Skip header and navigation

Refine By

52 records – page 1 of 6.

[Acute kidney injury and tubular biomarkers after hematopoietic stem cell transplantation].

https://arctichealth.org/en/permalink/ahliterature275530
Source
Ter Arkh. 2016;88(6):14-20
Publication Type
Article
Date
2016
Author
V A Dobronravov
K A Smirnov
B V Afanas'ev
O V Galkina
A V Smirnov
Source
Ter Arkh. 2016;88(6):14-20
Date
2016
Language
Russian
Publication Type
Article
Keywords
Acute Kidney Injury - diagnosis - etiology - metabolism - physiopathology
Adult
Biomarkers - blood
Chemokine CCL2 - blood
Female
Hematopoietic Stem Cell Transplantation - adverse effects
Humans
Kidney Function Tests
Kidney Tubules - metabolism - pathology - physiopathology
Male
Membrane Glycoproteins - blood
Middle Aged
Predictive value of tests
Prospective Studies
Receptors, Virus - blood
Reproducibility of Results
Russia
Abstract
To determine the value of molecular biomarkers (BMs) associated with tubular epithelial damage in developing and predicting acute kidney injury (AKI) after hematopoietic stem cell transplantation (HSCT).
The open-label observational prospective study enrolled 90 patients (46 males and 44 females) who had undergone HSCT. The concentrations of BMs (calbindin, clusterin, interleukin-18 (IL-18), kidney injury molecules-1 (KIM-1), glutathione S-transferase-p (GST-p), and monocyte chemoattractant protein-1 (MCP-1) were measured in urinary samples 7 days before HSCT (week 0) and at weeks 1, 2, 3, 4, and 5. Main clinical parameters were simultaneously monitored. AKI was diagnosed and stratified according to the Kidney Disease Improving Global Outcomes (KDIGO) guidelines.
At weeks 1, 2, 3, 4, and 5 after HSCT, the proportion of AKI cases was 7.8, 8.9, 12.5, 27.3, and 35.9%, respectively. The elevated urinary levels of BMs (above the median) were found to be substantially more common than AKI cases. The urinary excretion of the majority of BMs dramatically increased in the early HSCT period. The median number of simultaneously elevated BMs was 3 (2; 5) during the entire follow-up period. Clusterin, MCP-1 and KIM-1 positively and significantly correlated with serum creatinine at the week following the determination of BMs in the multivariate linear regression models adjusted for other confounders. The higher urinary KIM-1 and/or MCP-1 excretion regardless of other clinical indicators was associated with the higher relative risk (RR) of AKI, which increased by 2.3 times with a rise in one of these indicators and by 3.4 times with a rise in both indicators.
Multiple renal toxic effects after HSCT result in a substantial and simultaneous elevation of urinary excretion of BMs for tubular damage. Among the BMs studied, KIM-1 and MCP-1 seem to be the most suitable molecules for assessing the risk of AKI in this cohort of patient within the predictive diagnostic approach.
PubMed ID
27296256 View in PubMed
Less detail

Adsorption inhibition as a mechanism of freezing resistance in polar fishes.

https://arctichealth.org/en/permalink/ahliterature46812
Source
Proc Natl Acad Sci U S A. 1977 Jun;74(6):2589-93
Publication Type
Article
Date
Jun-1977
Author
J A Raymond
A L DeVries
Source
Proc Natl Acad Sci U S A. 1977 Jun;74(6):2589-93
Date
Jun-1977
Language
English
Publication Type
Article
Keywords
Acclimatization
Adsorption
Animals
Blood Proteins - physiology
Cold Climate
Fishes - physiology
Freezing
Glycoproteins - blood
Kinetics
Microscopy, Electron, Scanning
Molecular Weight
Protein Conformation
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Species Specificity
Abstract
Polar fishes are known to have serum proteins and glycoproteins that protect them from freezing, by a noncolligative process. Measurements of antifreeze concentrations in ice and scanning electron micrographs of freeze-dried antifreeze solutions indicate that the antifreezes are incorporated in ice during freezing. The antifreezes also have a pronounced effect on the crystal habit of ice grown in their presence. Each of four antifreezes investigated caused ice to grow in long needles whose axes were parallel to the ice c axis. Together these results indicate the antifreezes adsorb to ice surfaces and inhibit their growth. A model in which adsorbed antifreezes raise the curvature of growth steps on the ice surface is proposed to account for the observed depression of the temperature at which freezing occurs and agrees well with experimental observations. The model is similar to one previously proposed for other cases of crystal growth inhibition.
PubMed ID
267952 View in PubMed
Less detail

