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- Huang, H, et al.
(författare)
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Flow cytometric analysis of BHRF1 expression prohibiting apoptosis induced by radiation
- 1999
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Ingår i: The Annals of otology, rhinology, and laryngology. - : SAGE Publications. - 0003-4894 .- 1943-572X. ; 108:5, s. 481-484
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Tidskriftsartikel (refereegranskat)abstract
- The Epstein-Barr virus gene BHRF1 has homology with proto-oncogene bcl-2, which can protect cells from apoptosis. In order to investigate the effect of BHRF1 expression on the anti-apoptotic ability of nasopharyngeal carcinoma (NPC) cells after irradiation, a high—BHRF1 expression vector was constructed and transfected into the NPC cell line CNE2. Then, the alteration of proliferation and apoptosis in the cells was tested by flow cytometry after cobalt 60 irradiation. The results showed that BHRF1 expression could increase G1 delay and decrease the cell percentage in S phase before irradiation, and reduce the apoptotic rate of CNE2 cells and increase the cell percentage in S phase after irradiation. The results suggest that BHRF1 expression is able to alter the cell cycle and protect CNE2 cells from apoptosis induced by radiation.
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- Liu, Wei, et al.
(författare)
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Biosynthesis and function of all-trans- and 9-cis retinoic acid in parathyroid cells
- 1996
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Ingår i: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 229:3, s. 922-929
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Tidskriftsartikel (refereegranskat)abstract
- We demonstrate that cultured human and bovine parathyroid cells incubated with all-trans-[11,12-3H]-retinol convert this tracer into all-trans- and 9-cis-retinoic acid. By using RT-PCR, cellular retinol-binding protein type I (CRBP I), cellular retinoic acid binding protein I and II (CRABP I and II), retinoic acid receptors (RARs) alpha, beta and gamma, and 9-cis-retinoic acid receptor (RXR) alpha transcripts were detected in human parathyroid cDNA. CRBP I and CRABP I expression was confirmed by immunohistochemistry. Both 9-cis- and all-trans-RA were found to suppress parathyroid hormone (PTH) secretion from dispersed human adenomatous parathyroid cells, which was augmented by combined treatment with 1mM RA and 100 nM 1,25 (OH)2D3. The present data establish parathyroid gland as a target for retinoids and as a site of synthesis of the hormonal forms of vitamin A (retinol), all-trans- and 9-cis-retinoic acid.
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- Ni, Jiun, et al.
(författare)
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Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins
- 1997
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Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 272:16, s. 10853-10858
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Tidskriftsartikel (refereegranskat)abstract
- A new member of the human cystatin superfamily, called cystatin E, has been found by expressed sequence tag (EST) sequencing in amniotic cell and fetal skin epithelial cell cDNA libraries. The sequence of a full-length amniotic cell cDNA clone contained an open reading frame encoding a putative 28-residue signal peptide and a mature protein of 121 amino acids, including four cysteine residues and motifs of importance for the inhibitory activity of Family 2 cystatins like cystatin C. Recombinant cystatin E was produced in a baculovirus expression system and isolated. An antiserum against the recombinant protein could be used for affinity purification of cystatin E from human urine, as confirmed by N-terminal sequencing. The mature recombinant protein processed by insect cells started at amino acid 4 (cystatin C numbering), and displayed reversible inhibition of papain and cathepsin B (Ki values of 0.39 and 32 nM, respectively), in competition with substrate. Cystatin E is thus a functional cysteine proteinase inhibitor despite relatively low amino acid sequence similarities with human cystatins (26-34% identity with sequences for the Family 2 cystatins C, D, S, SN, and SA; <30% with the Family 1 cystatins, A and B, and domains 2 and 3 of the Family 3 cystatin, kininogen). Unlike other human low Mr cystatins, cystatin E is a glycoprotein, carrying an N-linked carbohydrate chain at position 108. Northern blot analysis revealed that the cystatin E gene is expressed in most human tissues, with the highest mRNA amounts found in uterus and liver. A strikingly high incidence of cystatin E clones in cDNA libraries from fetal skin epithelium and amniotic membrane cells (>0.5% of clones sequenced) indicates a protective role of cystatin E during fetal development.
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