-cell function and control.

The culture supernatant immunoglobulin (CSIg) of blood mononuclear cells (MNCs) from 14 patients with chronic lymphocytic leukemia (CLL) was determined using a panel of nanogram-sensitive radioimmunoassays that measured IgM, IgG, IgA, total kappa-Ig, and total lambda-Ig. Bone marrow cells from three patients were also cultured and the blood and marrow CSIg results were compared. The CSIg of 1-day cultures was employed as a measure of shed surface membrane Ig (SmIg) for the 7- and 14-day cultures.

Blockade by brefeldin A of intracellular transport of secretory proteins in mouse pituitary cells: effects on the biosynthesis of thyrotropin and free alpha-subunits.

We examined the effect of brefeldin A (BFA), a drug that inhibits the intracellular translocation of newly synthesized glycoproteins, on the biosynthesis of TSH and free alpha-subunits by pituitary tissue from hypothyroid mice. Incubation of tissue with 5 or 10 micrograms BFA/ml for 3.5 h caused marked dilatation of rough endoplasmic reticulum (RER) and mild swelling of Golgi in all pituitary cell types.

Structures of high-mannose oligosaccharides of mouse thyrotropin: differential processing of alpha- versus beta-subunits of the heterodimer.

We have determined the structures of high mannose (Man) oligosaccharide units of the alpha- and beta-subunits of mouse TSH heterodimers and of free alpha-subunits. Mouse thyrotropic tumor tissue, or pituitaries from euthyroid or hypothyroid mice, were incubated with D-[2-3H]Man, homogenized, and incubated in the presence or absence of pH 3 buffer to dissociate heterodimers. Highly enriched TSH beta-subunits, or TSH heterodimers, were obtained using anti-TSH beta serum and free alpha-subunits were subsequently obtained using anti-LH alpha-serum.

The subcellular sites of sulfation of mouse thyrotropin and free alpha subunits: studies employing subcellular fractionation and inhibitors of the intracellular translocation of proteins.

To determine the subcellular sites of sulfation of thyrotropin (TSH) and free alpha-subunits, mouse thyrotropic tumor minces were incubated simultaneously with [3H]Met and [35S]SO4 for 1 or 3h, homogenized, and fractionated by discontinuous sucrose gradient ultracentrifugation. Dual-labeled TSH or free alpha-subunits were immunoprecipitated, and analyzed by SDS-gel electrophoresis. Endoglycosidase F released all [35S], but little [3H], from the dual-labeled species, indicating that [35S]SO4 was incorporated into oligosaccharides of TSH and free alpha-subunits.