Microcalorimetric study of growth of Lactococcus lactis IL1403 at low glucose concentration in liquids and solid agar gels

2013 ◽  
Vol 559 ◽  
pp. 69-75 ◽  
Author(s):  
N. Kabanova ◽  
I. Stulova ◽  
R. Vilu
Keyword(s):  
Lactococcus Lactis ◽  
Glucose Concentration ◽  
Solid Agar ◽  
Agar Gels ◽  
Low Glucose ◽  
Lactis Il1403

scholarly journals Intraperitoneal Microdialysis as a Monitoring Method in the Intensive Care Unit

2014 ◽  
Vol 99 (6) ◽  
pp. 729-733 ◽  
Author(s):  
Tasiopoulos Konstantinos ◽  
Komnos Apostolos ◽  
Paraforos Georgios ◽  
Tepetes Konstantinos
Keyword(s):  
Intensive Care Unit ◽  
Intensive Care ◽  
Glucose Concentration ◽  
Repeated Measures ◽  
Statistical Significance ◽  
Monitoring Method ◽  
P Values ◽  
Repeated Measures Analysis ◽  
Low Glucose ◽  
Surgical Condition

Abstract Studies on surgical patients provide some evidence of prompt detection of enteric ischemia with microdialysis. The purpose of the study was to measure intraperitoneal microdialysis values (glucose, glycerol, pyruvate, and lactate) in patients hospitalized in an intensive care unit (ICU) with an underlying abdominal surgical condition and to correlate these values with patients' outcomes. Twenty-one patients, 10 female, were enrolled in the study. The intraperitoneal metabolite values were measured for 3 consecutive days, starting from the first day of ICU hospitalization. Descriptive and inferential statistics were performed. The t-test, repeated measures analysis, Holm's test, and a logistic regression model were applied. Level of statistical significance was set at P = 0.05. Mean age of participants was 68.10 ± 8.02 years old. Survivors exhibited statistically significantly higher glucose values on day 3 (6.61 ± 2.01 against 3.67 ± 1.62; P = 0.002). Mean lactate/ pyruvate (L/P) values were above 20 (35.35 ± 27.11). All non-survivors had a mean three day L/P values greater than 25.94. Low L/P values were related to increased survival possibilities. High microdialysis glucose concentration, high L/P ratio and low glucose concentration were the major findings during the first three ICU hospitalization days in non-survivors. Intraperitoneal microdialysis may serve as a useful tool in understanding enteric ischemia pathophysiology.

Effect of perfusate glucose concentration on rat lung glycolysis.

1979 ◽  
Vol 236 (3) ◽  
pp. E229 ◽  
Author(s):  
J S Kerr ◽  
N J Baker ◽  
D J Bassett ◽  
A B Fisher
Keyword(s):  
Glucose Concentration ◽  
Glucose Utilization ◽  
Glycogen Content ◽  
Lactate Production ◽  
Bicarbonate Buffer ◽  
Exogenous Glucose ◽  
Low Glucose ◽  
The Difference ◽  
Endogenous Substrates ◽  
The Relationship

We investigated the relationship between perfusate concentration of glucose and its utilization and lactate production derived from exogenous glucose and from metabolism of endogenous substrates. Isolated rat lungs were ventilated with 5% CO2 in air and perfused for 100 min with Krebs-Ringer bicarbonate buffer containing 3% bovine serum albumin, 10(-2) U/ml insulin, [U-14C]glucose and [5-3H]glucose. Glucose utilization, total lactate production, [14C]lactate production, and 3H2O production were measured. The apparent Km and Vmax for glucose utilization were 3.4 mM and 72.5 mumol/g dry wt per h, respectively. Lactate production from endogenous substrates, calculated as the difference between total and [14C]lactate, was 37.6 +/- 2.2 mumol/g dry wt (n = 36); it was unaffected by perfusate glucose concentration and by omission of insulin, but increased threefold with anoxia. Lactate production from 1.5 mM glucose was significantly less (P less than 0.02) with insulin omitted. Glycogen content was unchanged during perfusion without glucose. These results suggest that: 1) protein catabolism contributes to lung lactate production; 2) glucose utilization by lung is not maximal at resting physiological glucose concentrations; and 3) insulin is required at low glucose concentrations for maximal glycolytic rates.

