Biomedical subjects
Publications and source records attributed to J Lieberman.
A 34-year-old woman with homozygous a1-antitrypsin deficiency suffered from progressive, generalized cystic bronchiectasis. Although bronchiectasis was reported in the original monograph on the enzyme inhibitor deficiency, it has received minimal attention since then. Alpha1-antitrypsin levels should be measured in patients with severe bronchiectasis.
Young adults with cystic fibrosis have lower blood pressures than control subjects of similar age and sex. The low blood pressure may be related to the excessive loss of salt in the sweat of these patients. A beneficial effect of the cystic fibrosis gene may be protection against developing hypertension in both the homozygous and heterozygous states, especially if the heterozygote has borderline elevation of sweat electrolytes.
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Alpha1-antitrypsin deficiency is a genetic model that predisposes to pulmonary emphysema or a form of hepatic cirrhosis in man. The antitrypsin protein protects the tissues from proteolytic digestion by lysosomal proteases from inflammatory cells. The three causes of antitrypsin deficiency demonstrated to date are: 1) A defect in synthesis and release of the Z variant from the liver. 2) Presence of an inactive (null) gene for antitrypsin production, and 3) Increased lability of certain variants associated with the in vivo degradation of antitrypsin.
Contamination of werum by certain gram-negative bacteria has been shown to spoil the serum for measurement of trypsin inhibitory capacity (STIC) or for antitrypsin phenotyping. Such sera develop intense fibrinolytic activity when the STIC has dropped to itsminimal level, but antitrypsin concentration as measured by radial immunodiffusion remainsconstant. Cultures of ENTEROBACTER, Klebsiella, Bacillus subtilis, and Pseudomonas species were shown to have this capability, but production of the fibrinolytic enzyme by the bacteria was most proficient in the presence of human serum. The enzyme is believed to be of bacterial origin because of its lack of esterase activity, and because activation of serum plasmin by streptokinase did not affect the STIC. Care mustbe taken to avoid bacterial contamination of blood that is to be submitted for an STICassay and/or antitrypsin phenotyping. Serum should be prepared quickly, frozen soon,and stored and transported in a frozen state.
Serum trypsin inhibitory capacity and alpha(1)-antitrypsin concentrations were compared in venous and arterial bloods obtained simultaneously from patients with chronic airways obstruction. No significant venoarterial difference was observed in most patients, which was contrary to the published findings of Woolcock et al. (1972).
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A material that strongly reacts with antibodies against alpha(1)-antitrypsin, but has little trypsin inhibitory capacity, has been isolated and purified to homogeneity from human liver. The molecular weight of the crossreacting material is about 18,000, which is significantly lower than that of serum alpha(1)-antitrypsin. The material isolated from the liver of a homozygous variant subject (ZZ) with alpha(1)-antitrypsin deficiency is readily distinguished by electrophoresis from the material extracted from a normal (MM) subject. The tissues from a heterozygous variant subject (MZ) contain the two components. The immunologically crossreacting material is presumably synthesized by the gene that codes for alpha(1)-antitrypsin.
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