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1.
Gene ; 761: 145036, 2020 Nov 30.
Article in English | MEDLINE | ID: mdl-32777525

ABSTRACT

Lupinus albus γ-conglutin is proposed to positively affect glucose metabolism through inhibition of hepatic glucose production and insulin-mimetic activity; however, the action mechanism is not entirely known. Besides, most studies had focused on its effect on molecular targets directly related to glucose metabolism, and few studies have investigated how γ-conglutin may affect the liver gene expression or if it plays a role in other metabolic processes. Therefore, we investigated the influence of γ-conglutin on the liver transcriptome of streptozotocin-induced diabetic rats using DNA microarrays, ontological analyses, and quantitative PCR. Of the 22,000 genes evaluated, 803 and 173 were downregulated and upregulated, respectively. The ontological analyses of the differentially expressed genes revealed that among others, the mitochondria, microtubules, cytoskeleton, and oxidoreductase activity terms were enriched, implying a possible role of γ-conglutin on autophagy. To corroborate the microarray results, we selected and quantified, by PCR, the expression of two genes associated with autophagy (Atg7 and Snx18) and found their expression augmented two and threefold, respectively; indicating a higher autophagy activity in animals treated with γ-conglutin. Although complementary studies are required, our findings indicate for the first time that the hypoglycaemic effects of γ-conglutin may involve an autophagy induction mechanism, a pivotal process for the preservation of cell physiology and glucose homeostasis.


Subject(s)
Collectins/pharmacology , Lupinus/metabolism , Serum Globulins/pharmacology , Transcriptome/genetics , Animals , Blood Glucose/metabolism , Collectins/metabolism , Collectins/physiology , Diabetes Mellitus, Experimental/chemically induced , Diabetes Mellitus, Experimental/metabolism , Diabetes Mellitus, Type 2/metabolism , Glucose/metabolism , Insulin/metabolism , Liver/metabolism , Liver/pathology , Lupinus/genetics , Male , Plant Proteins/genetics , Rats , Rats, Wistar , Seeds/metabolism , Serum Globulins/metabolism , Serum Globulins/physiology
2.
Rev. cuba. hematol. inmunol. hemoter ; 27(3): 291-296, jul.-set. 2011.
Article in Spanish | CUMED | ID: cum-54092

ABSTRACT

Durante mucho tiempo se asumió que la hemoglobina y la mioglobina eran las únicas globinas de los vertebrados. En el año 2000 se descubrió un tercer tipo de globina, que sobre la base de su ubicación preferencial en el sistema nervioso fue denominada neuroglobina. Aunque aún se desconoce su función específica, se han planteado varias hipótesis entre las que se destaca la que sugiere que puede destoxificar las especies reactivas del oxígeno y el nitrógeno. Otros estudios proponen que es parte de una cadena de transducción de señales que transmite el estado redox de la célula o que inhibe la apoptosis. Aunque algunas funciones son más probables que otras, aún no se ha establecido definitivamente cuál es la función fisiológica de la neuroglobina en los vertebrados. No obstante, no hay dudas de que esta globina tiene una función esencial, conservada y que es beneficiosa para las neuronas(AU)


For a long time, it was taken for granted that hemoglobin and mioglobin were the only vertebrate globins. In 2000, a third type of globins was discovered on the basis of its preferential location in the nervous system and it was called neuroglobin. Although its specific function is still unknown, a number of hypotheses has been put forward, mainly the one suggesting that it may detoxify the reactive oxygen species and the nitrogen. On the other hand, other studies state that neuroglobin is part of a signal transduction chain that transmits the redox state of the cell or inhibits apoptosis. Though some functions are more probable than others, the real physiological function of neuroglobin in vertebrae has not been finally established. Nevertheless, this globin has undoubtedly an essential preserved function that is useful for neurons(AU)


Subject(s)
Humans , Male , Female , Globins/immunology , Neurons/microbiology , Neurons/immunology , Serum Globulins/physiology
3.
Rev. cuba. hematol. inmunol. hemoter ; 27(3): 291-296, jul.-set. 2011.
Article in Spanish | LILACS | ID: lil-615357