Effect of glucose and oxygen deprivation on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells

2003 ◽  
Vol 285 (6) ◽  
pp. R1453-R1460 ◽  
Author(s):  
S. D. Appleton ◽  
G. E. Lash ◽  
G. S. Marks ◽  
K. Nakatsu ◽  
J. F. Brien ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Protein Content ◽  
Heme Oxygenase ◽  
Glucose Concentration ◽  
Placental Tissue ◽  
Glucose Deprivation ◽  
First Trimester ◽  
Trophoblast Cells ◽  
Chorionic Villi ◽  
Low Glucose

Although hypoxia induces heme oxygenase (HO)-1 mRNA and protein expression in many cell types, recent studies in our laboratory using human placental tissue have shown that a preexposure to hypoxia does not affect subsequent HO enzymatic activity for optimized assay conditions (20% O2; 0.5 mM NADPH; 25 μM methemalbumin) or HO-1 protein content. One of the consequences of impaired blood flow is glucose deprivation, which has been shown to be an inducer of HO-1 expression in HepG2 hepatoma cells. The objective of the present study was to test the effects of a 24-h preexposure to glucose-deprived medium, in 0.5 or 20% O2, on HO protein content and enzymatic activity in isolated chorionic villi and immortalized HTR-8/SVneo first-trimester trophoblast cells. HO protein content was determined by Western blot analysis, and microsomal HO enzymatic activity was measured by assessment of the rate of CO formation. HO enzymatic activity was increased ( P < 0.05) in both placental models after 24-h preexposure to glucose-deficient medium in 0.5 or 20% O2. Preexposure (24 h) in a combination of low O2 and low glucose concentrations decreased the protein content of the HO-1 isoform by 59.6% ( P < 0.05), whereas preexposure (24 h) to low glucose concentration alone increased HO-2 content by 28.2% in chorionic villi explants ( P < 0.05). In this preparation, HO enzymatic activity correlated with HO-2 protein content ( r = 0.825). However, there was no correlation between HO-2 protein content and HO enzymatic activity in HTR-8/SVneo trophoblast cells preexposed to 0.5% O2 and low glucose concentration for 24 h. These findings indicate that the regulation of HO expression in the human placenta is a complex process that depends, at least in part, on local glucose and oxygen concentrations.

Ribosomes, ribosomal subunits and ribosomal proteins of Lactococcus lactis IL1403

Biochimie ◽  
1992 ◽  
Vol 74 (11) ◽  
pp. 995-1005 ◽  
Author(s):  
N LIMASNZOUZI ◽  
M GUERIN ◽  
D HAYES
Keyword(s):  
Lactococcus Lactis ◽  
Ribosomal Proteins ◽  
Ribosomal Subunits ◽  
Lactis Il1403

Non-enzymic copper reduction by menaquinone enhances copper toxicity in Lactococcus lactis IL1403

Microbiology ◽  
2013 ◽  
Vol 159 (Pt_6) ◽  
pp. 1190-1197 ◽  
Author(s):  
Helge K. Abicht ◽  
Yulia Gonskikh ◽  
Simon D. Gerber ◽  
Marc Solioz
Keyword(s):  
Lactococcus Lactis ◽  
Copper Toxicity ◽  
Lactis Il1403

Recombinant interleukin 6 with M cell-targeting moiety produced in Lactococcus lactis IL1403 as a potent mucosal adjuvant for peroral immunization

Vaccine ◽  
2015 ◽  
Vol 33 (16) ◽  
pp. 1959-1967 ◽  
Author(s):  
Hui-Shan Li ◽  
Da-Chuan Piao ◽  
Tao Jiang ◽  
Jin-Duck Bok ◽  
Chong-Su Cho ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Interleukin 6 ◽  
Cell Targeting ◽  
M Cell ◽  
Mucosal Adjuvant ◽  
Lactis Il1403

scholarly journals Alternative Lactose Catabolic Pathway in Lactococcus lactis IL1403

2005 ◽  
Vol 71 (10) ◽  
pp. 6060-6069 ◽  
Author(s):  
Tamara Aleksandrzak-Piekarczyk ◽  
Jan Kok ◽  
Pierre Renault ◽  
Jacek Bardowski
Keyword(s):  
Lactococcus Lactis ◽  
Protein A ◽  
Lactose Hydrolysis ◽  
Galactosidase Activity ◽  
Solid Media ◽  
Pathway Gene ◽  
Leloir Pathway ◽  
Catabolite Control Protein A ◽  
Lactis Il1403 ◽  
Strong Control

ABSTRACT In this study, we present a glimpse of the diversity of Lactococcus lactis subsp. lactis IL1403 β-galactosidase phenotype-negative mutants isolated by negative selection on solid media containing cellobiose or lactose and X-Gal (5-bromo-4-chloro-3-indolyl-β-d-galactopyranoside), and we identify several genes essential for lactose assimilation. Among these are ccpA (encoding catabolite control protein A), bglS (encoding phospho-β-glucosidase), and several genes from the Leloir pathway gene cluster encoding proteins presumably essential for lactose metabolism. The functions of these genes were demonstrated by their disruption and testing of the growth of resultant mutants in lactose-containing media. By examining the ccpA and bglS mutants for phospho-β-galactosidase activity, we showed that expression of bglS is not under strong control of CcpA. Moreover, this analysis revealed that although BglS is homologous to a putative phospho-β-glucosidase, it also exhibits phospho-β-galactosidase activity and is the major enzyme in L. lactis IL1403 involved in lactose hydrolysis.

Sign in / Sign up

Export Citation Format

Share Document