• BMB Reports
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• v.30 no.4
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• pp.299-301
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• 1997

The asialoglycoprotein receptor (ASGPR) was the first described mammalian lectin that mediates the specific binding and internalization of galactose/N-acetylgalactosamine-terminating glycoproteins by hepatic parenchymal cells. H1 and H2 are known as essential subunits of the functional ASGPR. There were close similarities in ASGPR H2 subunits between cultured cell line HepG2 and normal human liver cells including identical sequences at both termini. It was therefore expected that there may be some similarities between the subunits from normal liver cells and fetal liver cells. The two subunits of human fetal liver ASGPR. designated FL-H1 and FL-H2. were cloned from cDNA library by peR and the sequences were compared with the known HI and H2 sequences of HepG2, and the H1 sequence of nornal human liver cells. The results showed that FL-H1 was identical to H1 of HepG2. Whereas FL-H2 contains a 15-bp miniexon, but missing 57-bp at the near upstream from the membrane-spanning domain compared to H2 of HepG2 and normal human liver cells indicating that FL-H2 resulted from a differential splicing compared to HepG2 and normal liver cells.

• Animal cells and systems
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• v.12 no.4
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• pp.211-217
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• 2008

Bax, a pro-apoptotic member of Bcl-2 family proteins, plays a central role in the mitochondria-dependent apoptosis. Apoptotic signals induce the translocation of Bax from cytosol into the mitochondria, which triggers the release of apoptogenic molecules such as cytochrome C and apoptosis-inducing factor, AIF. Bax-inhibiting peptide(BIP) is a cell permeable peptide comprised of five amino acids designed from the Bax-interaction domain of Ku70. Because BIP inhibits Bax translocation and Bax-mediated release of cytochrome C, BIP suppresses Bax-dependent apoptosis. In this study, we observed that BIP inhibited staurosporine-induced neuronal death in cultured cerebral cortex and cerebellar granule cells, but BIP failed to rescue granule cells from trophic signal deprivation-induced neuronal death, although both staurosporine-induced and trophic signal deprivation-induced neuronal death are dependent on Bax. These findings suggest that the mechanisms of the Bax activation may differ depending on the type of cell death induction, and thus BIP exhibits selective suppression of a subtype of Bax-dependent neuronal death.

• Asian Pacific Journal of Cancer Prevention
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• v.13 no.7
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• pp.3385-3388
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• 2012

Objective: The study was conducted to assess biochemical profiles in premenopausal and postmenopausal women having breast cancer. Materials and Methods: A hospital based case control study was carried out at Manipal Teaching Hospital (MTH), Pokhara, Nepal. The analysed variables were age, metabolic profile including total cholesterol, triglycerides, HDL-C, LDL-C, blood sugar, insulin concentration, C-peptide, HbA1c and selenium. Descriptive statistics and testing of hypothesis were used for the analysis using EPI INFO and SPSS 16 software. Results: In premenopausal women, significant differences were noted for total cholesterol (P value <0.001), triglycerides (P value 0.002), HbA1c level (P value <0.001), insulin concentration (P value 0.030), C-peptide concentration (P value 0.001), and selenium (P value <0.001) between cases and controls. Insignificant results were found for HDL-C (P value 0.749), LDL-C (P value 0.933), blood sugar (P value 0.59) and BMI (P value 0.746). Similarly, significant difference in total cholesterol (P value <0.001), triglycerides (P value 0.001), LDL-C (P value <0.001), HDL-C (P value 0.025), blood sugar (P value <0.001), insulin concentration (P value <0.001), c-peptide concentration (P value <0.001), HbA1c level (P value <0.001) and selenium (P value <0.001) were observed for postmenopausal patients and controls. Conclusions: Assessing metabolic changes and their management may be important for control of breast cancer and increased survival.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.75-75
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• 2003

We have purified and characterized cecropin A-like antibacterial peptide from the hemolymph of immunized Galleria mellonella larvae. Acid extraction, gel filtration, preparative acid urea PAGE, and reversed-phase HPLC were used for purification of peptide. The molecular mass of the purified peptide was estimated to be 4160.68 Da by MALDI-TOF mass spectrometry. (omitted)

• Molecules and Cells
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• v.19 no.1
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• pp.54-59
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• 2005

Deoxyribonuclease I (DNase I) is a divalent cation dependent endonuclease and thought to be a significant barrier to effective gene delivery. The only known DNase I-specific inhibitor is monomeric actin which acts by forming a 1:1 complex with DNase I. Its use, however, is restricted because of tendency to polymerize under certain conditions. We screened two random phage peptide libraries of complexity $10^8$ and $10^9$ for DNase I binders as candidates for DNase I inhibitors. A number of DNase I-binding peptide sequences were identified. When these peptides were expressed as fusion proteins with Escherichia coli maltose binding protein, they inhibited the actin-DNase I interaction ($IC_{50}=0.1-0.7{\mu}M$) and DNA degradation by DNase I ($IC_{50}=0.8-8{\mu}M$). Plasmid protection activity in the presence of DNase I was also observed with the fusion proteins. These peptides have the potential to be a useful adjuvant for gene therapy using naked DNA.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.76-76
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• 2003

Here we report an antifungal peptide isolation from G. mellonella larvae. The peptide shows a high degree of sequence homology to an insect defensin, named heliomicin, first reported in Lepidoptera. The peptide was purified by a three-step procedure consisting of acid extraction, gel permeation chromatography and reversed-phase HPLC. First the N-terminal amino acid sequence of the purified peptide was determined by automated Edman degradation. (omitted)

• Preventive Nutrition and Food Science
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• v.8 no.1
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• pp.66-69
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• 2003

An angiotensin converting enzyme (ACE) inhibitory peptide was isolated and purified from the hydrolysates of duck meat protein. Duck meat protein was hydrolyzed using trypsin at 37$^{\circ}C$ for 2 hrs. An ACE inhibitory peptide was purified using membrane filtration, anion exchange chromatography, gel permeation chromatography, fast protein liquid chromatography, normal phase HPLC. The purified inhibitory peptide was identified to be a tetrapeptide, Glu-Asp-Leu-Glu having $IC_{50}$/ value of 85.9 $\mu$M.

• The Monthly Diabetes
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• s.189
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• pp.46-48
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• 2005

• The Monthly Diabetes
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• s.210
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• pp.34-36
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• 2007

• Bulletin of the Korean Chemical Society
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• v.32 no.4
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• pp.1183-1186
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• 2011

The unique Br signature was utilized for C-terminal amino acid sequencing of model peptides. C-terminal carboxyl group was selectively derivatized in peptides, containing side chain carboxyl group, using 1-ethyl-3-[3-dimethylaminopropyl]carbodiimide hydrochloride (EDC) and Br was introduced using 4-bromophenylhydrazine hydrochloride (BPH) in a one pot reaction. Matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) tandem mass spectra were obtained carrying the Br signature in the y-series ions. The Br signature facilitated C-terminal sequencing and discrimination of C-terminal carboxyl groups in the free acid and amide forms.