• Title/Summary/Keyword: C-peptide

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Glycemic control of type 2 diabetic patients after short-term zinc supplementation

  • Oh, Hyun-Mee;Yoon, Jin-Sook
    • Nutrition Research and Practice
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    • v.2 no.4
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    • pp.283-288
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    • 2008
  • This study was carried out to determine whether a short-tenn zinc supplementation contributes to beneficial changes in glycemic control among type 2 diabetic patients. Seventy-six diabetic subjects and 72 normal adults participated in this study. Subjects were divided into supplemented and control groups. Forty-four diabetic patients and 34 normal subjects were supplemented with 50 mg zinc daily as zinc gluconate for 4 weeks. Zinc status was assessed from fasting plasma levels and urinary excretion. The effects of zinc supplementation on fasting blood glucose, $HbA_{1c}$, insulin, and C-peptide were measured at the beginning of the study and after 4 weeks of supplementation. The changes in glycemic control indicators were compared between diabetic groups, classified by baseline $HbA_{1c}$ levels, and by diabetic duration. At baseline, the incidence of marginal zinc deficiency in the diabetic group, as determined by plasma zinc level, was approximately twice as high as in the normal adult group. The changes of $HbA_{1c}$ concentration, and fasting blood glucose following supplementation were not statistically significant in diabetic subjects. In normal subjects, a significant decrease of $HbA_{1c}$ occurred only in the zinc supplemented group. No significant changes were observed for serum insulin and C-peptide in diabetic as well as normal subjects. However, when the changes were compared by baseline $HbA_{1c}$ level, we found that diabetic subjects with $HbA_{1c}\;{\geq}\;7.5%$ showed significantly improved levels of $HbA_{1c}$ and fasting glucose after Zn supplementation. While such improvement in fasting blood glucose was significant among diabetics with shorter diabetic duration, significant levels of increase in serum insulin and C-peptide were observed in zinc supplemented subjects with longer diabetic duration. Fasting blood glucose was significantly decreased, whereas serum insulin and C-peptide were increased in diabetics with marginal zinc status. Therefore, we suggest that Zn supplementation for a short-term period may improve glycemic control in diabetic patients with higher $HbA_{1c}$ levels and marginal zinc status.

Antibacterial Activity of Peptides Synthesized Based on the Bombus ignitus abaecin, A Novel Proline-Rich Antimicrobial Peptide

  • Kim, Seong-Ryul;Lee, Eun-Mi;Yoon, Hyung-Joo;Choi, Yong-Soo;Yun, Eun-Young;Hwang, Jae-Sam;Jin, Byung-Rae;Lee, In-Hee;Kim, Ik-Soo
    • International Journal of Industrial Entomology and Biomaterials
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    • v.14 no.2
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    • pp.147-150
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    • 2007
  • Abaecin is a largest member of the proline-rich anti-microbial peptide family found only in the hymenopterans. A cDNA of abaecin was previously isolated and cloned from Bombus ignitus: the mature peptide of Bombus ignitus abaecin was composed of 39 amino acid residues. In the present study, we determined the antibacterial effect of B. ignitus abaecin synthesized at several lengths against several bacteria by radial diffusion assay. The 37-mer peptide (Ab37) inhibited the growth of Gram-negative bacteria Escherichia coli ML-35, Pseudomonas aeruginosa and Salmonela typhimurium, but showed limited inhibitory activity toward Gram-positive bacteria, except for Micrococcus luteus. The truncated 26-mer peptide (Ab26), which was synthesized after truncating some amino acid residues at both N-terminus and C-terminus from the Ab37 peptide, still showed equivalent antibacterial activity to the Ab37. On the other hand, several further truncated peptides exhibited lower activity then did Ab37 peptide.

