Ketoacidosis occurs in both Type 1 and Type 2 diabetes--a population-based study from Northern Sweden.

AIMS: To determine the occurrence of diabetic ketoacidosis (DKA) in adult Type 2 and Type 1 diabetic patients in Northern Sweden and to determine whether DKA presents with a different clinical picture in Type 2 compared with Type 1 diabetic subjects. METHODS: All adult patients from a hospital catchment area in Northern Sweden with diagnosed DKA episodes during 1997-2000 were included in a retrospective study. Medical records and laboratory reports were analysed. RESULTS: During the years 1997 to 2000, the average annual incidence rate for DKA was 5.9 per 100 000 adult inhabitants. Twenty-five patients developed DKA, eight (32%) had Type 2 diabetes, while 17 (68%) had Type 1 diabetes. Type 2 diabetic patients with DKA were older and had higher levels of C-peptide than Type 1 diabetic patients. On admission because of DKA, a similar degree of hyperglycaemia was present in Type 1 and Type 2 patients. Metabolic acidosis was more severe in Type 1 compared with Type 2 diabetic patients. In 50% of the Type 2 diabetic patients, diabetes was diagnosed at the episode of DKA. CONCLUSIONS: DKA occurs in Caucasian Type 2 diabetic patients within a Swedish population. Although the frequency of DKA is much higher in Type 1 diabetic patients, Type 2 diabetes may account for as much as one-third of the overall DKA cases.

X-ray diffraction studies of the structural organisation of prolamellar bodies isolated from Zea mays.

Transmission electron microscopy (TEM) indicates that maize prolamellar bodies (PLBs) are built up of tetrapodal units based on a highly convoluted but continuous lipid bilayer exhibiting diamond cubic (Fd3m) symmetry. Such lattices are often described in terms of infinite periodic minimal surfaces (IMPS) exhibiting zero net curvature and dividing the system into two identical subvolumes. If so, X-ray diffraction measurements would be expected to index on a double-diamond (Pn3m) lattice with a unit cell length half that of the TEM lattice. Our measurements index on a Fd3m lattice with a similar repeat distance to the TEM images. The PLB membrane is thus inherently asymmetric, probably as the result of the distribution of membrane protein.

Secondary structure of NADPH: protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods.

To study the secondary structure of the enzyme NADPH: protochlorophyllide oxidoreductase (PCOR), a novel method of enzyme isolation was developed. The detergent isotridecyl poly-(ethylene glycol) ether (Genapol X-080) selectively solubilizes the enzyme from a prolamellar-body fraction isolated from wheat (Triticum aestivum L.). The solubilized fraction was further purified by ion-exchange chromatography. The isolated enzyme was studied by fluorescence spectroscopy at 77 K, and by CD spectroscopy. The fluorescence-emission spectra revealed that the binding properties of the substrate and co-substrate were preserved and that photo-reduction occurred. The CD spectra of PCOR were analysed for the relative amounts of the secondary structures, alpha-helix, beta-sheet, turn and random coil. The secondary structure composition was estimated to be 33% alpha-helix, 19% beta-sheet, 20% turn and 28% random coil. These values are in agreement with those predicted by the Predict Heidelberg Deutschland and self-optimized prediction method from alignments methods. The enzyme has some amino acid identity with other NADPH-binding enzymes containing the Rossmann fold. The Rossmann-fold fingerprint motif is localized in the N-terminal region and at the expected positions in the predicted secondary structure. It is suggested that PCOR is anchored to the interfacial region of the membrane by either a beta-sheet or an alpha-helical region containing tryptophan residues. A hydrophobic loop-region could also be involved in membrane anchoring.

The rapidly phosphorylated 25 kDa polypeptide of the light- harvesting complex of photosystem II is encoded by the type 2 cab-II genes.

The main light-harvesting complex of Photosystem II (LHC II) in higher plants consists of two sub-populations. The 'inner' pool consists only of a 27 kDa polypeptide, whereas in the 'outer' pool both the 27 kDa and a 25 kDa polypeptide are found. We purified the 25 and the 27 kDa LHC II polypeptides from Scots pine and 25 kDa LHC II polypeptide from spinach. Protein sequencing after cleavage with endoproteinase Lys-C showed that the 25 kDa polypeptide is encoded by the Type 2 cab-II genes and the 27 kDa polypeptide by the Type I cab-II genes. A fatty acid was not covalently attached to the peptides assembled into the pigment-protein complex. Our results show that the different polypeptides seen on a gel are different gene products, and not the result of different processing.

