Adverse events associated with neonatal exchange transfusion for hyperbilirubinemia.

To estimate the incidence of blood exchange and determine causes and complication of blood exchange and identify strategies for risk reduction of Kernicterus in newborn with jaundice. From March 2004 to March 2006 in neonatal Department in children hospital, medical center Tehran, Iran, 346 neonates were admitted as neonatal jaundice without sign and symptoms of infections. We identified causes and complications of exchange. Of 346 infants with jaundice who received phototherapy. 50, 14.45 percent cases underwent exchange transfusion with mean age 9.38 + 5.75 days. The mean total Serum bilirubin level was 29.39 + 6.13 mg/dl. ABO incompatibility was the most common cause for hyperbilirubinemia. The incidence of apnea was 12% there was no direct death from exchange transfusion. To make payment women aware to observe jaundice regularly after birth of their child and short breast feeding to control dehydration.

Massive intraperitoneal hemorrhage from traumatic intrasplenic pseudoaneurysms: treatment using superselective embolotherapy.

The importance of splenic preservation in the setting of penetrating and blunt trauma has led to the development of more sophisticated and noninvasive methods for controlling splenic hemorrhage. Although controversy exists, transcatheter embolotherapy has challenged the use of splenectomy in patients suffering from persistent bleeding after splenic trauma. We describe a case of a 41-year-old man with hepatitis C, ethanol-induced liver disease, and portal hypertension who presented with splenic rupture secondary to blunt trauma. Continued intra-abdominal hemorrhage was successfully controlled by superselective embolotherapy using microcoils and gelatin sponge pledgets.

The inaccuracy of duplex ultrasonography in predicting patency of transjugular intrahepatic portosystemic shunts.

BACKGROUND & AIMS: A prospective double-blinded study with preset sonographic criteria has not been performed to assess the accuracy of duplex ultrasonography in determining the patency of transjugular intrahepatic portosystemic shunts (TIPS). The purpose of this study was to determine the sensitivity and specificity of duplex ultrasonography in predicting shunt malfunction using accepted preset sonographic criteria. METHODS: Sixty ultrasonographic and venographic follow-up comparisons were made on 38 cirrhotic patients who had undergone TIPS placement for variceal bleeding (n = 28) or intractable ascites (n = 10). Ultrasonographic results were analyzed by one of two board-certified ultrasonographers without knowledge of venographic findings. RESULTS: Of the 31 occluded (n = 8) and stenotic (n = 23) shunts, ultrasonography accurately predicted a shunt malfunction (occlusion or stenosis) in only 11 studies and incorrectly predicted patency in 20. Compared with venography, ultrasonography had a sensitivity of 35% and a specificity of 83% in predicting TIPS stenosis or occlusion. CONCLUSIONS: These results suggest that duplex sonography is not a sensitive test in predicting the presence of a hemodynamically significant stenosis and that shunt status should be assessed by venography and direct portal pressure measurements until a more reliable and proven noninvasive ultrasonographic criterion is devised.

Pulmonary artery pseudoaneurysm after tube thoracostomy.

Pulmonary artery pseudoaneurysm has been described as a complication of Swan-Ganz catheterization and right heart catheterization. Isolated cases of this condition occurring in blunt and penetrating chest trauma have been reported. In this communication, we describe the case of a patient with intracranial hemorrhage who required positive-pressure ventilation and in whom subsequent pneumothorax developed, necessitating tube thoracostomy. A persistent opacification of the lung field resulted in evaluation with computed chest tomography and color-flow Doppler ultrasonography. A pseudoaneurysm of the lingular segmental artery was identified and successfully obliterated by Gelfoam coil embolization.

The leu-1 gene of Neurospora crassa: nucleotide and deduced amino acid sequence comparisons.