ABSTRACT

Durante mucho tiempo se asumió que la hemoglobina y la mioglobina eran las únicas globinas de los vertebrados. En el año 2000 se descubrió un tercer tipo de globina, que sobre la base de su ubicación preferencial en el sistema nervioso fue denominada neuroglobina. Aunque aún se desconoce su función específica, se han planteado varias hipótesis entre las que se destaca la que sugiere que puede destoxificar las especies reactivas del oxígeno y el nitrógeno. Otros estudios proponen que es parte de una cadena de transducción de señales que transmite el estado redox de la célula o que inhibe la apoptosis. Aunque algunas funciones son más probables que otras, aún no se ha establecido definitivamente cuál es la función fisiológica de la neuroglobina en los vertebrados. No obstante, no hay dudas de que esta globina tiene una función esencial, conservada y que es beneficiosa para las neuronas


For a long time, it was taken for granted that hemoglobin and mioglobin were the only vertebrate globins. In 2000, a third type of globins was discovered on the basis of its preferential location in the nervous system and it was called neuroglobin. Although its specific function is still unknown, a number of hypotheses has been put forward, mainly the one suggesting that it may detoxify the reactive oxygen species and the nitrogen. On the other hand, other studies state that neuroglobin is part of a signal transduction chain that transmits the redox state of the cell or inhibits apoptosis. Though some functions are more probable than others, the real physiological function of neuroglobin in vertebrae has not been finally established. Nevertheless, this globin has undoubtedly an essential preserved function that is useful for neurons


Subject(s)
Humans , Male , Female , Globins/immunology , Neurons/immunology , Neurons/microbiology , Serum Globulins/physiology
4.
Afr Health Sci ; 8(4): 217-9, 2008 Dec.
Article in English | MEDLINE | ID: mdl-20589127

ABSTRACT

OBJECTIVE: Human immunodeficiency virus (HIV)-infected patients, especially those on antiretrovirals are at risk of cardiovascular disease (CVD). The haemorheologic and fibrinolgtic activity of treatment naïve Nigerian HIV-infected patients were investigated. METHODS: Blood was collected from 50 newly diagnosed treatment naïve HIV-infected patients and 50 apparently healthy HIV seronegative individuals that served as controls. Haematocrit values, plasma and serum viscosity, plasma fibrinogen concentration and euglobin lysis time were determined. RESULT: The mean +/- standard deviation of haematocrit value of HIV infected patients (31.70 +/- 6.33%) was significantly lower (p<0.0001) than those of controls (39.50 +/- 2.43%). The plasma serum viscosity, plasma fibrinogen concentration and euglobin lysis time of HIV-infected patients were significantly higher compared with those of controls (p<0.0001). CONCLUSION: Treatment naive Nigerian HIV-infected patients have a defective blood flow and fibrinolytic system, which may predispose them to CVD.


Subject(s)
Cardiovascular Diseases/etiology , Fibrinolysis/physiology , HIV Infections/physiopathology , Hemorheology/physiology , Blood Viscosity/physiology , Cardiovascular Diseases/complications , Case-Control Studies , Fibrinogen/analysis , HIV Infections/complications , HIV Infections/virology , HIV-1 , Hematocrit , Humans , Risk Factors , Serum Globulins/analysis , Serum Globulins/physiology
5.
East Afr Med J ; 82(2): 103-5, 2005 Feb.
Article in English | MEDLINE | ID: mdl-16122100

ABSTRACT

BACKGROUND: Malaria infection is still one of the major causes of morbidity and mortality among the under five year children in tropical Africa. Clinical and laboratory methods of assessing the risk factors for severity in order to adequately manage these children, therefore needs to be identified so that prompt and adequate treatment can be instituted early. Fibrinolytic activity has been postulated as one of the risk factors associated with severity of malaria infection. OBJECTIVE: To measure fibrinolytic activity euglobulin lysis time, (ELT) and fibrinogen levels in 50 Nigerian children with Plasmodium falciparum infection. DESIGN: A cross sectional study. SETTING: University of Benin Teaching Hospital, Benin City, Nigeria between January and December 2002. SUBJECTS: Fifty Nigerian children who were admitted with Plasmodium falciparum malaria infection in the paediatric wards of the hospital were recruited into the study. Thirty-four apparently healthy children who did not have malaria fever but who came for growth monitoring exercise and had some investigations done as part of this exercise were used as control for the study. The fibrinolytic activity in all the 84 children (both that had malaria infection and those who did not have malaria infection) were estimated by measuring the euglobulin lysis time (ELT). The fibrinogen levels in all the children were also estimated. The packed cell volume of the children was determined and some severely anaemic children had blood transfusions. RESULTS: Euglobin lysis time (ELT) was found to be higher in children with Plasmodium falciparum malaria infection (430 +/- 149) than in the controls (158 +/- 21.7, P< 0.01). Fibrinogen levels of 3.40 +/- 0.98 in children with malaria infection were high when compared to 2.21 +/- 0.81 in the controls. The children with malaria infection therefore had a decreased fibrinolytic activity and a proportionately high fibrinogen level. The average packed cell volume of the children with malaria infection was 29.64 +/- 2.13 while in the control it was 36.41 +/- 3.24. The study also showed that 50% of children with malaria had severe anaemia and subsequently had blood transfusions. Twenty percent of those who had transfusions died while being transfused. CONCLUSION: Children who have malaria infection have decreased fibrinolytic activity and proportionately high fibrinogen level which may contribute to the possible thromboembolic process in these children and hence higher risk of mortality from Plasmodium falciparum malaria infection.


