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Biomedical subjects

P Venge

Publications and source records attributed to P Venge.

At least 379 records · Page 21Linked to original sources
PubMed1978

The content of eosinophil cationic protein in eosinophil leucocytes. Study on normal controls and patients with bronchial asthma.

Eosinophil cationic protein constitutes a major part of eosinophil leucocyte granule protein. Low serum concentrations have previously been found in patients with bronchial asthma. As this might reflect a low intracellular content, eosinophils were isolated from normal controls and patients with bronchial asthma. Eosinophil cationic protein was estimated after extraction of the cells and a similar content was found in cells from both groups.

Asthma↗
PubMed1978

Serum ferritin during infection. A longitudinal study.

Serum ferritin, transferrin, iron and haptoglobin have been investigated in a longitudinal study in 18 patients hospitalized for various acute infections. Within a couple of days after the onset of an infection, a rise in serum ferritin was seen, the magnitude of which was not dependent on the type of infection (bacterial or viral). The serum ferritin level remained elevated for several weeks in some patients, and 7 out of the 18 patients still had abnormally high values 5 weeks after the onset of illness. The mean curves for serum ferritin and the acute phase reactant haptoglobin were parallel. Possible mechanisms causing the elevation in serum ferritin are discussed.

Acute Disease↗
PubMed1978

Myoglobin turnover--influence of renal and extrarenal factors.

The serum level of myoglobin, an LMW constituent of striated and myocardial muscle, has been studied in various clinical situations in order to obtain information about factors influencing myoglobin turnover. The myoglobin level was significantly correlated to different variables of GFR such as serum beta2-microglobulin, serum creatinine, and 51Cr-EDTA clearance. Following a successful renal transplantation rapid decrease in serum myoglobin was found parallel to increase in GFR's. In patients with advanced long-standing uremia, comparatively small elevations of serum myoglobin were seen when correlated to the degree of GFR reduction, demonstrating an influence of extrarenal factors on the myoglobin levels. The importance of extrarenal factors on the actual serum level of LMW proteins was also illustrated by serial studies on SLE patients receiving corticosteroid therapy. In these patients, elevations of serum myoglobin levels were found, but serum beta2-microglobulin levels gradually decreased during therapy. Finally, calculations based on curves of serum disappearance of myoglobin in patients with acute myocardial infarction indicate that only about 0.3 mg of myoglobin per day is released from the muscle pool during normal conditions, which suggests that myoglobin catabolism mainly occurs within the muscle tissue.

Adolescent↗
PubMed1978

Blood eosinophil leucocyte and eosinophil cationic protein. In vivo study of the influence of beta-2-adrenergic drugs and steroid medication.

The in vivo effect of beta-2-adrenergic stimulating and blocking drugs and of corticosteroid medication on blood eosinophils and serum eosinophil cationic protein (S-ECP) has been studied. The beta-2-adrenergic drugs, salbutamol and terbutaline, had an eosinopenic effect. They were able to decrease S-ECP concentration, which administration of steroid was not, indicating that only the adrenergic stimulators affect leucocyte secretion. Care must be taken in interpretation of blood eosinophil count and S-ECP concentration, and the actual medical treatment must be known.

Adrenal Cortex Hormones↗
PubMed1978

Blood eosinophil leucocytes and eosinophil cationic protein. Diurnal variation in normal subjects and patients with bronchial asthma.

Normal subjects and patients with bronchial asthma showed a similar diurnal variation in blood eosinophil count and serum eosinophil cationic protein concentration. The blood eosinophils showed the highest count during the night whereas serum eosinophil cationic protein showed the highest concentration in the early evening. It is concluded that this may result from a difference in hormonal or other influences.

Adult↗
PubMed1978

Myoglobinemia after myocardial infarction; influence of renal function.

Using a solid-phase radioimmunoassay for detection of serum myoglobin, the pattern of myoglobinemia was investigated in patients with acute myocardial infarction. All patients with acute infarcts had a marked rise in serum myoglobin concentration. Peak serum myoglobin concentration was found on an average 9 h after the initial onset of chest pain. Late onset of myoglobin peaks without signs of reinfarction as well as sustained abnormal myoglobinemia, in the majority of patients, could be explained by impaired renal function. The peak serum level of myoglobin correlated (r = 0.92) to the peak level of ASAT supporting the idea that the detection of myoglobin in serum may be a useful diagnostic aid in the qualitative diagnosis of myocardial infarction.

