There was no history of trauma or surgery On examination, he was

There was no history of trauma or surgery. On examination, he was unconscious with signs of meningeal irritation and asymmetrical pupils. Computed tomography (CT) scan of brain revealed pneumocephalus. He died immediately after the CT scan. He was later found to be immunocompetent. Computed tomography scan (figures 1 and ​and2)2) showed moderate dilatation of lateral ventricles with intraventricular air pockets, small bilateral intracranial air pockets in the sulci. The CT features were suggestive of meningitis with ventriculitis. Figure 1 Computed tomography (CT) scan of the brain. Arrows show moderate dilatation of lateral ventricles with intraventricular air pockets Inhibitors,research,lifescience,medical as well as small bilateral

intracranial air pockets in the sulci. Figure 2 Computed tomography (CT) scan of the brain. Arrows show intraventricular air pockets and small intracranial air pockets in Inhibitors,research,lifescience,medical the sulci. Discussion Pneumocephalus is defined as the presence of air or gas within the cranial cavity. It is classified as extradural, subdural, subarachnoid, intracerebral and intraventricular. Pneumocephalus is usually caused by trauma or surgery.1 Spontaneous, non-traumatic pneumocephalus is an uncommon condition. In nontraumatic cases, meningitis is a rare cause of pneumocephalus and one should suspect anaerobic infection.2 It Inhibitors,research,lifescience,medical may also be due

to anaerobic, aerobic, or mixed infection. It is fatal in most of the cases.3
Tumor protein 52 (TP53) gene, which encodes transcription factor P53, maps Inhibitors,research,lifescience,medical to chromosome 17pl 3.1, spanning around 20 kilobase (kb) pairs, and comprises 11 exons.1 The P53 gene

is well-suited to mutational spectrum analysis for several reasons. Since P53 mutations are common in many human cancers,2 its modest size (11 exons, 393 amino acids) permits study of the entire coding region. It is Inhibitors,research,lifescience,medical highly conserved in vertebrates, allowing extrapolation of data from animal models.3 Structural Features The human P53 protein contains 393 amino acids, and has been divided structurally and functionally into four domains. The first 42 amino acids at the Rutecarpine N-terminus constitute a transcriptional activation domain that interacts with the basal transcriptional machinery in positively regulating gene expression. Amino acids 13–23 in the P53 protein are identical in a number of diverse species. The sequence-specific DNA-binding domain of P53 is localized between amino acid residues 102 and 292. This domain folds into a four-stranded and five-stranded antiparallel β sheet that in turn is a scaffold for two α-helical loops that interact directly with the DNA. Amino acid residues 324–355 are required for this selleck screening library oligomerization of the protein. The C-terminal 26 amino acids form an open protease sensitive domain composed of nine basic amino acid residues that bind to DNA and RNA readily with some sequence or structural preferences.4,5 Two promoters have been identified in the P53 gene.

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