Subject(s)
Fibrinolysis/physiology , Malaria, Falciparum/physiopathology , Blood Coagulation Tests , Child, Preschool , Fibrinogen/analysis , Humans , Malaria, Falciparum/blood , Plasminogen Activators/blood , Serum Globulins/analysis , Serum Globulins/physiology
6.
Basic Clin Pharmacol Toxicol ; 96(6): 413-9, 2005 Jun.
Article in English | MEDLINE | ID: mdl-15910404

ABSTRACT

Improvement of endothelial function caused by statin treatment is not related to lowering of the cholesterol levels but results primarily from statin pleiotropic effects. Accordingly, we designed a pilot study in 10 normocholesterolaemic and 10 hypercholesterolaemic patients with peripheral arterial occlusive disease to investigate potential biological effects of statins in relation to their effects on endothelial function. The patients were treated with simvastatin 40 mg/daily for 3 months. Simvastatin led to significant reduction in total cholesterol and trigliceride levels in normocholesterolaemic and hypercholesterolaemic patients. Elongation of pain-free and total walking distance was observed in both groups studied. Inconsiderable changes in rest ankle brachial index were seen. Flow-mediated dilation increased in normocholesterolaemic group by 153% and in the hypercholesterolaemic group by 180% after 3 months of treatment. Euglobulin clot lysis time was shortened significantly in both groups each time after drug intake. Platelet aggregates ratio was increased in normocholesterolaemic patients by 8.9% and in hypercholesterolaemic patients by 17.6% each time after intake and remained significantly increased during the observation after 1 and 3 months. Simvastatin inhibited platelet aggregation induced by collagen and ADP in both study groups 3 hr after intake, but the platelets of hypercholesterolaemic patients were less sensitive to these aggregatory agents after 3 months of treatment. Simvastatin therapy caused clinical improvement in normocholesterolaemic and hypercholesterolaemic patients with peripheral occlusive disease. It is suggested that this effect is due to the restoration of endothelial function.


Subject(s)
Anticholesteremic Agents/therapeutic use , Arterial Occlusive Diseases/drug therapy , Hypercholesterolemia/drug therapy , Simvastatin/therapeutic use , Aged , Ankle/blood supply , Arterial Occlusive Diseases/blood , Blood Coagulation Tests , Blood Pressure/drug effects , Blood Pressure/physiology , Blood Pressure Determination , Brachial Artery/physiology , Cholesterol/blood , Cholesterol, HDL/blood , Cholesterol, LDL/blood , Exercise Test/drug effects , Female , Humans , Hypercholesterolemia/blood , Male , Middle Aged , Platelet Aggregation/drug effects , Serum Globulins/drug effects , Serum Globulins/physiology , Triglycerides/blood
7.
Postgrad Med J ; 80(948): 610-2, 2004 Oct.
Article in English | MEDLINE | ID: mdl-15466998

ABSTRACT

Fibrinolytic activity, using euglobulin lysis time (ELT), was assessed in 46 Nigerians with type 2 diabetes mellitus to study the effect of the disease on fibrinolytic component of haemostasis. There were 20 females and 26 males. Fifty age matched non-diabetics and apparently healthy Nigerians were similarly studied as controls; there were 24 females and 26 males. In the patients, the mean (SD) age of the females was 56.7 (12.0) years and mean (SD) ELT was 276.4 (62.2) min; the mean age of the males was 55.7 (8.5) years and mean ELT was 303.5 (51.5) min. The mean age for female controls was 54.3 (12.6) years and their mean ELT was 198.3 (37.5) min; the mean age of the male controls was 53.4 (11.0) years and mean ELT was 181.6 (39.4) min. There was reduced fibrinolytic activity in diabetic Nigerians as revealed by significantly prolonged ELT in diabetic patients compared with healthy controls. There was good correlation between the blood glucose level and ELT. The observed changes in fibrinolytic activity in this study were not affected by duration of illness. The prolonged ELT in the diabetic population is an additional risk factor for thromboembolic disorders. Fibrinolytic agents may therefore be useful in the management of diabetes mellitus.


