Effect of labour and delivery on plasma hepatic enzymes in the newborn.

OBJECTIVE: To study the relationship between cord blood hepatic enzymes and obstetric and neonatal outcome in a Chinese population. MATERIALS AND METHODS: The study group consisted of 288 low-risk Chinese women with singleton term pregnancies. The following enzymes were assayed in cord blood: lactate dehydrogenase (LDH), glutamyl transferase (GGT), aspartate aminotransferase (AST) and alanine transferase (ALT). These were correlated to maternal and neonatal characteristics. RESULTS: A strong correlation was noted between cord blood AST and LDH (R = 0.582, p < 0.01), which was absent amongst those infants delivered by elective cesarean section. LDH, AST and ALT were negatively correlated with cord arterial pH and base excess (BE). GGT was inversely related only to gestational age (R = -0.18, p < 0.01). Both LDH and AST were weakly correlated with the duration of the first and second stages of labour. LDH was most closely linked to arterial pH, whereas AST was related to both arterial BE and duration of the second stage. CONCLUSIONS: The reference values are comparable to those published for Caucasian populations. There are moderate elevations in LDH and AST associated with the onset of labour and changes in acid-base status.

Purification and characterization of apolipoprotein C-II from human plasma by high-pressure liquid chromatography.

Apolipoprotein C-II, which activates lipoprotein lipase, was isolated from normal subjects and purified to homogeneity by reverse-phase high-pressure liquid chromatography (HPLC). The partially purified product from DEAE-cellulose chromatography was eluted from a Radial Pak C18 cartridge in a radial compression module using a linear gradient of 0.01 M ammonium bicarbonate and acetonitrile. The final product was homogeneous by polyacrylamide gel electrophoresis (pH 8.9), isoelectric focusing (pH 2.5-6.5), Ouchterlony double immunodiffusion, analytical HPLC and amino acid analysis. The purification of apolipoprotein C-II from normal subjects will permit the elucidation of its amino acid sequence and subsequent comparison with the known sequence of apolipoprotein C-II isolated from patients with hyperlipoproteinemia.

Tangier disease. High density lipoprotein deficiency due to defective metabolism of an abnormal apolipoprotein A-i (ApoA-ITangier).

Tangier disease is a rare familial disorder characterized by enlarged orange tonsils, transient peripheral neuropathy, hepatosplenomegaly, and lymphadenopathy, as well as striking reductions in plasma high density lipoproteins (HDL) and their major protein constituents, apolipoproteins (apo)A-I and A-II. In order to test the hypothesis that Tangier patients have abnormal apoA-I or apoA-II, the in vitro lipoprotein binding and in vivo metabolic characteristics of these proteins isolated from normal and Tangier plasma, were studied in normal subjects and patients with Tangier disease. After incubation with normal plasma, significantly greater percentages of radiolabeled Tangier apoA-I were associated with the 1.063-g/ml supernate (6%) and the 1.21 g/ml infranate (19%), and a lower percentage with HDL (75%), than those observed for normal apoA-I (2, 8, and 90%, respectively). In contrast, the lipoprotein binding properties of normal and Tangier apoA-II were very similar. Following the injection of radiolabeled normal and Tangier apoA-I into normal subjects (n = 4), the mean residence times of the specific activity for apoA-I(Tangier) were significantly lower, both in plasma (1.29 d) and in HDL (1.34 d), than those observed for normal apoA-I (3.80 and 4.06 d). In Tangier homozygotes the decay rates of these tracers were very rapid and were similar. No significant differences between the kinetics of normal and Tangier apoA-II were observed in normal subjects (n = 2). Tangier homozygotes (n = 3) had mean plasma HDL cholesterol, apoA-I, and apoA-II concentrations that were 4, 2, and 11% of normal (n = 24), respectively, whereas for heterozygotes (n = 3) these values were 46, 62, and 68% of normal. In homozygotes, in contrast to normals or heterozygotes, a significant fraction of both apoA-I and apoA-II were found in the 1.063-g/ml supernate instead of in HDL. Homozygotes had apoA-I(Tangier) synthesis rates and residence times that were 41 and 5% of values observed for normal apoA-I in normal subjects, and for apoA-II in homozygotes, these parameters were 63 and 18% of normal. Heterozygotes had apoA-I synthesis rates and residence times that were 92 and 66% of normal, and for apoA-II these values were 101 and 64% of normal. These data are consistent with the concept that apoA-I(Tangier) is functionally and metabolically distinct from normal apoA-I, and is the cause of the striking hypercatabolism of apoA-I and apoA-II, and the lipoprotein abnormalities observed in Tangier disease.

Tangier disease: a structural defect in apolipoprotein A-I (apoA-I Tangier).

Tangier disease is a familial disorder characterized by orange tonsils, cholesterol ester deposition in reticuloendothelial cells, abnormal chylomicron remnants, and a marked reduction in high density lipoproteins. Plasma concentrations of the apolipoproteins apo-A-I and apoA-II in patients with Tangier disease are approximately 1% and 7% of those in normal subjects, respectively. Previous studies have shown that the low plasma concentrations of apoA-I and apoA-II are due to increased fractional catabolism with a relatively normal apoA-I and apoA-II synthesis. Plasma apoA-I and apoA-II were isolated to electrophoretic homogeneity from delipidated plasma lipoproteins from a patient with Tangier disease. ApoA-I Tangier differed from apoA-I from control subjects in amino acid composition, electrophoretic mobility, apparent molecular weight on sodium dodecyl sulfate/polyacrylamide gel electrophoresis, and heterogeneity of isoforms on isoelectric focusing. ApoA-II Tangier, however, appeared to be identical to normal apoA-II in amino acid composition and in immunological as well as chemical properties. These results have been interpreted as indicating that apoA-I Tangier has a different covalent structure than does normal apoA-I, and apoA-II Tangier is identical to normal apoA-II. This structural change in apoA-I Tangier is associated with rapid catabolism of apoA-I Tangier-and apoA-II Tangier-containing plasma lipoproteins, and it leads to the deficiency in high density lipoproteins, abnormal chylomicron remnants, and the intracellular accumulation of cholesterol ester characteristic of Tangier disease.