Initial experience with computed tomographic colonography applied for noncolorectal cancerous conditions.

Purpose: The aim of this study was to asses retrospectively the performance of computed tomography colonography (CTC) for noncolorectal cancerous conditions.

Material And Methods: A total of 44 patients with non-colorectal cancerous conditions underwent CTC. We researched the indications for CTC or present illness and evaluated the CTC imaging findings.

Extracellular acidic environments induce phosphorylation of ZAP-70 in Jurkat T cells.

In solid tumor and inflammation loci, low pH conditions have been observed as a consequence of either a lack of sufficient vascularization or excess activity of tumor cells, and T cells have been reported to infiltrate tumors and inflammation sites. However, it remains unclear how extracellular acidic environments affect immune cell function. A previous report proposed that a different signal transduction cascade might occur under low pH conditions in Jurkat T cells (Fukamachi T, Saito H, Kakegawa T, Kobayashi H.

Identification of AUF1 as a rapamycin-responsive binding protein to the 5'-terminal oligopyrimidine element of mRNAs.

In vertebrates, mRNAs containing a 5'-terminal oligopyrimidine (TOP) motif are coordinately post-transcriptionally regulated. Binding of specific proteins to this element has been proposed to downregulate expression of TOP mRNAs at the level of translational initiation. We previously reported that rapamycin induces binding activity to the TOP element of ribosomal protein (r-protein) L32 mRNA.

Processing of XynE (110-kDa) of Aeromonas caviae ME-1 to 72-kDa xylanase in Escherichia coli transformant.

An extracellular 72-kDa xylanase from an Escherichia coli transformant that harbored pXED30 carrying xynE of Aeromonas caviae ME-1 was purified by extraction following SDS-PAGE to electrophoretic homogeneity. The analysis of N-terminal 10 amino acid residues (Gly-Ala-Arg-Ala-Gln-Ala-Ala-Ala-Asp-Val) revealed a 72-kDa product derived by the cleavage of Gly26-Gly27 at the N-terminal region of 110 kDa XynE. The 72-kDa xylanase from A.

The processing of high-molecular-weight xylanase (XynE, 110 kDa) from Aeromonas caviae ME-1 to 60-kDa xylanase (XynE60) in Escherichia coli and purification and characterization of XynE60.

A xylanase gene (xynE) encoding XynE (110 kDa) was cloned from a lambda phage genomic library of Aeromonas caviae ME-1 which is a multiple-xylanase-producing bacterium. Upon nucleotide sequence analysis, we found that xynE comprises 2823 by and encodes a protein of 941 amino acid residues (104,153 Da), which was similar to endo-beta-1,4-xylanases which are categorized to glycosyl hydrolase family 10. An Escherichia coli transformant that harbored pXED30 carrying xynE produced 110-, 84-, 72-, and 66-kDa xylanases in the cell-free extract, and 72- and 66-kDa xylanases in the culture supernatant.