The Neurospora crassa leu-1 gene encodes beta-isopropylmalate dehydrogenase (IPMDH; EC 1.1.1.85), an enzyme in the leucine biosynthetic pathway. We determined the nucleotide sequence of the entire leu-1 gene and of four independent cDNA clones. By comparing the genomic and cDNA sequences, four introns were identified in the 5' portion of the gene and a single open reading frame was established. One of the introns is located within the 5'-noncoding region of the transcript. The deduced amino acid sequence encoded by leu-1 was aligned with that of the homologous yeast enzyme and extensive sequence identity was uncovered. The lesion present in a conventional leu-1 mutant was identified as the insertion of a single base pair.

Protein synthesis in rabbit reticulocytes. Purification and characterization of a double-stranded RNA-dependent protein synthesis inhibitor from reticulocyte lysates.

Reticulocyte lysates contain a latent form of eukaryotic peptide chain initiation factor 2 (eIF-2) kinase (dsI) which becomes activated in the presence of double-stranded RNA and ATP and inhibits protein synthesis. The latent form of dsI has been partially purified from reticulocyte ribosomal salt wash. The purified dsI has been activated by incubation in the presence of poly(rI).poly(rC) and [gamma 32P]ATP and the activated dsI has been further purified to near homogeneity. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, purified [32P]dsI shows an intensely staining 67,000-dalton polypeptide band which corresponds to a single 67,000-dalton radioactive band. During Sephadex (G-200) gel filtration, both the latent form of dsI and the activated dsI elute similarly with a peak corresponding to a molecular weight of 67,000. Purified dsI phosphorylates the 38,000-dalton subunit of eIF-2 and, under conditions of eIF-2 phosphorylation, dsI strongly inhibits AUG-dependent Met-tRNAf binding to 40 S ribosomes. Also, in partial reactions, eIF-2 alpha (P) formed by phosphorylation of eIF-2 using dsI and ATP, is not recognized by two eIF-2 ancillary factors, Co-eIF-2B and Co-eIF-2C. These results are similar to those reported previously for the heme-regulated eIF-2 kinase (Das, A., Ralston, R. O., Grace, M., Roy, R., Ghosh-Dastidar, P., Das H. K., Yaghmai, B., Palmieri, S., and Gupta, N. K. (1979) Proc. Natl. Acad. Sci. U. S. A. 76,5076-5079) and suggest that dsI, like the heme-regulated eIF-2 kinase phosphorylates eIF-2 and eIF-2 alpha (P) thus formed, in both cases, is not recognized by Co-eIF-2B and Co-eIF-2C, and is inactive in some step(s) of Met-tRNAf.40 S initiation complex formation.

Protein synthesis in rabbit reticulocytes. Co-eIF-2A reverses mRNA inhibition of ternary complex (Met-tRNAf.eIF-2.GTP) formation by eIF-2.

mRNAs, at low concentrations, drastically inhibit ternary complex formation by eIF-2 (Met-tRNAf.eIF-2.GTP) and, when added to the preformed ternary complex, cause extensive dissociation of the complex. Co-eIF-2A stimulates (2- to 4-fold) Met-tRNAf binding to eIF-2 and, in the presence of excess Co-eIF-2A, the stimulated Met-tRNAf binding to eIF-2 is fully resistant to mRNAs. Other cofactors tested such as Co-eIF-2B and Co-eIF-2C do not reverse mRNA inhibition of ternary complex formation.

Protein synthesis in rabbit reticulocytes. Preparation of homogeneous Met-tRNAf deacylase and studies of its role in protein synthesis.

Met-tRNAf deacylase from reticulocyte ribosomes has been purified to homogeneity. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the homogeneous preparation gives a single protein band corresponding to a molecular weight of approximately 67,000. Purified Met-tRNAf deacylase degrades free Met-tRNAf and also Met-tRNAf bound to 40 S ribosomes in the presence of AUG codon but does not degrade Met-tRNAf in the ternary complex, Met-tRNAf.eIF-2.GTP. Purified Met-tRNAf deacylase does not inhibit protein synthesis in reticulocyte lysates at any concentration tested indicating that Met-tRNAf deacylase is not a protein synthesis inhibitor. Antibodies against Met-tRNAf deacylase have been prepared by immunizing a chicken with homogeneous preparation of Met-tRNAf deacylase. Addition of anti-Met-tRNAf deacylase does not have any effect on protein synthesis in reticulocyte lysates indicating that Met-tRNAf deacylase is not required for protein synthesis.

