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Article: Effect of heat-shock proteins for relieving physiological stress and enhancing the production of penicillin acylase in Escherichia coli.

Wu, Ming-Shen / Pan, Kao-Lu / Chou, C Perry

2007 Volume 96, Issue 5, Page(s) 956–966

Abstract: High-level expression of recombinant penicillin acylase (PAC) using the strong trc promoter system in Escherichia coli is frequently limited by the processing and folding of PAC precursors (proPAC) in the periplasm, resulting in physiological stress and ... ...

Abstract	High-level expression of recombinant penicillin acylase (PAC) using the strong trc promoter system in Escherichia coli is frequently limited by the processing and folding of PAC precursors (proPAC) in the periplasm, resulting in physiological stress and inclusion body formation in this compartment. Periplasmic heat-shock proteins with protease or chaperone activity potentially offer a promise for overcoming this technical hurdle. In this study, the effect of the two genes encoding periplasmic heat-shock proteins, that is degP and fkpA, on pac overexpression was investigated and manipulation of the two genes to enhance the production of recombinant PAC was demonstrated. Both DeltadegP and DeltafkpA mutants showed defective culture performance primarily due to growth arrest. However, pac expression level was not seriously affected by the mutations, indicating that the two proteins were not directly involved in the pathway for periplasmic processing of proPAC. The growth defect caused by the two mutations (i.e., DeltadegP and DeltafkpA) was complemented by either one of the wild-type proteins, implying that the function of the two proteins could partially overlap in cells overexpressing pac. The possible role that the two heat-shock proteins played for suppression of physiological stress caused by pac overexpression is discussed.
MeSH term(s)	Escherichia coli/drug effects ; Escherichia coli/enzymology ; Escherichia coli/metabolism ; Gene Expression/drug effects ; Heat-Shock Proteins/pharmacology ; Inclusion Bodies ; Penicillin Amidase/biosynthesis ; Penicillin Amidase/genetics ; Periplasm/enzymology ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics
Chemical Substances	Heat-Shock Proteins ; Recombinant Proteins ; Penicillin Amidase (EC 3.5.1.11)
Language	English
Publishing date	2007-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	280318-5
ISSN	1097-0290 ; 0006-3592
ISSN (online)	1097-0290
ISSN	0006-3592
DOI	10.1002/bit.21161
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Article ; Online: Development of a whole-cell screening system for evaluation of the human CYP1A2-mediated metabolism.

Chu, Chih-Chieh / Pan, Kao-Lu / Yao, Hsien-Tsung / Hsu, John Tsu-An

Biotechnology and bioengineering

2011 Volume 108, Issue 12, Page(s) 2932–2940

Abstract: Cytochrome P450 1A2 (CYP1A2) is an important member of cytochrome P450 involved in drug metabolism. In this study, a cell line, Huh7-1A2-I-E, with high expression level of CYP1A2 is established based on Huh7 cells. To achieve this, we constructed a ... ...