Purification and Characterization of an Antifungal Peptide from the Seeds of Phytolacca americana (미국자리공 종실로부터 항균성 펩타이드의 분리 및 특성 연구)

  • 손대영;신봉정;윤대진;성기영;정영륜
    • Korean Journal Plant Pathology
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    • v.14 no.3
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    • pp.203-208
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    • 1998
  • We isolated and characterized an antifungal peptide from the seeds of Phytolacca americana. Growth inhibition assay with Botrytis cinerea was used to screen inhibitory proteins from 60 different plant species. A 4 kDa antifungal peptide (Pa-AFP) inhibitory to hyphal growth of B. cinerea was found in the seeds of P. americana. The peptide Pa-AFP was purified to homogeneity by chromatographies of Sephadex G-50, DEAE-Sepharose, Sephacryl S-300, and C18 reverse-phase HPLC. Western blot analysis showed that a polyclonal antibody raised against the purified peptide cross-reacted with a 4 kDa protein in seeds but not in root and leaf tissues of P. americana. Pa-AFP inhibited the hyphal growth of Botrytis cinerea, Rihzoctonia solani, Fusarium oxysporum, and Magnaporthe grisea. Pa-AFP exhibited growth inhibition of Saccharomyces cerevisiae strain BWG7a, which was sensitive to osmotin.

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Separation and Purification of Angiotensin-I Converting Enzyme Inhibitory Peptides from Layer Hydrolysate (김 가수분해물로부터 Angiotensin-I Converting Enzyme저해 Peptide의 분리$\cdot$정제)

  • LEE Heon-Ok;KIM Dong-Soo;DO Jeong-Ryong;KWAN Dae-Young
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.34 no.2
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    • pp.164-172
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    • 2001
  • The angiotensin-I converting enzyme (ACE) inhibitors from laver hydrolysate was isolated. Among the 13 kinds of proteases, Maxazyme NNP was most effective for preparing the high ACE inhibitory compound. In extraction conditions of ACE inhibitory peptide from laver hydrolysate, ACE inhibitory activity of hydrolysate treated with diethylether for decolorization and that of $70\%$ ethanol soluble fraction among the different ethanol concentrations were higher than other preparations. Low molecular fraction less than 3,000 dalton of layer hydrolysate separated by ultrafiltration had the highest ACE inhibitory activity, for further separation of ACE inhibitory peptide from laver hydrolysate, gel filtration chromatography (Sephadex G-25), reverse-phase HPLC (ODS & Vydac C-18) and gel permeation chromatography (Superdex Peptide HR) were performed. The molecular mass of the ACE inhibitory peptide fractions of gel permeation chromatography determined by electrospray-mass spectrometer were 413.48 (S1O2V2V1P),346.86 (S1O2V2V2P) and 320.32 (S2O6V3V1P) dalton and their amino acid sequence were Val-Gln-Gly-Asn, Thr-Glu-Thr and Phe-Arg, respectively.

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High-Level Expression of A Bacillus subtilis Mannanase Gene in Escherichia coli. (대장균에서 Bacillus subtilis의 Mannanase 유전자 과잉발현)

  • 권민아;손지영;윤기홍
    • Microbiology and Biotechnology Letters
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    • v.32 no.3
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    • pp.212-217
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    • 2004
  • The gene coding for mannanase from Bacillus subtilis WL-7, a number of glycosyl hydrolase family 26, was hyperexpressed in Escherichia coli. Two recombinant plasmids, pE7MAN and pENS7, were constructed by introducing the complete mannanase gene and the mature mannanase gene lacking N-terminal signal peptide region into a expression vector pET24a(+), respectively. The level of mannanase produced by E. coli BL21 (DE3) carrying pENS7, which included the mature mannanase gene, was considerably higher than that by E. coli BL21 (DE3)/pE7MAN. Almost mannanase produced by the recombinant E. coli carrying pENS7 at growth temperature of $37^{\circ}C$ existed as inactive enzyme of insoluble form. Growth at temperature below $31^{\circ}C$ increased the soluble fraction of mannanase having catalytic activity in the recombinant E. coli cells. The highest productivity of active mannanase was observed in cell-free extract of the recombinant E. coli grown at growth temperature ranging from $25^{\circ}C$ to $28^{\circ}C$, while mannanase activity per soluble protein of the cell-free extract was highest in the cells grown at $^31{\circ}C$.