Antifreeze glycoproteins from Polar fish. Effects of freezing conditions on cooperative function.

https://arctichealth.org/en/permalink/ahliterature3393
Source
J Biol Chem. 1980 Jan 25;255(2):659-62
Publication Type
Article
Date
Jan-25-1980
Author
D M Mulvihill
K F Geoghegan
Y. Yeh
K. DeRemer
D T Osuga
F C Ward
R E Feeney
Source
J Biol Chem. 1980 Jan 25;255(2):659-62
Date
Jan-25-1980
Language
English
Publication Type
Article
Keywords
Animals
Arctic Regions
Fishes - blood
Freezing
Glycopeptides - blood
Glycoproteins - blood
Molecular Weight
Research Support, U.S. Gov't, P.H.S.
Sodium Chloride
Abstract
Antifreeze glycoproteins and glycopeptides that function noncolligatively contribute one-third of the freezing temperature depression in the blood serum of some polar fishes and enable them to survive at low temperature (-1.9 degree C). There are at least eight closely related glycoproteins and glycopeptides ranging in molecular weight from 32,000 to 2,600 and numbered 1 to 8 in order of decreasing size. Under conditions of negligible supercooling, the glycopeptides have weaker antifreeze activity than the glycoproteins (20% on a weight basis, or 5% on a molar basis); in mixtures of both, their activities are additive. When nucleation is initiated in supercooled solutions (-4 to -5 degrees C), the glycopeptides are inactive, while the glycoproteins still show activity; when mixtures of both are nucleated in supercooled solutions, cooperative potentiation occurs, and the full activities of the glycopeptides are found. On nucleation of supercooled solutions of the glycoprotein alone or of the mixtures, the temperature rises above the freezing temperature ("overshoots") to an extent dependent upon the extent of supercooling; the temperature of the sample then decreases to form a plateau at the true freezing temperature.
PubMed ID
7356636 View in PubMed
Less detail

Association between microfibrillar-associated protein 4 (MFAP4) and micro- and macrovascular complications in long-term type 1 diabetes mellitus.

https://arctichealth.org/en/permalink/ahliterature282243
Source
Acta Diabetol. 2017 Apr;54(4):367-372
Publication Type
Article
Date
Apr-2017
Author
S L Blindbæk
A. Schlosser
A. Green
U. Holmskov
G L Sorensen
J. Grauslund
Source
Acta Diabetol. 2017 Apr;54(4):367-372
Date
Apr-2017
Language
English
Publication Type
Article
Keywords
Adult
Aged
Aged, 80 and over
Biomarkers - blood
Cardiovascular Diseases - blood - complications - diagnosis
Carrier Proteins - blood
Cross-Sectional Studies
Denmark
Diabetes Mellitus, Type 1 - blood - complications - diagnosis
Diabetic Angiopathies - blood - diagnosis
Diabetic Neuropathies - blood - complications - diagnosis
Diabetic Retinopathy - blood - complications - diagnosis
Extracellular Matrix Proteins - blood
Female
Glycoproteins - blood
Humans
Male
Middle Aged
Predictive value of tests
Risk factors
Abstract
To evaluate microfibrillar-associated protein 4 (MFAP4) as a marker of micro- and macrovascular complications in patients with type 1 diabetes.
This cross-sectional study included 203 persons with a long duration of type 1 diabetes from a population-based cohort ascertained in the former Funen County, Denmark. Detection of plasma-MFAP4 (pMFAP4) was performed by the AlphaLISA Technique. Diabetic retinopathy (DR) was graded in accordance with the Early Treatment Diabetic Retinopathy Study adaptation of the modified Airlie House classification. A monofilament test was used to test for neuropathy, and nephropathy was evaluated in a single spot urine sample. Data describing macrovascular disease were obtained from the Danish National Patient Register.
Median age and duration of diabetes were 58.7 and 43 years, respectively, and 61% were males. High levels of pMFAP4 were found in participants of old age, in women and in non-smokers (p 
PubMed ID
28039584 View in PubMed
Less detail

Changes in circulating progenitor cells are associated with outcome in heart failure patients: a longitudinal study.