Protein synthesis in rabbit reticulocytes. A study of the mechanism of interreaction of fluorescently labeled co-eIF-2A with eIF-2 using fluorescence polarization.

5-Dimethylaminonaphthalene-1-sulfonyl (dansyl)-Co-eIF-2A was prepared using homogeneous Co-eIF-2A. Dansyl-Co-eIF-2A was as active as untreated Co-eIF-2A when assayed for stimulation of ternary complex formation and also for protection of the ternary complex from dissociation by aurintricarboxylic acid. The mechanism of interaction of dansyl-Co-eIF-2A with eIF-2 was studied by measuring changes in fluorescence polarization. These studies indicate that dansyl-Co-eIF-2A interacts specifically with the ternary complex and does not interact with free eIF-2 or with two other high molecular weight protein complexes, Co-eIF-2B and Co-eIF-2C. Mg2+ inhibits ternary complex formation by eIF-2 and Co-eIF-2C relieves this Mg2+ inhibition of ternary complex formation. In both cases, the changes in fluorescence polarization of dansyl-Co-eIF-2A correlate well with the extent of ternary complex formed.

Protein synthesis in rabbit reticulocytes. Demonstration of the requirements for eIF-2 and Co-eIF-2A for peptide chain initiation using immune sera.

Antisera to eIF-2 and Co-eIF-2A have been prepared by immunizing two chickens separately with homogeneous preparations of either eIF-2 or Co-eIF-2A. Addition of anti-eIF-2 or anti-Co-eIF-2A to reticulocyte lysates strongly inhibits protein synthesis and, in each case, protein synthesis inhibition is reversed by the addition of the corresponding homogeneous factor. Protein synthesis inhibition by anti-Co-eIF-2A is not reversed by eIF-2 at any concentration tested indicating an absolute requirement for Co-eIF-2A in protein synthesis. Also, in partial peptide chain initiation reactions, the addition of anti-Co-eIF-2A inhibits Co-eIF-2A stimulation of ternary complex formation by eIF-2 and Co-eIF-2A protection of ternary complexes in the presence of aurintricarboxylic acid.

Protein synthesis in rabbit reticulocytes: mechanism of protein synthesis inhibition by heme-regulated inhibitor.

Partially purified Met-tRNAf binding factor, eIF-2, was phosphorylated by using heme-regulated inhibitor (HRI). Phosphorylated eIF-2 was freed from HRI by phosphocellulose column chromatography. Analysis by isoelectric focusing showed 100% phosphorylation of the 38,000-dalton subunit of eIF-2. Both eIF-2 and eIF-2(P) formed ternary complexes with Met-tRNAf and GTP with almost the same efficiency, and in both cases the ternary complex formation was drastically inhibited by prior addition of Mg2+. However, whereas the ternary complexes formed with eIF-2 could be stimulated by Co-eIF-2C at 1 mM Mg2+ and dissociated by Co-eIF-2B at 5 mM Mg2+, the ternary complexes formed with eIF-2(P) were unresponsive to both Co-eIF-2B and Co-e-IF-2C. Also, under conditions of eIF-2 phosphorylation, HRI drastically inhibited AUG-dependent Met-tRNAf binding to 40S ribosomes. However, HRI (in the presence of ATP) had no effect on the joining of preformed Met-tRNAf . 40S . AUG complex to the 60S ribosomal subunit to form Met-tRNAf-80S . AUG complex. These studies suggest that HRI inhibits protein synthesis initiation by phosphorylation of the 38,000-dalton subunit of eIF-2. HRI-phosphorylated eIF-2 does not interact with at least two other protein factors, Co-eIF-2B and Co-eIF-2C, and is thus inactive in protein synthesis initiation.