Abstract	Cytochrome P450 1A2 (CYP1A2) is an important member of cytochrome P450 involved in drug metabolism. In this study, a cell line, Huh7-1A2-I-E, with high expression level of CYP1A2 is established based on Huh7 cells. To achieve this, we constructed a recombinant lentiviral vector, pLenti-1A2-I-E, containing a single promoter encoding CYP1A2 followed by an internal ribosome entry site (IRES) to permit the translation of enhanced green fluorescence protein (EGFP). Such a design has greatly facilitated the selection of stable cell lines because the translations of CYP1A2 and EGFP proteins would be based on a single bi-cistronic mRNA. The Huh7-1A2-I-E cells were evaluated as a cell-based model for identification of CYP1A2 inhibitors and for studies of cytotoxicity resulted from CYP-mediated drug metabolism. Treatment of Huh7-1A2-I-E cells and the Huh7-E control cells with aflatoxin B1 showed that cells with CYP1A2 expression are much more sensitive to aflatoxin B1 and the cellular toxicity of aflatoxin B1 in Huh7-1A2-I-E cells could be prevented by furafylline, a CYP1A2 inhibitor. A collection of approximately 200 drugs were screened using this system and results indicate that for most drugs the metabolism by CYP1A2 is unlikely to have made a major contribution to the in vitro cytotoxicity except for thimerosal and evoxine. Several previously unidentified CYP1A2 inhibitors such as evoxine and berberine were also identified in this study.
MeSH term(s)	Berberine/metabolism ; Berberine/pharmacology ; Cell Line ; Cytochrome P-450 CYP1A2/genetics ; Cytochrome P-450 CYP1A2/metabolism ; Cytochrome P-450 CYP1A2 Inhibitors ; Drug Evaluation, Preclinical/methods ; Drug-Related Side Effects and Adverse Reactions ; Enzyme Inhibitors/metabolism ; Enzyme Inhibitors/pharmacology ; Humans ; Recombinant Proteins/antagonists & inhibitors ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Theophylline/analogs & derivatives ; Theophylline/metabolism ; Theophylline/pharmacology
Chemical Substances	Cytochrome P-450 CYP1A2 Inhibitors ; Enzyme Inhibitors ; Recombinant Proteins ; Berberine (0I8Y3P32UF) ; Theophylline (C137DTR5RG) ; furafylline (C2087G0XX3) ; CYP1A2 protein, human (EC 1.14.14.1) ; Cytochrome P-450 CYP1A2 (EC 1.14.14.1)
Language	English
Publishing date	2011-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	280318-5
ISSN	1097-0290 ; 0006-3592
ISSN (online)	1097-0290
ISSN	0006-3592
DOI	10.1002/bit.23256
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Article ; Online: Enhanced recombinant protein production and differential expression of molecular chaperones in sf -caspase-1-repressed stable cells after baculovirus infection

Lai Yiu-Kay / Hsu John T-A / Chu Chih-Chieh / Chang Teng-Yuan / Pan Kao-Lu / Lin Chih-Chien

BMC Biotechnology, Vol 12, Iss 1, p

2012 Volume 83

Abstract: Abstract Background There are few studies that have examined the potential of RNA inference (RNAi) to increase protein production in the baculovirus expression vector system (BEVS). Spodoptera frugiperda (fall armyworm) ( Sf )-caspase-1-repressed stable ... ...

Abstract	Abstract Background There are few studies that have examined the potential of RNA inference (RNAi) to increase protein production in the baculovirus expression vector system (BEVS). Spodoptera frugiperda (fall armyworm) ( Sf )-caspase-1-repressed stable cells exhibit resistance to apoptosis and enhancement of recombinant protein production. However, the mechanism of recombinant protein augmentation in baculovirus-infected Caspase-repressed insect cells has not been elucidated. Results In the current study, we utilized RNAi-mediated Sf -caspase-1-repressed stable cells to clarify how the resistance to apoptosis can enhance both intracellular (firefly luciferase) and extracellular (secreted alkaline phosphatase [SEAP]) recombinant protein production in BEVS. Since the expression of molecular chaperones is strongly associated with the maximal production of exogenous proteins in BEVS, the differential expression of molecular chaperones in baculovirus-infected stable cells was also analyzed in this study. Conclusion The data indicated that the retention of expression of molecular chaperones in baculovirus-infected Sf -caspase-1-repressed stable cells give the higher recombinant protein accumulation.
Keywords	Apoptosis ; Baculovirus ; Chaperone ; RNA interference ; Sf -caspase-1 ; Biotechnology ; TP248.13-248.65 ; Chemical technology ; TP1-1185 ; Technology ; T ; DOAJ:Biotechnology ; DOAJ:Life Sciences ; DOAJ:Biology and Life Sciences
Subject code	570
Language	English
Publishing date	2012-11-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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Article ; Online: Development of NS3/4A protease-based reporter assay suitable for efficiently assessing hepatitis C virus infection.

Pan, Kao-Lu / Lee, Jin-Ching / Sung, Hsing-Wen / Chang, Teng-Yuang / Hsu, John T-A

Antimicrobial agents and chemotherapy

2009 Volume 53, Issue 11, Page(s) 4825–4834

Abstract: A cell culture system for the production of hepatitis C virus (HCV) whole virions has greatly accelerated studies of the virus life cycle and the discovery of anti-HCV agents. However, the quantification of the HCV titers in a whole-virus infection/ ... ...

