[Low molecular heparin for treatment of venous thrombosis in two very low-birth-weight pre-term infants with genetic risk factors]. / Niedermolekulares Heparin bei Frühgeborenen mit hereditären Risikofaktoren und venösen Thrombosen.

We describe the use of low molecular weight heparin to treat venous thrombosis in two very low-birth-weight pre-term infants (GA: 30 and 27 weeks) both with genetic and acquired prothrombotic risk factors. Initially both infants were treated with unfractionated heparin. Since in one infant no effect on the thrombus size was observed and in the other infant there was an increase in size, the anticoagulation therapy was switched to subcutaneously injected low molecular heparin (Enoxaparin). During enoxaparin therapy the anti-Xa-level was carefully monitored and dosages were adjusted accordingly. Partial resolution of the thrombosis was achieved in both infants during enoxaparin therapy. No clot extension or recurrence of thrombosis occurred. An accidental overdose of Enoxaparin (100 times the required dosage) was administered to one infant without any consequences. Our data suggest that the use of low molecular weight heparin (Enoxaparin) for treatment of venous thrombosis in our two preterm infants was practical, safe and effective.

Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.

In this study we provide, for the first time, experimental evidence that a protein homologous to bacterial Ffh is part of an SRP-like ribonucleoprotein complex in hyperthermophilic archaea. The gene encoding the Ffh homologue in the hyperthermophilic archaeote Acidianus ambivalens has been cloned and sequenced. Recombinant Ffh protein was expressed in E. coli and subjected to biochemical and functional studies. A. ambivalens Ffh encodes a 50.4-kDa protein that is structured by three distinct regions: the N-terminal hydrophilic N-region (N), the GTP/GDP-binding domain (G) and a C-terminal located C-domain (C). The A. ambivalens Ffh sequence shares 44-46% sequence similarity with Ffh of methanogenic archaea, 34-36% similarity with eukaryal SRP54 and 30-34% similarity with bacterial Ffh. A polyclonal antiserum raised against the first two domains of A. ambivalens Ffh reacts specifically with a single protein (apparent molecular mass: 46 kDa, termed p46) present in cytosolic and in plasmamembrane cell fractions of A. ambivalens. Recombinant Ffh has a melting point of tm = 89 degreesC. Its intrinsic GTPase activity obviously depends on neutral pH and low ionic strength with a preference for chloride and acetate salts. Highest rates of GTP hydrolysis have been achieved at 81 degreesC in presence of 0.1-1 mm Mg2+. GTP hydrolysis is significantly inhibited by high glycerol concentrations, and the GTP hydrolysis rate also markedly decreases by addition of detergents. The Km for GTP is 13.7 microm at 70 degreesC and GTP hydrolysis is strongly inhibited by GDP (Ki = 8 microm). A. ambivalens Ffh, which includes an RNA-binding motif in the C-terminal domain, is shown to bind specifically to 7S RNA of the related crenarchaeote Sulfolobus solfataricus. Comparative sequence analysis reveals the presence of typical signal sequences in plasma membrane as well as extracellular proteins of hyperthermophilic crenarchaea which strongly supposes recognition events by an Ffh containing SRP-like particle in these organisms.

Measuring the human pelvis: a comparison of direct and radiographic techniques using a modern United States--based sample.

Seven measurements were taken on a sample of 50 human cadaveric pelves, all white Texans born in the 20th century. Two separate methodologies were used to obtain these data: radiographs and direct measurements. These two methodologies were compared and contrasted, with the relative advantages and disadvantages of each explored. Results indicate that significant differences exist between the two methodologies. Pelvic height, breadth of symphysis, sacro-iliac breadth (P = 0.0001) and anterior upper spinal breadth (P = 0.0002) were larger when measured directly. Pelvic breadth, transverse diameter of the pelvic brim, and height of the ilium did not significantly differ between methodologies (P = 0.2037, P = 0.5253, P = 0.1752). Due to secular changes and inherent intrapopulational variation, taking measurements either directly from modern cadaveric specimens or radiographically on living volunteers in a limited geographic or socioeconomic grouping, rather than from skeletal collections or archived radiographs, may be more appropriate for providing data for current anthropometric applications.

The signal recognition particle receptor alpha subunit of the hyperthermophilic archaeon Acidianus ambivalens exhibits an intrinsic GTP-hydrolyzing activity.

Two adjacent genes of the acidophilic and hyperthermophilic crenarchaeon Acidianus ambivalens were cloned and sequenced. The 1.6 kb genomic nucleotide sequence under investigation consists of the 1.12 kb SRa gene encoding the putative signal recognition particle receptor alpha subunit (SR alpha, 42.2 kDa) and the 186 basepair secE gene coding for the putative secretory component secE subunit (6800 Da). The SR alpha protein is structured by three distinct regions: the N-terminal hydrophilic H-region, the following X-region and the C-terminal GTP-binding domain. A polyclonal anti-E. coli lacZ/A. ambivalens SR alpha antiserum detects a 51 kDa cell protein (p51) on immunoblots. Proteolysis of the recombinant SR alpha protein by Proteinase K produces a 31.6 kDa protease-resistant protein fragment comprising X-region and G-domain. The protein binds tightly to the GTP-agarose affinity matrix in a temperature-dependent manner. It hydrolyzes GTP readily at higher temperatures only in the presence of Mg2+. Point mutations (T326N) and (D329A) in the G-4 element of A. ambivalens SR alpha G-domain diminish the GTPase activity significantly. In contrast, the deletion mutant protein SR alpha (delta1-92) lacking the hydrophilic H-region displays a higher GTP-hydrolyzing activity when compared to the unmodified recombinant protein. Addition of GDP greatly inhibits GTP hydrolysis in mutant and unmodified A. ambivalens SR alpha.

A putative signal recognition particle receptor alpha subunit (SR alpha) homologue is expressed in the hyperthermophilic crenarchaeon Sulfolobus acidocaldarius.

A 1.64 kb genomic DNA sequence from the hyperthermophilic crenarchaeon Sulfolobus acidocaldarius is composed of two adjacent genes. The first functionally unassigned open reading frame (orf-1) comprises 450 base pairs. The second 1.1 kb large open reading frame encodes the putative signal recognition particle receptor alpha subunit (SR alpha). Both genes are expressed under the heterotrophic growth conditions of the organism. The main transcript of orf-1 appears as a monocistronic RNA in Northern hybridization. With regard to SR alpha the transcription pattern was investigated by reverse transcription polymerase chain reaction and primer extension analysis. A polyclonal antiserum directed against E. coli lacZ'/Sulfolobus SR alpha fusion protein detects a 40.5 kDa protein (p41) in agreement with the 41.4 kDa as deduced from the nucleotide sequence.

Nucleotide sequence of a gene cluster encoding ribosomal proteins in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.

A 1.6 kb genomic DNA fragment derived from the extremely thermoacidophilic archaeon Sulfolobus acidocaldarius (DSM 639) comprises four open reading frames. The sequence contains three genes encoding crenarchaeal ribosomal proteins with apparent molecular masses of 6.3 kDa, 15.2 kDa and 9.9 kDa, which all represent strongly basic properties. These were identified by sequence comparison as RL46, RL31 and RL33. One open reading frame encodes a new polypeptide (22.1 kDa, pI = 7.3) with no homology to known proteins. The latter is transcribed as a common mRNA with RL46 and RL31. This gene cluster immediately precedes another cluster including genes encoding the putative SRP receptor alpha subunit as well as the putative secEp.