Subject(s)
Diabetes Mellitus, Type 2/blood , Fibrinolysis/physiology , Adult , Aged , Aged, 80 and over , Female , Humans , Male , Middle Aged , Nigeria , Serum Globulins/physiology
8.
J Biol Chem ; 277(25): 22453-9, 2002 Jun 21.
Article in English | MEDLINE | ID: mdl-11956209

ABSTRACT

Surfactant protein D (SP-D) and serum conglutinin are closely related members of the collectin family of host defense lectins. Although normally synthesized at different anatomic sites, both proteins participate in the innate immune response to microbial challenge. To discern the roles of specific domains in the function of SP-D in vivo, a fusion protein (SP-D/Cong(neck+CRD)) consisting of the NH(2)-terminal and collagenous domains of rat SP-D (rSP-D) and the neck and carbohydrate recognition domains (CRDs) of bovine conglutinin (Cong) was expressed in the respiratory epithelium of SP-D gene-targeted (SP-D(-/-)) mice. While SP-D/Cong(neck+CRD) fusion protein did not affect lung morphology and surfactant phospholipid levels in the lungs of wild type mice, the chimeric protein substantially corrected the increased lung phospholipids in SP-D(-/-) mice. The SP-D/Cong(neck+CRD) fusion protein also completely corrected defects in influenza A clearance and inhibited the exaggerated inflammatory response that occurs following viral infection. However, the chimeric protein did not ameliorate the ongoing lung inflammation, enhanced metalloproteinase expression, and alveolar destruction that characterize this model of SP-D deficiency. By contrast, a single arm mutant (RrSP-D(Ser15,20)) partially restored antiviral activity but otherwise failed to rescue the deficient phenotype. Our findings directly implicate the CRDs of both SP-D and conglutinin in host defense in vivo. Our findings also strongly suggest that the molecular mechanisms underlying impaired pulmonary host defense and abnormal lipid metabolism are distinct from those that promote ongoing inflammation and the development of emphysema.


Subject(s)
Collectins , Glycoproteins/genetics , Glycoproteins/physiology , Lung/abnormalities , Pulmonary Surfactants/genetics , Pulmonary Surfactants/physiology , Serum Globulins/genetics , Serum Globulins/physiology , Administration, Inhalation , Animals , Blotting, Western , Bronchoalveolar Lavage Fluid/chemistry , Carbohydrate Metabolism , Cattle , Cytokines/biosynthesis , DNA, Complementary/metabolism , Emphysema/metabolism , Enzyme-Linked Immunosorbent Assay , Genetic Vectors , Influenza A virus/genetics , Macrophages, Alveolar/metabolism , Mice , Mice, Transgenic , Models, Genetic , Phosphatidylcholines/metabolism , Phospholipids/metabolism , Protein Binding , Protein Structure, Tertiary , Pulmonary Surfactant-Associated Protein D , Recombinant Fusion Proteins/metabolism
10.
J Vet Intern Med ; 14(5): 475-8, 2000.
Article in English | MEDLINE | ID: mdl-11012107

ABSTRACT

A normal plasma colloid osmotic pressure (COP) interval was established for foals and compared to values for adult horses. Plasma samples were obtained from 38 Thoroughbred foals that had normal findings on postfoaling examination and 10 healthy Thoroughbred adult horses. Samples were analyzed using a commercially available colloid osmometer. Fifty samples were obtained from 38 foals. Twelve foals had 2 samples taken, 1 during the 1st 24 hours of life and the 2nd between 24 and 72 hours of life. For foals with 2 samples, only 1 randomly selected value was used in group analysis. Total plasma protein, albumin, and globulin concentrations were measured on all samples from foals. The mean measured plasma COP for foals was 18.8 +/- 1.9 mm Hg for the 38 samples analyzed. Measured plasma COP did not differ significantly over the time period examined for either the 12 paired samples (P = .13) or with regression analysis of the 38 samples (P = .13). Calculation of mean COP, based on previously published quadratic equations using total protein, albumin, and globulin concentrations, underestimated mean measured foal COP values except for when total protein measured by refractometer was used in the Landis-Pappenheimer equation. In conclusion, the plasma COP interval (95% CI: 15.0 mm Hg, 22.6 mm Hg) obtained for healthy foals in this study was found to be lower than that of healthy adult Thoroughbreds (20.6 +/- 0.7 mm Hg, P = .006).