Abstract	A cell culture system for the production of hepatitis C virus (HCV) whole virions has greatly accelerated studies of the virus life cycle and the discovery of anti-HCV agents. However, the quantification of the HCV titers in a whole-virus infection/replication system currently relies mostly on reverse transcription-PCR or immunofluorescence assay, which would be cumbersome for high-throughput drug screening. To overcome this problem, this study has generated a novel cell line, Huh7.5-EG(Delta4B5A)SEAP, that carries a dual reporter, EG(Delta4B5A)SEAP. The EG(Delta4B5A)SEAP reporter is a viral protease-cleavable fusion protein in which the enhanced green fluorescence protein is linked to secreted alkaline phosphatase (SEAP) in frame via Delta4B5A, a short peptide cleavage substrate for NS3/4A viral protease. This study demonstrates that virus replication/infection in the Huh7.5-EG(Delta4B5A)SEAP cells can be quantitatively indicated by measuring the SEAP activity in cell culture medium. The levels of SEAP released from HCV-infected Huh7.5-EG(Delta4B5A)SEAP cells correlated closely with the amounts of HCV in the inocula. The Huh7.5-EG(Delta4B5A)SEAP cells were also shown to be a suitable host for the discovery of anti-HCV inhibitors by using known compounds that target multiple stages of the HCV life cycle. The Z'-factor of this assay ranged from 0.64 to 0.74 in 96-well plates, indicating that this reporter system is suitable for high-throughput screening of prospective anti-HCV agents.
MeSH term(s)	Alkaline Phosphatase/genetics ; Alkaline Phosphatase/metabolism ; Antiviral Agents/pharmacology ; Carrier Proteins/genetics ; Carrier Proteins/physiology ; Cell Line ; Genes, Reporter ; Hepacivirus/drug effects ; Hepacivirus/physiology ; High-Throughput Screening Assays ; Humans ; Intracellular Signaling Peptides and Proteins ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/physiology ; Viral Proteins/genetics ; Viral Proteins/physiology ; Virus Replication
Chemical Substances	Antiviral Agents ; Carrier Proteins ; Intracellular Signaling Peptides and Proteins ; NS3 protein, hepatitis C virus ; NS4A cofactor peptide, Hepatitis C virus ; Viral Nonstructural Proteins ; Viral Proteins ; Alkaline Phosphatase (EC 3.1.3.1)
Language	English
Publishing date	2009-08-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/AAC.00601-09
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Article ; Online: Enhanced recombinant protein production and differential expression of molecular chaperones in sf-caspase-1-repressed stable cells after baculovirus infection.

Lai, Yiu-Kay / Hsu, John T-A / Chu, Chih-Chieh / Chang, Teng-Yuan / Pan, Kao-Lu / Lin, Chih-Chien

BMC biotechnology

2012 Volume 12, Page(s) 83

Abstract: Background: There are few studies that have examined the potential of RNA inference (RNAi) to increase protein production in the baculovirus expression vector system (BEVS). Spodoptera frugiperda (fall armyworm) (Sf)-caspase-1-repressed stable cells ... ...

Abstract	Background: There are few studies that have examined the potential of RNA inference (RNAi) to increase protein production in the baculovirus expression vector system (BEVS). Spodoptera frugiperda (fall armyworm) (Sf)-caspase-1-repressed stable cells exhibit resistance to apoptosis and enhancement of recombinant protein production. However, the mechanism of recombinant protein augmentation in baculovirus-infected Caspase-repressed insect cells has not been elucidated. Results: In the current study, we utilized RNAi-mediated Sf-caspase-1-repressed stable cells to clarify how the resistance to apoptosis can enhance both intracellular (firefly luciferase) and extracellular (secreted alkaline phosphatase [SEAP]) recombinant protein production in BEVS. Since the expression of molecular chaperones is strongly associated with the maximal production of exogenous proteins in BEVS, the differential expression of molecular chaperones in baculovirus-infected stable cells was also analyzed in this study. Conclusion: The data indicated that the retention of expression of molecular chaperones in baculovirus-infected Sf-caspase-1-repressed stable cells give the higher recombinant protein accumulation.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Caspases/chemistry ; Caspases/genetics ; Caspases/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Plasmids/genetics ; Plasmids/metabolism ; RNA Interference ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics ; Sf9 Cells ; Spodoptera ; Transfection
Chemical Substances	Molecular Chaperones ; Recombinant Proteins ; Caspases (EC 3.4.22.-)
Language	English
Publishing date	2012-11-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1472-6750
ISSN (online)	1472-6750
DOI	10.1186/1472-6750-12-83
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Article ; Online: LDOC1 silenced by cigarette exposure and involved in oral neoplastic transformation.