Aged↗
PubMed1977

Low levels of eosinophil cationic proteins in patients with asthma.

Arginine-rich cationic proteins are a major constituent of the granules of eosinophil leucocytes. In healthy individuals, serum levels of cationic proteins were correlated with blood eosinophil-counts. In asthma patients blood eosinophil-counts were raised but serum cationic-protein levels were lower than expected. Some patients with intrinsic asthma had very low cationic-protein levels despite high eosinophilia. A challenge test in one patient caused a striking decrease in serum cationic proteins but no change in eosinophil-count. Assays of serum "eosinophil" cationic proteins may be useful in the differentiation of atopic and intrinsic asthma and may throw light on pathogenesis.

Arginine↗
PubMed1977

Radioimmunoassay of human eosinophil cationic protein.

A radioimmunosorbent assay has been developed which allows the detection in serum of a cationic protein derived from eosinophil granulocytes. In 34 healthy individuals the mean level was 31 microgram/1. with a range of 5-55 microgram/l. The serum concentration of 'eosinophil' cationic protein was correlated (p less than 0.001) to the number of eosinophil granulocytes in peripheral blood. Quantitation of 'eosinophil' cationic protein in serum might be useful in the study of eosinophil granulocyte turnover and function in vivo.

Blood Proteins↗
PubMed1977

Serum myeloperoxidase and lactoferrin in neutropenia.

Radioimmunosorbent assays for determination of serum content of the neutrophil proteins myeloperoxidase and lactoferrin are described. Serial studies were performed in patients with neutropenia. In 2 cases of cyclic neutropenia the myeloperoxidase level showed slight variations within the normal range during the cycle while lactoferrin displayed a clear correlation with neutrophil counts. In 1 case with persistent agranulocytosis myeloperoxidase was normal but lactoferrin was extremely low. During the regeneration phase of drug-induced neutropenia neutrophil counts and serum lactoferrin increased in a parallel fashion. Since serum myeloperoxidase was normal during profounded neutropenia it is suggested to derive primarily from myeloperoxidase-rich granulopoietic precursor cells of the marrow. Serum lactoferrin on the other hand seems to derive from leakage of more granulopoietic cells of blood and marrow. Studies of neutrophil proteins of serum may aid in evaluation of neutropenic patients.

Adolescent↗
PubMed1977

Myeloperoxidase and lactoferrin of blood neutrophils and plasma in chronic granulocytic leukaemia.

Myeloperoxidase, restricted to primary granules, and lactoferrin, restricted to secondary granules, were determined in plasma and neutrophils of peripheral blood in chronic granulocytic leukaemia (CGL). Plasma myeloperoxidase was increased 2-3 times while plasma lactoferrin increased 2-8 times. This discrepancy indicates different modes of release or elimination. A correlation was found between the leucocyte count and plasma myeloperoxidase or lactoferrin. A correlation was also found between cellular and plasma levels of lactoferrin but not for myeloperoxidase indicating the source for plasma lactoferrin to be circulating leucocytes, which may not be the case for plasma myeloperoxidase. Decreased neutrophil lactoferrin was found in 71% of the CGL cases while myeloperoxidase was decreased in 18%. Serial studies on individual CGL subjects showed low cellular lactoferrin during phases with rapidly expanding leucocytosis indicating defective maturation of neutrophils or abnormal release because of prolonged intravascular life-span.

Adult↗
PubMed1977

Arginine-rich cationic proteins of human eosinophil granules: comparison of the constituents of eosinophilic and neutrophilic leukocytes.

Several arginine-rich cationic proteins previously isolated from granules of leukemic myeloid cells have been found to reside primarily in human eosinophil leukocytes. The major component has a molecular weight of 21,000 and it contains approximately 2.6 moles of zinc per mole of protein. Velocity centrifugation of cytoplasm from leukocytes of patients with marked eosinophilia showed that this group of proteins is packaged in the crystalloid-containing large eosinophil granules. Approximately 30% of the protein content of eosinophil granules belonged to this group of cationic proteins. Bactericidal or esterolytic activities of the cationic proteins were not detected, nor did they inhibit guinea pig anaphylatoxin or histamine-induced contraction. The basic protein previously demonstrated in guinea pig eosinophils may be analogous to the group of basic proteins of human eosinophils but great differences are found for molecular weight and amino acid composition.