Subject(s)
Blood Circulation/physiology , Blood Proteins/physiology , Horses/physiology , Animals , Animals, Newborn , Blood Proteins/analysis , Colloids , Female , Fibrinogen/analysis , Linear Models , Male , Osmotic Pressure , Reference Values , Refractometry/veterinary , Regression Analysis , Serum Albumin/analysis , Serum Albumin/physiology , Serum Globulins/analysis , Serum Globulins/physiology , Shock/therapy , Shock/veterinary
12.
Acta Astronaut ; 45(3): 171-6, 1999 Aug.
Article in English | MEDLINE | ID: mdl-11542806

ABSTRACT

The aim of this study was to carry out a comparative study of water balance and water protein composition of the blood during exposure to acute (abrupt restriction of motor activity) and ordinary rigorous bed rest of 7 days. The studies were performed on 30 long distance runners aged 22-25 years old who had a VO2, max of 66 ml kg-1 min-1 on the average. The volunteers were divided into three equal groups: the volunteers in the 1st group were under a normal ambulatory life conditions (control subjects), the volunteers of the 2nd group subjected to an acute bed rest (abrupt restriction of motor activity) regime (acute bed rested subjects) and the volunteers of the 3rd group were submitted to ordinary and rigorous bed rest (rigorous bed rested subjects). All volunteers were on an average of 13.8 km day before taking part in this investigation. The 2nd and 3rd groups of volunteers were kept under a rigorous bed rest regime for 7 days. During the prebed rest period and actual bed rest period plasma volume (PV), total protein and protein fractions (albumins and globulins) and hematocrit were measured. Exposure to acute bed rest conditions induced a significant increase in hematocrit, hemoglobin concentration, protein fractions and marked decrease in (PV) and water balance which were significantly more pronounced than during exposure to ordinary rigorous bed rest. It was concluded that exposure to acute bed rest conditions induces significantly greater changes in water balance and water protein concentration of the blood of endurance trained volunteers than exposure to ordinary rigorous bed rest conditions.


Subject(s)
Bed Rest , Blood Proteins/analysis , Body Water/physiology , Physical Endurance , Adaptation, Physiological , Adult , Body Height , Body Mass Index , Drinking , Hematocrit , Hemoglobins , Humans , Oxygen Consumption , Plasma Volume/physiology , Serum Albumin/physiology , Serum Globulins/physiology , Urine
13.
Immunobiology ; 199(2): 165-89, 1998 Aug.
Article in English | MEDLINE | ID: mdl-9777404

ABSTRACT

The collectins are oligomeric molecules composed of C-type lectin domains attached to collagen regions via alpha-coiled neck regions. Five members of the collectins have been characterized. Mannan-binding lectin (MBL), conglutinin and collectin-43 (CL-43) are serum proteins produced by the liver. Lung surfactant protein A (SP-A) and lung surfactant protein D (SP-D) are mainly found in the lung, where they are synthesized by alveolar type II cells and secreted to the alveolar surface. The collectins are believed to play an important role in innate immunity. They bind oligosaccharides on the surface of a variety of microbial pathogens. After binding of the collectins to the microbial surface effector mechanisms such as agglutination, neutralizing or opsonization of the microorganisms for phagocytosis are initiated. SP-A and SP-D stimulate chemotaxis of phagocytes and once bound to the phagocytes, the production of oxygen radicals can be induced. In the case of MBL the opsonization can be further enhanced by complement activation via the MBLectin pathway while conglutinin interacts with the complement system by binding to the complement degradation product iC3b. A number of receptors and binding molecules interacting with the collectins are found on the membrane or in association with the membrane of various cells responsible for phagocytosis and clearance of microorganisms. This paper focus on the structural aspects of the collectins and the receptors for collectins.