Lee, Chia-Huei / Pan, Kao-Lu / Tang, Ya-Chu / Tsai, Ming-Hsien / Cheng, Ann-Joy / Shen, Mei-Ya / Cheng, Ying-Min / Huang, Tze-Ta / Lin, Pinpin

Oncotarget

2015 Volume 6, Issue 28, Page(s) 25188–25201

Abstract: Previously, we identified global epigenetic aberrations in smoking-associated oral squamous cell carcinoma (OSCC). We hypothesized that cigarette exposure triggers OSCC through alteration of the methylome of oral cells. Here we report that cigarette ... ...

Abstract	Previously, we identified global epigenetic aberrations in smoking-associated oral squamous cell carcinoma (OSCC). We hypothesized that cigarette exposure triggers OSCC through alteration of the methylome of oral cells. Here we report that cigarette smoke condensate (CSC) significantly changes the genomic 5-methyldeoxycytidine content and nuclear accumulation of DNA methyltransferase 1 (DNMT1) and DNMT3A in human untransformed oral cells. By using integrated analysis of cDNA and methylation arrays of the smoking-associated dysplastic oral cell line and OSCC tumors, respectively, we identified four epigenetic targets--UCHL1, GPX3, LXN, and LDOC1--which may be silenced by cigarette. Results of quantitative methylation-specific PCR showed that among these four genes, LDOC1 promoter was the most sensitive to CSC. LDOC1 promoter hypermethylation and gene silencing followed 3 weeks of CSC treatment. LDOC1 knockdown led to a proliferative response and acquired clonogenicity of untransformed oral cells. Immunohistochemistry showed that LDOC1 was downregulated in 53.3% (8/15) and 57.1% (20/35) of premalignant oral tissues and early stage OSCCs, respectively, whereas 76.5% (13/17) of normal oral tissues showed high LDOC1 expression. Furthermore, the microarray data showed that LDOC1 expression had decreased in the lung tissues of current smokers compared with that in those of never smokers and had significantly decreased in the lung tumors of smokers compared with that in normal lung tissues. Our data suggest that CSC-induced promoter methylation may contribute to LDOC1 downregulation, thereby conferring oncogenic features to oral cells. These findings also imply a tumor suppressor role of LDOC1 in smoking-related malignancies such as OSCC and lung cancer.
MeSH term(s)	Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Carcinoma, Non-Small-Cell Lung/genetics ; Carcinoma, Non-Small-Cell Lung/metabolism ; Carcinoma, Non-Small-Cell Lung/pathology ; Carcinoma, Squamous Cell/genetics ; Carcinoma, Squamous Cell/metabolism ; Carcinoma, Squamous Cell/pathology ; Cell Line, Tumor ; Cell Proliferation ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/metabolism ; Cell Transformation, Neoplastic/pathology ; DNA (Cytosine-5-)-Methyltransferase 1 ; DNA (Cytosine-5-)-Methyltransferases/genetics ; DNA (Cytosine-5-)-Methyltransferases/metabolism ; DNA Methylation ; DNA Methyltransferase 3A ; Gene Expression Profiling/methods ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Neoplastic ; Gene Silencing ; Head and Neck Neoplasms/genetics ; Head and Neck Neoplasms/metabolism ; Head and Neck Neoplasms/pathology ; Humans ; Hyperplasia ; Immunohistochemistry ; Lung Neoplasms/genetics ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Mouth Neoplasms/genetics ; Mouth Neoplasms/metabolism ; Mouth Neoplasms/pathology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Oligonucleotide Array Sequence Analysis ; Promoter Regions, Genetic ; RNA Interference ; Smoke/adverse effects ; Smoking/adverse effects ; Smoking/genetics ; Smoking/pathology ; Squamous Cell Carcinoma of Head and Neck ; Time Factors ; Tissue Array Analysis ; Transfection ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism
Chemical Substances	Biomarkers, Tumor ; DNMT3A protein, human ; LDOC1 protein, human ; Nuclear Proteins ; Smoke ; Tumor Suppressor Proteins ; DNA (Cytosine-5-)-Methyltransferase 1 (EC 2.1.1.37) ; DNA (Cytosine-5-)-Methyltransferases (EC 2.1.1.37) ; DNA Methyltransferase 3A (EC 2.1.1.37) ; DNMT1 protein, human (EC 2.1.1.37)
Language	English
Publishing date	2015-08-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.4512
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Article ; Online: Diosgenin, a plant-derived sapogenin, exhibits antiviral activity in vitro against hepatitis C virus.