Diurnal Variations in Serum Glucose, Insulin and C-Peptide of Normal Korean Adults (정상(正常) 한국인(韓國人) 혈청(血淸) 포도당(葡萄糖), Insulin 및 C-Peptide의 일중(日中) 변동(變動)에 관(關)한 연구(硏究))

  • Hong, Kee-Suk;Choi, Du-Hyok;Chung, June-Key;Lee, Hong-Kyu;Koh, Chang-Soon
    • The Korean Journal of Nuclear Medicine
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    • v.17 no.1
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    • pp.41-53
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    • 1983
  • It is already well known that many factors are involved in maintaining normal blood glucose level. The amount and components of meal are also thought to be some of the factors which affect the blood glucose and insulin levels. It is reported that as for Koreans sugar takes up over 75% out of 2,098 kcal, the average daily calorie intake per adult. It implies that Koreans take a high-sugar diet compared with Westerners who take $40\sim50%$ of sugar out of their total average daily calorie. For the purpose of studying diurnal variations in serum glucose, insulin and C-peptide of normal Korean adults based on ordinary Korean diet, we selceted 13 normal Korean male adults and divided them into two groups, Group I (7 persons) and Group II (6 persons). We put Group I on 3,100kcal and 75% sugar diet, and Group II on 2,100 kcal and 69% sugar diet per day for over 4 days. Serum glucose, insulin and C-peptide were checked every 30 minutes or every hour throughout 24 hours. Results are as follows: 1. As for serum glucose level, in the prep ran dial fasting state in the morning, $mean{\pm}S.D.$ of Group I was $91.1{\pm}8.2mg%$, while that of Group II is $82.5{\pm}4.4mg%$. Both groups showed peaks of increased glucose level at postprandial 1 hour after each meal. The peak returned to the level shown during the fasting state at postprandial 1 hour after breakfast while the relatively high glucose levels were maintained respectively even for 2 or 3 hours.after lunch and dinner. 2. As for serum insulin level, Group showed $mean{\pm}S.D.$ of $14.7{\pm}3.0{\mu}U/ml$ while Group II shows that of $7.0{\pm}2.6{\mu}U/ml$ in the fasting state. Group I particularly showed the largest peak from preprandial a half or one and half an hour to postprandial one hour of lunch, and made relatively small peaks $(47.7{\pm}10.8{\mu}U/ml)$ at postorandial 1 hour after breakfast and dinner. No such large peak was marked in Group II, though it showed relatively similar patterns of peak after each meal. 3. As for C-peptide, in the fasting state, Group I and Group II showed $3.50{\pm}1.85$ and $1.66{\pm}0.53ng/ml$ of $mean{\pm}S.D.$, respectively. Group II showed peaks parallel to those for insulin level. None out of seven in Group I showed expected increase in C-peptide based insulin secretion at a half or one and half an hour before lunch. On the contrary, C-peptide increased in 5 subjects out of seven in Group I at 11:00 p.m. when insulin did not increase. 4. According to the integrated concentration method for a measurement of 24-hour total. insulin secretion rate, the $mean{\pm}S.D.$ of Group I was $76.4{\pm}15.2$ U and that of Group II was $58.6{\pm}21.1$ U. The above results confirm that Koreans, when given ordinary diet of 2,100 kcal and 69%, sugar, show insulin secretion pattern essentially similar to that of Westerners. On the contrary, when they are put on a high-calorie diet of 3,100 kcal a day, 75% of which is sugar, insulin secretion can be increased before lunch without increase in blood glucose. These results implies that insulin secretion can be affected by some other factors. The observation that an increase in C-peptide after 11 : 00 p.m. independent of insulin level supports an assertion that insulin secretion and C-peptide secretion can be thought as being physiologically dissociable, and these changes of diurnal patterns in the levels of serum insulin and C-peptide are thought to be resulted from the large meal and high-carbohydrate diet.

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Studies on the inhibitory substance of yeast growth - (Part 1) Isolation and biochemical characteristics of yeast growth inhibitor - (항효모성물질(抗酵母性物質)에 관(關)한 연구(硏究) - (제 1 보)(第 1 報) 분리(分離) 및 그 생화학적작용(生化學的作用)과 성질(性質)에 대(對)해서 -)