Subject(s)
Carrier Proteins/chemistry , Complement C1q/chemistry , Protein Conformation , Amino Acid Sequence , Animals , Bacteria/immunology , Carbohydrate Sequence , Carrier Proteins/genetics , Carrier Proteins/physiology , Chromosome Mapping , Chromosomes, Human, Pair 10/genetics , Collectins , Complement C1q/physiology , Genes , Glycoproteins/chemistry , Glycoproteins/genetics , Glycoproteins/physiology , Humans , Lectins/chemistry , Lectins/genetics , Lectins/physiology , Models, Molecular , Molecular Sequence Data , Oligosaccharides/metabolism , Opsonin Proteins/immunology , Phagocytosis , Polymorphism, Genetic , Proteolipids/chemistry , Proteolipids/genetics , Proteolipids/physiology , Pulmonary Surfactant-Associated Protein A , Pulmonary Surfactant-Associated Protein D , Pulmonary Surfactant-Associated Proteins , Pulmonary Surfactants/chemistry , Pulmonary Surfactants/genetics , Pulmonary Surfactants/physiology , Rats , Receptors, Cell Surface/physiology , Serum Globulins/chemistry , Serum Globulins/genetics , Serum Globulins/physiology , Species Specificity , Structure-Activity Relationship , Substrate Specificity , Ficolins
14.
Am J Kidney Dis ; 30(6): 822-8, 1997 Dec.
Article in English | MEDLINE | ID: mdl-9398127

ABSTRACT

Human immunodeficiency virus nephropathy (HIVN) continues to challenge nephrologic consultative services at major urban institutions. Although noted in the literature, the decreased incidence of peripheral edema in HIVN has been unexplained to date. In HIV patients, total proteins frequently are found to be elevated due to an elevated globulin fraction. The impact that plasma proteins, specifically globulins, have on the total oncotic pressure has not been reported in HIVN, but may play a role in the paucity of edema noted in this proteinuric population. To evaluate the contributions of serum globulin to the total oncotic pressure and the presence or absence of edema in HIVN, we randomly selected 27 patients with proteinuria greater than 2.5 g/24 hr and serum albumin less than 3.1 g/dL from patients presenting to the nephrology outpatient clinic at the University of Miami/Jackson Memorial Hospital. Seventeen of the patients (63%) had a known diagnosis of HIV infection (group 1). These patients were subdivided into two subgroups: those presenting with clinically evident edema on physical examination (n = 7 [41%]; group 1A) and those who had an absence of edema (n = 10 [59%]; group 1B). Conversely, group 2 comprised 10 patients without known HIV infection, of whom six (60%) had edema (group 2A) and four (40%) did not (group 2B). Blood pressures were noted, and mean arterial pressure was calculated using standard formulas. Serum albumin, serum total proteins, and urine total proteins were measured using standard laboratory methods. Oncotic pressures for albumin (alpha), globulin (beta), and total protein (c) were calculated using the following formula: COPpl = alpha(2.8c + 0.18c2 + 0.012c3) + beta(0.9c + 0.12c2 + 0.004c3). We used Student's t-test to analyze the data. There is no significant difference between the albumin concentrations of HIV patients without edema (group 1B) and non-HIV patients with edema (group 2A), with mean concentrations of 2.3 +/- 0.1 g/dL versus 2.3 +/- 0.15 g/dL, respectively (P = NS). Group 1B, however, has a total oncotic pressure of 17.1 +/- 1.5 mm Hg, whereas both groups with edema (groups 1A and 2A) have statistically significant lower total oncotic pressures (12.1 +/- 2.3 mm Hg and 12.9 +/- 1.1 mm Hg, respectively; P < 0.05). The globulin oncotic pressures may account for some of the differences in total oncotic pressures, being significantly higher for those patients without edema in group 1B compared with group 2A (7.1 +/- 0.9 mm Hg v 3.9 +/- 0.4 mm Hg, respectively; P < 0.05). In patients with HIV, however, the presence or absence of edema is mandated by albumin concentration because both groups have similar globulin concentrations (group 1A 3.1 +/- 0.1 g/dL v group 1B 3.8 +/- 0.3 g/dL; P = NS). Mean arterial pressure does not play a role in edema formation in this study because the HIV patients without edema had the higher blood pressures (group 1B 97.8 +/- 4.7 mm Hg v group 2A 84.7 +/- 5.5 mm Hg; P < 0.05). We conclude that globulins play an important role in maintaining oncotic pressure in low albumin states. HIVN patients with increased serum immune globulin may benefit from higher globulin oncotic pressure, delaying the onset of clinical edema in the setting of proteinuria.