Wang, Ya-Jean / Pan, Kao-Lu / Hsieh, Tsung-Chih / Chang, Teng-Yuan / Lin, Wen-Hsing / Hsu, John T-A

Journal of natural products

2011 Volume 74, Issue 4, Page(s) 580–584

Abstract: Diosgenin (3β-hydroxy-5-spirostene, 1), a plant-derived sapogenin, is used as a dietary supplement. However, the biological effects of 1 related to viral replication remain unexplored. In this study, the effects of 1 on hepatitis C virus (HCV) ... ...

Abstract	Diosgenin (3β-hydroxy-5-spirostene, 1), a plant-derived sapogenin, is used as a dietary supplement. However, the biological effects of 1 related to viral replication remain unexplored. In this study, the effects of 1 on hepatitis C virus (HCV) replication were evaluated. Based on a reporter-based HCV subgenomic replicon system, 1 was found to inhibit HCV replication at low micromolar concentrations. The EC(50) (concentration at which 50% of HCV replication is inhibited) of 1 was 3.8 μM. No cellular toxicity was observed at this concentration. Diosgenin (1) also significantly reduced the levels of viral RNA and viral proteins as evaluated by quantitative real-time reverse transcriptase PCR and Western blot analysis, respectively. In addition, in an alternative HCV antiviral system more closely aligned to all steps involved in the HCV infection and life cycle, 1 totally abolished HCV replication at 20 μM. Moreover, 1 reduced the phosphorylation of signal transducer and activator of transcription 3. A combination of 1 and interferon-α exerted an additive effect on the resultant anti-HCV activity.
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/isolation & purification ; Antiviral Agents/pharmacology ; Dietary Supplements/analysis ; Diosgenin/chemistry ; Diosgenin/isolation & purification ; Diosgenin/pharmacology ; Hepacivirus/drug effects ; Hepacivirus/genetics ; Humans ; Molecular Structure ; RNA, Viral/analysis ; RNA, Viral/drug effects ; Sapogenins/chemistry ; Sapogenins/isolation & purification ; Sapogenins/pharmacology ; Viral Nonstructural Proteins/drug effects
Chemical Substances	Antiviral Agents ; RNA, Viral ; Sapogenins ; Viral Nonstructural Proteins ; Diosgenin (K49P2K8WLX)
Language	English
Publishing date	2011-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	304325-3
ISSN	1520-6025 ; 0163-3864
ISSN (online)	1520-6025
ISSN	0163-3864
DOI	10.1021/np100578u
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Article ; Online: Identification of trans,trans-2,4-decadienal metabolites in mouse and human cells using liquid chromatography-mass spectrometry.

Pan, Kao-Lu / Huang, Wei-Jan / Hsu, Ming-Hua / Lee, Hui-Ling / Liu, Huei-Ju / Cheng, Chia-Wei / Tsai, Ming-Hsien / Shen, Mei-Ya / Lin, Pinpin

Chemical research in toxicology

2014 Volume 27, Issue 10, Page(s) 1707–1719

Abstract: trans,trans-2,4-Decadienal (tt-DDE), a lipid peroxidation product of linolieic acid, is the most abundant aldehyde identified in cooking oil fumes and is readily detectable in food products as well as in restaurant emissions. Previously, we have reported ...