Anaerobic phagocytosis, killing, and degradation of Streptococcus pneumoniae by human peripheral blood leukocytes.

Encapsulated Streptococcus pneumoniae of serotypes 2, 9N, 14, 21, and 23F and an unencapsulated variant of type 2 pneumococci were efficiently phagocytosed by both aerobically and anaerobically incubated human leukocytes. In the presence of O2, the pneumococci rapidly lost their viability, whereas during anaerobiosis, killing was considerably delayed. Type 14 pneumococci radiolabeled with [14C]choline or [14C]ethanolamine for cell wall teichoic acid, [14C]uracil for nucleic acids, or [14C]arachidonic acid for unsaturated cytoplasmic membrane lipids were used in studies of the fate of bacterial macromolecules after phagocytosis. The degradation of teichoic acid, RNA, and DNA during anaerobiosis approached that recorded in air at 60 min of incubation (45 to 70% and 55 to 75%, respectively). In contrast, the marked loss of [14C]arachidonic acid from pneumococcal membrane lipids observed in aerobic leukocytes did not occur during anaerobic incubation. Hence, lipid peroxidation could be involved in the rapid aerobic leukocyte killing of pneumococci, whereas a different leukocyte function of as yet unknown nature appears to be responsible for the killing seen in anaerobiosis. Autolysis-resistant type 14 pneumococci were obtained by substituting ethanolamine for choline in a defined culture medium. Differences between such bacteria and normal (autolytic) pneumococci in their killing and degradation by leukocytes were not detected in either the presence or the absence of O2. The aerobic and anaerobic handling of phagocytosed pneumococci by human blood leukocytes thus proceeded independently of the bacterial autolytic system.

A Comparison between Prolamellar Bodies and Prothylakoid Membranes of Etioplasts of Dark-Grown Wheat Concerning Lipid and Polypeptide Composition.

The aim of the present investigation was to find factors critical for the co-existence of prolamellar bodies and prothylakoids in etioplasts of wheat (Triticum aestivum L. cv Starke II). The lipid composition of the prolamellar body and prothylakoid fractions was qualitatively similar. However, the molar ratio of monogalactosyl diacylglycerol to digalactosyl diacylglycerol was higher in the prolamellar body fraction (1.6 +/- 0.1), as was the lipid content on a protein basis. Protochlorophyllide was present in both fractions. The dominating protein of the prolamellar body fraction was protochlorophyllide oxidoreductase. This protein was present also in prothylakoid fractions. The other major protein of the prothylakoid fraction was the coupling factor 1, subunit of the chloroplast ATPase. From the lipid and protein data, we conclude that prolamellar bodies are formed when monogalactosyl diacylglycerol is present in larger amounts than can be stabilized into planar bilayer prothylakoid membranes by lamellar lipids or proteins.

Localization of Galactolipid Biosynthesis in Etioplasts Isolated from Dark-Grown Wheat (Triticum aestivum L.).

Etioplasts were isolated from leaves of dark-grown wheat (Triticum aestivum L. var Starke II). Galactolipid biosynthesis was assayed in an envelope-rich fraction and in the fraction containing the rest of the etioplast membranes by measuring incorporation of (14)C from uridine-diphospho[(14)C]galactose into monogalactosyl diacylglycerol and digalactosyl diacylglycerol. More than half of the galactolipid biosynthetic capability was found in the fraction of inner etioplast membranes. This fraction was subfractioned into fractions enriched in prolamellar bodies and membrane vesicles (prothylakoids), respectively. All membrane fractions obtained from etioplasts were able to carry out galactolipid biosynthesis, although the activity was very low in prolamellar body-enriched fractions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed markedly different polypeptide patterns between the different fractions. It is concluded that the capability of galactolipid biosynthesis of etioplasts probably is not restricted to the envelope, but is also present in the inner membranes of this plastid.