Subject(s)
AIDS-Associated Nephropathy/complications , Edema/etiology , Proteinuria/etiology , Serum Albumin/analysis , AIDS-Associated Nephropathy/blood , AIDS-Associated Nephropathy/urine , Adult , Aged , Blood Pressure , Blood Proteins/analysis , Blood Urea Nitrogen , Creatinine/blood , Edema/physiopathology , HIV Enteropathy/complications , HIV Seronegativity , Humans , Incidence , Middle Aged , Osmotic Pressure , Proteinuria/metabolism , Serum Albumin/physiology , Serum Globulins/analysis , Serum Globulins/physiology
15.
Appl Human Sci ; 15(5): 239-42, 1996 Sep.
Article in English | MEDLINE | ID: mdl-8979405

ABSTRACT

To clarify the stage of fibrinolytic activation by hyperbaric oxygen (HBO) exposure, we examined its alterations in human during and after the HBO exposure. Eight healthy female volunteers breathed oxygen at 284 kPa (2.8 atmospheres absolute). Blood samples were collected before compression, shortly after compression to the pressure 284 kPa, shortly before the start of decompression, shortly after decompression, and then again 3 hours after decompression. We estimated the euglobulin fibrinolytic activity (EFA) and, the activities and antigens of both tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor-1 (PAI-1). The PAI-1 activity and PAI-1 antigen showed significant decrease after compression to a pressure 284 kPa, before the start of decompression, and after decompression. The EFA level and t-PA activity rose significantly shortly after decompression, and 3 hours later returned on baseline. These findings suggest that fibrinolytic activity is elicited after HBO rather than during HBO.


Subject(s)
Fibrinolysis/physiology , Hyperbaric Oxygenation , Adult , Antigens/analysis , Antigens/immunology , Blood Coagulation/physiology , Blood Pressure/physiology , Female , Humans , Plasminogen Activator Inhibitor 1/blood , Plasminogen Activator Inhibitor 1/immunology , Serum Globulins/physiology , Tissue Plasminogen Activator/blood , Tissue Plasminogen Activator/immunology
16.
Biochem J ; 316 ( Pt 1): 43-8, 1996 May 15.
Article in English | MEDLINE | ID: mdl-8645231

ABSTRACT

Conglutinin is a bovine serum protein which was first described as a vertebrate lectin. This protein belongs to the family of C-type lectins. These lectins are composed of four characteristic domains: (1) an N-terminal cysteine-rich domain, (2) a collagen-like domain, (3) a neck domain and (4) a carbohydrate recognition domain (CRD). Recently lectins have been shown to function as immunoglobulin-independent defence molecules due to a complement-mediated mechanism or opsonization. Our previous study showed that bovine conglutinin can inhibit haemagglutination by influenza A viruses and act by directly neutralizing them due to its lectin properties. In order to elucidate the biological role of the collagen-like domain, a recombinant partial conglutinin lacking this collagen-like domain was produced in an Escherichia coli system and its biological activities were examined. A 497 bp sequence, consisting of a short collagen region (two repeats of G-X-Y amino acid sequences), the neck domain, and the CRD of conglutinin cDNA, was amplified by the reverse-transcriptase PCR technique. The cDNA was transferred to a bacterial expression vector system (pRSET-A) and stable transfectants with a high level of conglutinin production were obtained. SDS/PAGE and Western blotting analyses showed a recombinant fusion protein of 27 kDa. Results of a cross-linking study and gel-filtration assay indicated that the recombinant conglutinin can form a trimeric structure and that it has sugar binding activity and specificity similar to that of native conglutinin. The recombinant conglutinin was also found to inhibit haemagglutination caused by influenza A virus as well as to possess less conglutination activity. These results suggest that in order for conglutinin to inhibit haemagglutination caused by the influenza virus, as well as to have sugar binding activity or to form trimers, it does not require the N-terminal and collagenous domains; however, they are essential for full conglutination activity.


Subject(s)
Collectins , Hemagglutination/drug effects , Influenza A virus/immunology , Serum Globulins/chemistry , Serum Globulins/physiology , Amino Acid Sequence , Animals , Base Sequence , Cattle , Collagen/chemistry , Complement Fixation Tests , Cross-Linking Reagents , DNA Primers , Escherichia coli , Lectins , Mannans , Molecular Sequence Data , Polymerase Chain Reaction , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , Recombinant Proteins/pharmacology , Serum Globulins/pharmacology , Sheep
17.
Am J Clin Pathol ; 102(6): 794-6, 1994 Dec.
Article in English | MEDLINE | ID: mdl-7801893