https://arctichealth.org/en/permalink/ahliterature107110
Source
Can J Cardiol. 2013 Dec;29(12):1657-64
Publication Type
Article
Date
Dec-2013
Author
Ana C Alba
Spencer D Lalonde
Vivek Rao
Stephen D Walter
Gordon H Guyatt
Heather J Ross
Author Affiliation
Heart Failure/Transplant Program, Toronto General Hospital, University Health Network, Toronto, Ontario, Canada. Electronic address: Carolina.alba@uhn.ca.
Source
Can J Cardiol. 2013 Dec;29(12):1657-64
Date
Dec-2013
Language
English
Publication Type
Article
Keywords
Aged
Antigens, CD - blood
Antigens, CD34 - blood
Cell Count
Colony-Forming Units Assay
Endothelial Cells - pathology
Female
Glycoproteins - blood
Heart Failure - mortality - pathology
Heart Transplantation - statistics & numerical data
Heart-Assist Devices - statistics & numerical data
Humans
Longitudinal Studies
Male
Middle Aged
Ontario
Oxygen - blood
Patient Admission - statistics & numerical data
Patient Outcome Assessment
Peptides - blood
Prognosis
Stem Cells - pathology
Vascular Endothelial Growth Factor Receptor-2 - blood
Ventricular Dysfunction, Left - mortality - pathology
Abstract
Circulating progenitor cells (CPCs) are involved in the process of endothelial repair and are a prognostic factor in cardiovascular diseases. We evaluated the association between serial measurements of CPCs and functional capacity and outcomes in heart failure (HF).
We included 156 consecutive consenting ambulatory HF patients (left ventricular ejection fraction
PubMed ID
24054922 View in PubMed
Less detail

[Changes in indices of connective tissue in patients with alcoholic and non-alcoholic steatohepatitis and their correction with glutargin]

https://arctichealth.org/en/permalink/ahliterature47109
Source
Lik Sprava. 2004 Oct-Nov;(7):25-8
Publication Type
Article
Author
O S Khukhlina
Source
Lik Sprava. 2004 Oct-Nov;(7):25-8
Language
Ukrainian
Publication Type
Article
Keywords
Adult
Collagen - blood - metabolism
Connective Tissue - drug effects - metabolism
Diabetes Mellitus, Type 2 - complications - metabolism
Dipeptides - therapeutic use
English Abstract
Extracellular Matrix - drug effects - metabolism
Fatty Liver - complications - drug therapy - metabolism
Fatty Liver, Alcoholic - complications - drug therapy - metabolism
Glycoproteins - blood - metabolism
Glycosaminoglycans - blood - metabolism
Humans
Middle Aged
Protective Agents - therapeutic use
Abstract
The study of protein and carbohydrate components of extracellular matrix in patients with alcoholic and non alcoholic steatohepatitis developed on the background of type 2 diabetes mellitus has shown a significant increase in collagen and glycosaminoglycan synthesis along with the enhancement of proteolytic and compensatory collagenous activity of blood plasma in patients with alcoholic steatohepatitis and inhibition of collagenolytic and proteolytic activity of blood plasma in patients with non alcoholic steatohepatitis against the background of diabetes mellitus, decrease in glycoprotein synthesis. Glutargin enhances metabolism of connective tissue by impeding collagen and glycosaminoglycan synthesis, activating proteoglycan production, augmenting blood plasma activity in patients with non alcoholic steatohepatitis, hindering proteolysis in patients with alcoholic steatohepatitis as well as increasing the excretion of connective tissue metabolites through urinary tracts.
PubMed ID
15724606 View in PubMed
Less detail

Circulating amounts of osteoprotegerin and RANK ligand: genetic influence and relationship with BMD assessed in female twins.

