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Biomedical subjects

I Olsson

Publications and source records attributed to I Olsson.

At least 163 records · Page 9Linked to original sources
PubMed1978

Neutrophil and eosinophil granulocytes in bacterial infection: sequential studies of cellular and serum levels of granule proteins.

The intraneutrophilic concentrations of lactoferrin, myeloperoxidase, collagenase and chymotrypsin-like cationic proteins were measured sequentially during acute bacterial infection. The serum levels of lactoferrin and myeloperoxidase were also followed as well as the 'eosinophil' cationic protein as a marker for eosinophil leucocytes. During the early course of infection there was a profound but reversible decrease of intraneutrophilic lactoferrin. The levels of cellular collagenase and chymotrypsin-like cationic proteins also tended to decrease reversibly during day 2-8 in most cases; myeloperoxidase levels were normal except for two cases. Serum myeloperoxidase and lactoferrin correlated with blood neutrophil counts. In spite of the absence of peripheral eosinophils the 'eosinophil' cationic proteins of serum were increased on the first day of infection, which may reflect increased eosinophil turnover.

Bacterial Infections↗
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

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↗
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

Purification of human granulocyte catalase in chronic myeloid leukemia.

Human granulocyte catalase (hydrogen peroxide:hydrogen peroxide oxidoreductase, EC 1.11.1.6) was purified from chronic myeloid leukemia cells. The purification procedure included heat precipitation, ammonium sulphate fractionation, DEAE-Sephadex chromatography, gel chromatography on Sephadex G-200 and isoelectric focusing with an approximate yield of 30% and a 1000-fold purification. The molecular weight of the subunit obtained by sodium dodecyl sulphate electrophoresis was 65 800. So20,w was 11.6 +/- 0.24. The pH-optimum was 6.6-6.7 and the spectrum showed a major peak at 405 nm and shoulders at 500, 540 and 625 nm typical for catalase. The electrophoretic mobility was towards the anode at pH 8.6 and identical to normal granulocyte and erythrocyte catalase. These three species of catalase gave the reaction of identity on immunodiffusion and crossed immunoelectrophoresis. The content of catalase and its activity of isolated granulocytes were approximately identical in normal and chronic myeloid leukemia granulocytes while the specific activity of leukemic catalase was higher than normal. No difference in catalase content was found between mature and immature leukemic granulocytes.

Catalase↗
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

Acute myeloid leukaemia with the Philadelphia chromosome.

A case report of serial chromosome studies on a 26-year-old male with acute myeloid leukaemia (AML) is presented. The classic Philadelphia chromosome (Ph1) translocation, t (9;22) was found in 77% of the metaphases at diagnosis and in 100% in relapse; during a 3-month remission period the cytogenetic picture was normal or the Ph1 was present in a minor cell population only. The clinical and morphologic features of this case indicated that it was really a case of AML and less likely chronic myeloid leukaemia (CML) presenting in blast crisis. It is suggested that the oncogen producing the 9;22-translocation and CML may also induce AML in rare instances.

Adult↗
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

The extracellular release of granulocyte collagenase and elastase during phagocytosis and inflammatory processes.

Human granulocytes release 25-30% of the granular neutral proteases, collagenase and elastase, to the exterior of the cell during phagocytosis of yeast cells or immune complexes. Similar amounts of myeloperoxidase and lactoferrin are released. Crossed immunoelectrophoresis demonstrated that collagenase and elastase released extracellularly formed complexes with serum alpha1-antitrypsin. The presence of alpha1-antitrypsin complexes with granulocyte collagenase and elastase were also demonstrated in inflammatory processes, e.g. in the peritoneal exudate of acute peritonitis. The reactivity of neutrophil proteases with natural plasma protease inhibitors must be considered in assessing the role of these proteases as the etiologic agent of tissue damage and degradation during the inflammatory process.

Acute Disease↗
PubMed1977

Localization of chymotrypsin-like cationic protein, collagenase and elastase in azurophil granules of human neutrophilic polymorphonuclear leukocytes.

The subcellular localization of granulocyte collagenase, elastase and chymotrypsin-like cationic protein was determined using velocity centrifugation of cytoplasmic granules of human polymorphonuclear leukocytes. The proteases were assayed by immunochemical and enzymatic methods. Measurements of lactoferrin and myeloperoxidase distinguish exactly between constituents of specific and azurophil granules. Collagenase, elastase and chymotrypsin-like cationic proteins showed an almost identical sharp and unimodal distribution. They co-sedimented with myeloperoxidase demonstrating that these enzymes are localized exclusively in the azurophil granules.

Adult↗
PubMed1977

Elastases from human and canine granulocytes, II. Interaction with protease inhibitors of animal, plant, and microbial origin.

Inhibitors of animal, plant, and microbial origin were tested against human and canine granulocytic elastases. The trypsin-chymotrypsin inhibitors from dog submandibular glands, from soybeans (Bowman-Birk) and from chickpeas show strong interaction with these proteases (Ki = 10(-8) - 10(-9)M). The trypsin-kallikrein inactivator of bovine organs (Trasylol) is not active against granulocytic elastases or against human granulocytic cathepsin G. Elastatinal, a specific inhibitor of elastases, isolated from actinomycetes (Streptomyces griseoruber), forms stable complexes with elastase from human (Ki = 6.2 X 10(-6)M) and canine granulocytes (Ki = 1.1 X 10(-6)M). A possible therapeutic application of these inhibitors for the inactivation of granulocytic proteases, which are able to degrade connective tissue in different pathological states, is discussed.

Animals↗
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

Neutral proteases of human granulocytes. IV. Interaction between human granulocyte collagenase and plasma protease inhibitors.

Purified human granulocyte collagenase was inactivated by serum through the formation of complexes with alpha 1-antitrypsin and alpha 2-macroglobulin. A molar combining ratio of 1:1 was observed for each inhibitor. The affinity of alpha 2-macroglobulin was about 10 times that of alpha 1-antitrypsin for granulocyte collagenase. The molar concentration of alpha 1-antitrypsin in the blood exceeds that of alpha 2-macroglobulin by about 12 times, so that the inhibitors may be equally important for defence against granulocyte collagenase.

Granulocytes↗
PubMed1976

Immobilization of enzymes based on hydrophobic interaction. III. Adsorbent substituent density and its impact on the immobilization of beta-amylase.

Hexyl-groups have been introduced into crosslinked Sepharose 6B, yielding gels with degrees of substitution which range from 0.02 to 0.70 mol hexyl-side chain per mole galactose residue. The gels were exposed to beta-amylase in solution, and the resulting adsorbates indicated a monotonic increase in adsorption capacity with an increasing hexyl-content. Adsorbate activity, by contrast, displayed a maximum for a carrier gel with a hexyl-galactose ratio of 0.51. Adsorbates based on gels with different hexyl-content were used in column reactors for continuous maltose production from a soluble starch substrate.

Adsorption↗