ABSTRACT

Euglobulin lysis time is a global test for the study of fibrinolysis. The aim of this study was to evaluate the influence of storage of plasma and euglobulin precipitates on euglobulin lysis time, by testing samples stored in different conditions. In 20 healthy subjects, euglobulin lysis time was measured by (1) euglobulin precipitates prepared within 90 minutes from blood withdrawal (reference euglobulin lysis time); (2) euglobulin precipitates obtained from platelet-poor plasma stored for 24 hours at either -80 degrees C or at -20 degrees C; (3) euglobulin precipitates frozen for 24 hours at either -80 degrees C or at -20 degrees C; (4) euglobulin precipitates dissolved in Owren's buffer and frozen for 24 hours at either -80 degrees C or at -20 degrees C. Euglobulin lysis time measured on euglobulin precipitates dissolved in Owren's buffer and stored at -20 degrees C and at -80 degrees C, and euglobulin lysis time measured on platelet-poor plasma stored at -20 degrees C were significantly longer than the reference euglobulin lysis time (at least P < .05). On the contrary, no changes were observed in euglobulin lysis time measured on platelet-poor plasma stored at -80 degrees C, and on euglobulin precipitates undissolved and stored at -20 degrees C and at -80 degrees C versus reference euglobulin lysis time. The pattern was similar in samples obtained both before and after venous occlusion. These data indicate that the freezing of samples of platelet-poor plasma or euglobulin precipitates at -80 degrees C and of euglobulin precipitates at -20 degrees C makes the simultaneous determination of a large number of samples collected at different times the previous day possible.


Subject(s)
Blood Preservation , Fibrinolysis , Serum Globulins/physiology , Adult , Female , Humans , Male , Time Factors
18.
Scand J Immunol ; 39(5): 439-45, 1994 May.
Article in English | MEDLINE | ID: mdl-8191219

ABSTRACT

A broad range of plant lectins have recently been shown to inhibit the infectivity of herpes simplex virus type 1 (HSV-1) in vitro. We decided to investigate the role of mammalian lectins in infection with herpes simplex virus. Two lectins, conglutinin and mannan-binding protein (also called mannose-binding protein, MBP), belonging to the collectin family of lectins, were examined. Four week-old BALB/c mice were injected subcutaneously with 100 micrograms bovine conglutinin or 50 micrograms human MBP 1 day before intravenous infection with 5 x 10(4) PFU of herpes simplex virus type 2 (HSV-2). A three-fold increase in virus titre of the liver was observed on day 3 of the infection in the mice pretreated with conglutinin or MBP, whereas no effect was seen on days 1 and 5. In a standard plaque assay using Vero cells we were not able to demonstrate reproducibly either infection inhibition or infection enhancement, when virus was pre-incubated with differing concentrations of the collectins. The concentrations used were similar to those used by us in vivo, and by others in in vitro experiments showing inhibition of the infectivity of HSV-1 with plant lectins. In an ELISA with HSV-2 antigens captured on anti-HSV-2 antibodies, calcium-dependent and carbohydrate inhibitable binding of the collectins was observed. Our results indicate that the effect of endogenous mammalian collectins in vivo may not be neutralization as suggested by the data using plant lectins. Instead, the previously described opsonizing activity of the mammalian collectins may provide the virions with an alternative port of entry into cells leading to infection enhancement.


Subject(s)
Carrier Proteins/physiology , Herpes Simplex/immunology , Herpesvirus 2, Human/immunology , Serum Globulins/physiology , Animals , Carrier Proteins/blood , Cattle , Chlorocebus aethiops , Collectins , Complement C1q/metabolism , Disease Models, Animal , Herpes Simplex/blood , Mice , Mice, Inbred BALB C , Serum Globulins/metabolism , Vero Cells
19.
Clin Physiol ; 14(2): 181-6, 1994 Mar.
Article in English | MEDLINE | ID: mdl-8205749

ABSTRACT

In 12 healthy young men, strenuous cycling exercise in the supine position, caused platelet aggregability to decrease and the ADP threshold to rise from 7.0 microM resting, to 9.5 exercising (P < 0.01). At the same time, fibrinolytic activity increased markedly: euglobulin clot lysis time shortened from 178 to 68 min, PAI-1 fell from 8.91 to 5.16 IU ml-1, and t-PA rose from 0.56 to 3.95 IU ml-1, all three values were significant to P < 0.01. When the erect posture was assumed after lying at ease for 1 h after exercise, it did not increase platelet activity as expected, but caused a modest increase of fibrinolytic activity. These results suggest that supine exercise will not affect the haemostatic system adversely.


Subject(s)
Exercise/physiology , Fibrinolysis/physiology , Platelet Aggregation/physiology , Supine Position/physiology , Adult , Catecholamines/blood , Hemodynamics , Humans , Male , Serotonin/blood , Serum Globulins/physiology
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