https://arctichealth.org/en/permalink/ahliterature67185
Source
Bone. 2005 Apr;36(4):727-35
Publication Type
Article
Date
Apr-2005
Author
Bo Abrahamsen
Jacob Vb Hjelmborg
Paul Kostenuik
Lis S Stilgren
Kirsten Kyvik
Stephen Adamu
Kim Brixen
Bente L Langdahl
Author Affiliation
Department of Endocrinology, Odense University Hospital, Denmark. b.abrahamsen@dadlnet.dk
Source
Bone. 2005 Apr;36(4):727-35
Date
Apr-2005
Language
English
Publication Type
Article
Keywords
Adult
Bone Density
Carrier Proteins - blood
Contraceptives, Oral - administration & dosage
Denmark
Female
Glycoproteins - blood
Humans
Membrane Glycoproteins - blood
Menopause
Middle Aged
Receptors, Cytoplasmic and Nuclear - blood
Receptors, Tumor Necrosis Factor - blood
Registries
Regression Analysis
Research Support, Non-U.S. Gov't
Smoking
Abstract
Osteoprotegerin (OPG) is a circulating receptor that inhibits osteoclastogenesis by binding to RANK ligand (RANKL). OPG knock-out animals develop severe osteoporosis. Treatment with OPG lowers bone resorption and increases BMD. OPG production is influenced by a wide range of hormones and cytokines. The influence of genetic factors on circulating amounts of OPG and RANKL is not known. BMD has been demonstrated to have a high heritability and there is evidence also that bone turnover and bone loss rates are controlled at least in part by genetic factors. OBJECTIVE: Assessing the genetic impact on serum OPG and RANKL in women and estimation of the relative contribution of this inheritance to the total heritability of BMD. METHODS: 188 female twins (52 DZ and 42 MZ pairs) from the Danish Twin Registry were included in the study. Mean age was 35 years (range 19-64 years), average spine BMD was 1.04 +/- 0.11 g/cm2. Serum levels of OPG and RANKL were measured by ELISA (Biomedica, Vienna, Austria). This register covers twins born in Denmark since 1870. Heritability and environmental influence was assessed using a maximum-likelihood model for genetic pleiotropy. RESULTS: RANKL levels showed a negative correlation with age and lower values in smokers. OPG levels were higher in postmenopausal women. Heritability (h(2)) was 85% for spine BMD and 52% for serum RANKL after adjustment for age, smoking and BMI. By contrast, there was no significant genetic influence on OPG levels (h(2) = 0, 95% CI: 0 to 0.31). Serum OPG was determined almost exclusively by individual environment (e(2) = 0.79), with a small, non-significant contribution from shared environment (c(2) = 0.21). Restricting analyses to the 158 premenopausal twins did not alter the findings. CONCLUSIONS: Serum OPG and RANKL levels have only a weak relation to BMD in healthy women. Phenotype correlations indicate that the genes that contribute to twin similarity for BMD are not genes regulating serum levels of RANKL or OPG. The weak correlation with BMD appears to consist in shared environmental factors.
PubMed ID
15781001 View in PubMed
Less detail

A comparison of high-mobility group-box 1 protein, lipopolysaccharide-binding protein and procalcitonin in severe community-acquired infections and bacteraemia: a prospective study.