Abstract	trans,trans-2,4-Decadienal (tt-DDE), a lipid peroxidation product of linolieic acid, is the most abundant aldehyde identified in cooking oil fumes and is readily detectable in food products as well as in restaurant emissions. Previously, we have reported the toxicological effects of tt-DDE in vitro and in vivo. However, the metabolic pathways of tt-DDE in vivo remain unclear. In our present study, we combined liquid chromatography-mass spectrometry with triple quadrupole and time-of-flight to identify tt-DDE metabolites in the urine of mice orally administered tt-DDE. We identified two tt-DDE metabolites, 2,4-decadienoic acid and cysteine-conjugated 2,4-decadien-1-ol, in the urine of mice gavaged with tt-DDE and in human hepatoma cell cultures. The structure of 2,4-decadienoic acid was confirmed upon comparison of its tandem mass spectrometry (MS/MS) spectrum and retention time with those of synthetic standards. The moieties of cysteine and alcohol on cysteine-conjugated 2,4-decadien-1-ol were validated by treating cell cultures with stable-isotope-labeled cysteine and 4-methylpyrazole, an alcohol dehydrogenase inhibitor. The MS/MS spectra of a cysteine standard and ionized cysteine detached from cysteine-conjugated 2,4-decadien-1-ol were identical. Two metabolic pathways for the biotransformation of tt-DDE in vivo are proposed: (i) the oxidation of tt-DDE to the corresponding carboxylic acid, 2,4-decadienoic acid, in liver cells and (ii) glutathione (GHS) conjugation, GSH breakdown, and aldehyde reduction, which generate cysteine-conjugated 2,4-decadien-1-ol in both liver and lung cells. In conclusion, this platform can be used to identify tt-DDE metabolites, and cysteine-conjugated 2,4-decadien-1-ol can serve as a biomarker for assessing exposure to tt-DDE.
MeSH term(s)	Aldehydes/analysis ; Aldehydes/pharmacology ; Aldehydes/urine ; Animals ; Biomarkers/analysis ; Biomarkers/urine ; Biotransformation ; Cell Line ; Cell Survival/drug effects ; Chromatography, High Pressure Liquid ; Cysteine/chemistry ; Glutathione/chemistry ; Glutathione/metabolism ; Humans ; Isomerism ; Isotope Labeling ; Male ; Mice ; Mice, Inbred ICR ; Oxidation-Reduction ; Pyrazoles/chemistry ; Tandem Mass Spectrometry
Chemical Substances	Aldehydes ; Biomarkers ; Pyrazoles ; 2,4-decadienal (2363-88-4) ; fomepizole (83LCM6L2BY) ; Glutathione (GAN16C9B8O) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2014-10-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639353-6
ISSN	1520-5010 ; 0893-228X
ISSN (online)	1520-5010
ISSN	0893-228X
DOI	10.1021/tx500199b
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Article ; Online: Perinatal outcomes in pregnancies managed with antenatal insulin glargine.

Egerman, Robert S / Ramsey, Risa D / Kao, Lu W / Bringman, Jay J / Haerian, Haleh / Kao, Jerome L / Bush, Andrew J

American journal of perinatology

2009 Volume 26, Issue 8, Page(s) 591–595

Abstract: We compared perinatal outcomes in pregnancies in which insulin glargine was used in the management of patients with pregnancies in which standard insulin therapy was used at a single institution. A retrospective analysis of 114 pregnant patients with ... ...