  • Seu, Jung-Hwn;Kho, Yung-Hee
    • Applied Biological Chemistry
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    • v.15 no.1
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    • pp.19-25
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    • 1972
  • A kind of peptide which posseses an yeaststatic activity was isolated from Astragalus membranaceus Bunge and following characteristics was obtained. 1. The isoelectric pH of this peptide was 8.2 and histidine, an alkaline amino acid, was identified from this peptide. 2. This substance showes conspicuous heat stability and does not indicate any remarkable reduction of yeaststatic activity even for 5 hours treatment at $100^{\circ}C$. or for 30 minutes at $121^{\circ}C$. 3. The inhibitory activity of the yeast growth is not originated from the yeastcidal action but yeaststatic effect of this sample. 4. The sample shows strong stability ranging from pH 2 to 10. 5. The saccharide; glucose, sucrose, maltose, gives no effect on the yeaststatic activity of the sample even high concentration, 15 percent, and also no effect gives by magnesium, calcium and phosphate salts. 6. The available concentration of this sample on the inhibition of yeast growth was located at the ppm extent, for example, the concentration of fifty percent growth inhibition to Saccharomyces cerevisiae or S. carsbergensis was 4 ppm and 3 ppm to Candida pulcherrima, 13 ppm to S. coreanus, 18 ppm to S. sake and 38 ppm to C. tropicalis. 7. On the alcohol fermentation of S. coreanus, the peptide, an yeast growth inhibitor, gives no effect at all. 8. This substance is named as Astradix-P (Astragalus membranaceus, Radix, Peptide).

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Cloning and functional expression of a cecropin-A gene from the Japanese oak silkworm, Antheraea yamamai (천잠 cecropin-A 유전자 클로닝 및 재조합 발현)

  • Kim, Seong-Ryul;Choi, Kwang-Ho;Kim, Sung-Wan;Goo, Tae-Won;Hwang, Jae-Sam
    • Journal of Sericultural and Entomological Science
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    • v.52 no.1
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    • pp.45-51
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    • 2014
  • A cecropin-A gene was isolated from the immunized larvae of the Japanese oak silkworm, Antheraea yamamai and designed Ay-CecA. The complete Ay-CecA cDNA consists of 419 nucleotides with 195 bp open reading frame encoding a 64 amino acid precursor that contains a putative 22-residue signal peptide, a 4-residue propetide and a 37-residue mature peptide with a theoretical mass of 4046.81. The deduced amino acid sequence of the peptide evidenced a significant degree of identity (62 ~ 78% identity) with other lepidopteran cecropins. Like many insect cecropin, Ay-CecA also harbored a glycine residue for C-terminal amidation at the C-end, which suggests potential amidation. To understand this peptide better, we successfully expressed bioactive recombinant Ay-CecA in Escherichia coli that are highly sensitive to the mature peptide. For this, we fused mature Ay-CecA gene with insoluble protein ketosteroid isomerase (KSI) gene to avoid the cell death during induction. The fusion KSI-CecA protein was expressed as inclusion body. The expressed fusion protein was purified by Ni-NTA immobilized metal affinity chromatography (IMAC), and cleaved by cyanogen bromide (CNBr) to release recombinant Ay-CecA. The purified recombinant Ay-CecA showed considerably antibacterial activity against Gram-negative bacteria, E. cori ML 35, Klebsiella pneumonia and Pseudomonas aeruginosa. Our results proved that this peptide with a potent antibacterial activity may play a role in the immune response of Japanese oak silkworm.

Screening Peptides Binding Specifically to Colorectal Cancer Cells from a Phage Random Peptide Library

  • Wang, Jun-Jiang;Liu, Ying;Zheng, Yang;Liao, Kang-Xiong;Lin, Feng;Wu, Cheng-Tang;Cai, Guan-Fu;Yao, Xue-Qing
    • Asian Pacific Journal of Cancer Prevention
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    • v.13 no.1
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    • pp.377-381
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    • 2012
  • The aim of this study was to screen for polypeptides binding specifically to LoVo human colorectal cancer cells using a phage-displayed peptide library as a targeting vector for colorectal cancer therapy. Human normal colorectal mucous epithelial cells were applied as absorber cells for subtraction biopanning with a c7c phage display peptide library. Positive phage clones were identified by enzyme-linked immunosorbent assay and immunofluorescence detection; amino acid sequences were deduced by DNA sequencing. After 3 rounds of screening, 5 of 20 phage clones screened positive, showing specific binding to LoVo cells and a conserved RPM motif. Specific peptides against colorectal cancer cells could be obtained from a phage display peptide library and may be used as potential vectors for targeting therapy for colorectal cancer.