https://arctichealth.org/en/permalink/ahliterature162518
Source
Crit Care. 2007;11(4):R76
Publication Type
Article
Date
2007
Author
Shahin Gaïni
Ole G Koldkjaer
Holger J Møller
Court Pedersen
Svend S Pedersen
Author Affiliation
Department of Infectious Diseases, Odense University Hospital, Søndre Boulevard 29, DK-5000 Odense C, Denmark. shahin.gaini@ouh.regionsddanmark.dk
Source
Crit Care. 2007;11(4):R76
Date
2007
Language
English
Publication Type
Article
Keywords
Acute-Phase Proteins
Aged
Bacteremia - blood - diagnosis - mortality
Biological Markers - blood
Calcitonin - blood
Carrier Proteins - blood
Community-Acquired Infections - blood - diagnosis - mortality
Denmark - epidemiology
Female
HMGB1 Protein - blood
Humans
Male
Membrane Glycoproteins - blood
Middle Aged
Predictive value of tests
Prospective Studies
Protein Precursors - blood
Severity of Illness Index
Survival Analysis
Abstract
High-mobility group box-1 protein (HMGB1) has been known as a chromosomal protein for many years. HMGB1 has recently been shown to be a proinflammatory cytokine with a role in the immunopathogenesis of sepsis. Lipopolysaccharide-binding protein (LBP) has a central role in the innate immune response when the host is challenged by bacterial pathogens. Procalcitonin (PCT) has been suggested as a marker of severe bacterial infections and sepsis. The aim of the present study was to investigate levels of HMGB1, LBP and PCT in a well-characterised sepsis cohort. The study plan included analysis of the levels of the inflammatory markers in relation to the severity of infection, to the prognosis and to the ability to identify patients with bacteraemia.
Patients suspected of having severe infections and admitted to a department of internal medicine were included in a prospective manner. Demographic data, comorbidity, routine biochemistry, microbiological data, infection focus, severity score and mortality on day 28 were recorded. Plasma and serum were sampled within 24 hours after admission. Levels of all studied markers (HMGB1, LBP, PCT, IL-6, C-reactive protein, white blood cell count and neutrophils) were measured with commercially available laboratory techniques.
A total of 185 adult patients were included in the study; 154 patients fulfilled our definition of infection. Levels of HMGB1, LBP and PCT were higher in infected patients compared with a healthy control group (P
Notes
Cites: Mol Cell Biol. 1999 Aug;19(8):5237-4610409715
Cites: Science. 1999 Jul 9;285(5425):248-5110398600
Cites: J Infect Dis. 1999 Nov;180(5):1584-910515819
Cites: Pediatr Infect Dis J. 1999 Oct;18(10):875-8110530583
Cites: Crit Care Med. 2005 Mar;33(3):564-7315753748
Cites: Swiss Med Wkly. 2005 Aug 6;135(31-32):451-6016208582
Cites: Thromb Haemost. 2005 Nov;94(5):975-916363239
Cites: Microbes Infect. 2006 Mar;8(3):946-5216483818
Cites: Crit Care. 2006;10(2):R5316569262
Cites: Clin Chim Acta. 2006 Oct;372(1-2):173-816797518
Cites: Pancreas. 2006 Nov;33(4):359-6317079940
Cites: J Leukoc Biol. 2007 Jan;81(1):67-7417060363
Cites: Crit Care Med. 2007 Apr;35(4):1061-717334246
Cites: Crit Care. 2007;11(2):R3217346334
Cites: Intensive Care Med. 2000 Mar;26 Suppl 2:S153-818470711
Cites: Am J Respir Crit Care Med. 2001 Nov 15;164(10 Pt 1):1768-7311734424
Cites: Scand J Clin Lab Invest. 2001;61(7):523-3011763410
Cites: Swiss Med Wkly. 2001 Oct 20;131(41-42):595-60211820070
Cites: Clin Infect Dis. 2002 Jul 15;35(2):156-6112087521
Cites: Clin Chim Acta. 2002 Sep;323(1-2):59-7212135807
Cites: J Infect Dis. 2003 Jan 15;187(2):287-9112552453
Cites: Surg Infect (Larchmt). 2001 Fall;2(3):193-202; discussion 202-312593709
Cites: J Biol Chem. 2003 May 2;278(18):15587-9412594207
Cites: Scand J Infect Dis. 2003;35(9):577-8414620138
Cites: Crit Care. 2003 Dec;7(6):R154-914624690
Cites: Intensive Care Med. 2003 Dec;29(12):2157-6114569424
Cites: Anaesth Intensive Care. 2003 Dec;31(6):629-3614719423
Cites: Crit Care. 2004 Feb;8(1):R12-2014975050
Cites: Eur J Clin Microbiol Infect Dis. 2004 Jul;23(7):539-4415221617
Cites: Scand J Infect Dis. 2004;36(5):365-7115287382
Cites: Immunology. 2004 Oct;113(2):153-6215379975
Cites: Eur J Clin Microbiol Infect Dis. 2004 Sep;23(9):699-70415309668
Cites: J Chronic Dis. 1987;40(5):373-833558716
Cites: Biometrics. 1988 Sep;44(3):837-453203132
Cites: Chest. 1992 Jun;101(6):1481-31600757
Cites: Lancet. 1993 Feb 27;341(8844):515-88094770
Cites: Arch Surg. 1994 Feb;129(2):220-67508221
Cites: Intensive Care Med. 1996 Jul;22(7):707-108844239
Cites: Crit Care Med. 1998 Jun;26(6):1001-69635646
Cites: N Engl J Med. 1999 Jan 21;340(3):207-149895401
Cites: Crit Care Med. 1999 Mar;27(3):498-50410199528
Cites: Clin Chem Lab Med. 1999 Mar;37(3):271-410353471
Cites: Intensive Care Med. 1999 Jun;25(6):556-6610416906
PubMed ID
17625012 View in PubMed
Less detail

[Effect of sessions of measured inhalatory oxygen therapy on the content and distribution of serum glycoproteins in the active phase of rheumatism in children]

https://arctichealth.org/en/permalink/ahliterature43339
Source
Pediatriia. 1973 Mar;(3):22
Publication Type
Article
Date
Mar-1973

52 records – page 1 of 6.