Abstract	We compared perinatal outcomes in pregnancies in which insulin glargine was used in the management of patients with pregnancies in which standard insulin therapy was used at a single institution. A retrospective analysis of 114 pregnant patients with diabetes (pregestational or gestational) managed at a single center between January 2004 and August 2006 was undertaken. Sixty-five patients managed with insulin glargine were compared with 49 patients managed with neutral protamine Hagedorn (NPH) insulin. Both groups were also treated with short-acting insulin (either regular, lispro, or aspart insulin). Maternal age, parity, prepregnancy weight, body mass index, duration of diabetes, hemoglobin A (1C) (at entry and final recorded) and gestational age at entry were similar for each group (glargine and NPH). Thirty patients had gestational diabetes (18 glargine and 12 NPH); there were no differences in numbers of patients in higher-order White's classification between the two groups. Cesarean section for obstetric reasons included labor abnormalities, malpresentation, fetal distress, and suspected macrosomia. There were no differences in gestational age at delivery, birth weight, preeclampsia, or frequency of cesarean section (total or for obstetric reasons). The frequency of shoulder dystocia was higher in the NPH group. Regarding neonatal outcomes, gestational age at delivery, birth weight, Apgar scores, admission to the neonatal intensive care unit, respiratory distress syndrome, hypoglycemia, and congenital anomalies were similar between the two groups. From this retrospective analysis, no adverse maternal or neonatal effects were seen from maternal administration of insulin glargine. A larger multicenter study is needed to confirm these findings. This preliminary report suggests that use of insulin glargine during pregnancy can be considered if maternal metabolic control is suboptimal using the standard split-mix regimen.
MeSH term(s)	Adult ; Diabetes, Gestational/drug therapy ; Female ; Humans ; Hypoglycemic Agents/therapeutic use ; Infant, Newborn ; Insulin/analogs & derivatives ; Insulin/therapeutic use ; Insulin Aspart ; Insulin Glargine ; Insulin Lispro ; Insulin, Isophane ; Insulin, Long-Acting ; Pregnancy ; Pregnancy Outcome ; Pregnancy in Diabetics/drug therapy
Chemical Substances	Hypoglycemic Agents ; Insulin ; Insulin Lispro ; Insulin, Long-Acting ; Insulin Glargine (2ZM8CX04RZ) ; Insulin, Isophane (53027-39-7) ; Insulin Aspart (D933668QVX)
Language	English
Publishing date	2009-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	605671-4
ISSN	1098-8785 ; 0735-1631
ISSN (online)	1098-8785
ISSN	0735-1631
DOI	10.1055/s-0029-1220782
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Article: Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli.

Pan, Kao-Lu / Hsiao, Hsu-Chou / Weng, Chiao-Ling / Wu, Ming-Sheng / Chou, C Perry

Journal of bacteriology

2003 Volume 185, Issue 10, Page(s) 3020–3030

Abstract: Enhancement of the production of soluble recombinant penicillin acylase in Escherichia coli via coexpression of a periplasmic protease/chaperone, DegP, was demonstrated. Coexpression of DegP resulted in a shift of in vivo penicillin acylase (PAC) ... ...

Abstract	Enhancement of the production of soluble recombinant penicillin acylase in Escherichia coli via coexpression of a periplasmic protease/chaperone, DegP, was demonstrated. Coexpression of DegP resulted in a shift of in vivo penicillin acylase (PAC) synthesis flux from the nonproductive pathway to the productive one when pac was overexpressed. The number of inclusion bodies, which consist primarily of protein aggregates of PAC precursors in the periplasm, was highly reduced, and the specific PAC activity was highly increased. DegP was a heat shock protein induced in response to pac overexpression, suggesting that the protein could possibly suppress the physiological toxicity caused by pac overexpression. Coexpression of DegP(S210A), a DegP mutant without protease activity but retaining chaperone activity, could not suppress the physiological toxicity, suggesting that DegP protease activity was primarily responsible for the suppression, possibly by degradation of abnormal proteins when pac was overexpressed. However, a shortage of periplasmic protease activity was not the only reason for the deterioration in culture performance upon pac overexpression because coexpression of a DegP-homologous periplasmic protease, DegQ or DegS, could not suppress the physiological toxicity. The chaperone activity of DegP is proposed to be another possible factor contributing to the suppression.
MeSH term(s)	Enzyme Precursors/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli/physiology ; Gene Expression Regulation, Bacterial ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Inclusion Bodies/metabolism ; Penicillin Amidase/chemistry ; Penicillin Amidase/genetics ; Penicillin Amidase/metabolism ; Periplasm/metabolism ; Periplasmic Proteins/genetics ; Periplasmic Proteins/metabolism ; Protein Folding ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Serine Endopeptidases/genetics ; Serine Endopeptidases/metabolism
Chemical Substances	Enzyme Precursors ; Heat-Shock Proteins ; Periplasmic Proteins ; Recombinant Proteins ; DegP protease (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Penicillin Amidase (EC 3.5.1.11)
Language	English
Publishing date	2003-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.185.10.3020-3030.2003
Database	MEDical Literature Analysis and Retrieval System OnLINE

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