Acid Phosphatase↗
PubMed1977

Kinetic studies of phagocytosis of IgG-coated latex particles with a thrombocyte counter.

An assay was developed making possible the measurement of the initial rate of phagocytosis of IgG-coated polyvinyl toluene latex particles by human leukocytes. With the use of the volume-discrimating ability of a Trombo-Counter, the small latex particles could be selectively counted, but cells and internalized particles were not counted. The phagocytic uptake was greatley enhanced by an IgG coating of the particles as compared to the uptake of uncoated or albumin-coated particles. An almost complete inhibition of particle uptake was obtained at ice-bath temperature and in the presence of N-ethyl maleimide. Heat-inactivated serum and monomeric IgG inhibited the phagocytic reaction. In the presence of fresh serum a stimulatory effect on the final phagocytic capacity was noticed, but the initial rate of particle uptake varied depending on the preincubation time of particles with serum.

Blood Cell Count↗
PubMed1975

Cationic proteins of human granulocytes. V. Interaction with plasma protease inhibitors.

Several cationic proteins of human granulocytes possess chymotrypsin-like and bactericidal activities. The heat-labile chymotrypsin-like activity is inhibited by serum, owing to complex formation with alpha2-macroglobulin and alpha1-antitrypsin. The molar affinity of the cationic proteins for alpha2-macroglobulin is much higher than that for alpha1-antitrypsin. The results indicate that the molar combining ratios are 1:1 for cationic protein to alpha1-antitrypsin and 2:1 for cationic protein to alpha2-macroglobulin. The proteolytic activity against fibrinogen and casein is inhibited by both alpha2-macroglobulin and alpha1-antitrypsin, whereas the activity against small molecular synthetic substrates is inhibited by alpha1-antitrypsin but not alpha2-macroglobulin. The heat-stable bactericidal action of the cationic proteins against Staphylococcus was also inhibited by serum, probably owing to complex formation with alpha2-macroglobulin and alpha1-antitrypsin.

Blood Proteins↗
PubMed1975

Cationic proteins of human granulocytes. VI. Effects on the complement system and mediation of chemotactic activity.

The chymotrypsin-like cationic proteins of human granulocytes are shown to possess the ability to produce conversion of the complement components C1s, C4, C3, and C5 as detected by crossed immuno-electrophoresis. This ability seems to be a direct proteolytic effect. Incubation of cationic proteins with serum or functionally pure preparations of C3 and C5 is shown to generate the formation of chemotactic activity which is abolished by prolonged incubation. Also, the chemotactic activity of porcine C5a or spontaneously activated C5 is abolished by incubation with cationic proteins. It is suggested that the chymotrypsin-like cationic proteins of human granulocytes after extrusion from the phagocytic cell play an important role for generation of inflammatory mediators.

Antigen-Antibody Reactions↗
PubMed1975

Cationic proteins of human granulocytes. IV. Esterase activity.

The purfied antibacterial cationic proteins 1 to 7 (component 1 being the most cationic) of human neutrophil granulocytes have been assayed for enzyme activities. Components 1 to 4 and component 7 exhibited activities on tyrosine esters indicating a chymotrypsin-like activity with a neutral pH optimum. The inhibition of the esterase activity by diisopropyl fluorophosphate and phenylmethyl sulfonylfuoride also indicated the similarity to chymotrypsin, with a serine residue in the active center. In addition, the cationic proteins attacked complex substrates like casein and fibrinogen, suggesting a true proteolytic activity. Since the esterase activity of these proteins is heat-labile but the antibacterial activity against Staphylococcus aureus is heat-stable, it is concluded that the chymotrypsin-like activity is not essential for the microbicidal activity. There is evidence to suggest that the cationic proteins of human granulocytes are present in the cytoplasmic granules and exhibit antibacterial activity after release to the phagocytic vacuole and that, after extrusion from the cell, the proteins might be involved in the mediation of the inflammatory process due to enzyme and cationic activities.

Arginine↗