Distribution Patterns of Proteolytic Enzymes in Normal and Leukaemic Human Leucocytes

Haschen, Reinhard J.; Krug, Karl

doi:10.1038/209511a0

Cited by 26 publications

(9 citation statements)

References 10 publications

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“…The spontaneous fibrinolytic activity at pH 7.65 might be due to the socalled alkaline protease which has been demonstrated by several authors (e.g. Haschen et al 1966). It is known that alkaline protease is partly inhibited by STBI (Mounter et al 1960), which we also found.…”

Section: Discussionsupporting

confidence: 82%

“…Both fibrinolysis and intravascular coagulation have been suggested as possible causes for bleeding. Haschen et al (1966) and Young et al (1962) found an increase of alkaline protease of leucocytes in various types of leukaemia, whereas the acid protease was not significantly changed. Also, Rosenthal (1963) and Cattan et al (1966) found that plasma fibrinolytic activity in leukaemia was related to the morphological picture.…”

Section: Discussionmentioning

confidence: 93%

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Fibrinolytic Activity of Leucocytes in Smears of Bone Marrow and Peripheral Blood

Prokopowicz¹,

Stormorken²

1968

Scandinavian Journal of Haematology

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A cytochemical method for studying fibrinolytic (proteolytic) activity in specified white cells in blood and bone marrow smears has been developed and the spontaneous fibrinolytic activity at pH 6.0 and 7.65 as well as the activity of a plasminogen‐like proenzyme were studied. These fibrinolytic enzymes appeared in the granulocytic and monocytic series; their activity depending upon the maturation stage. The enzymes appear in promyelocytes, reach the highest activity in metamyelocytes and in band cells and then gradually decrease during maturation. No significant differences between mature neutrophils, eosinophils and basophils were observed. Megakaryocytes, erythroblasts, erythrocytes and lymphocytes were devoid of significant fibrinolytic activity. Some implications of these findings are discussed.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 93%

Fibrinolytic Activity of Leucocytes in Smears of Bone Marrow and Peripheral Blood

Prokopowicz¹,

Stormorken²

1968

Scandinavian Journal of Haematology

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“…Moreover, the weak solubility in vitro and the neutral pH optimum of the receptor-modifying activity and its suppression by ax-antitrypsin and other natural protease inhibitors agree completely with the present information on the properties of neutral PMN proteases in man. In fact, protease activity which is characterized by these criteria was found in human PMNs by many investigators, and various proteolytic and esteroproteolytic specificities which are associated with it are already known [5,7,9,11].…”

Section: Discussionmentioning

confidence: 99%

Antigenic Alteration of Red Cell Surfaces Exposed to Enzymatic Actions of Autologous Polymorphonuclear Leukocytes

Arend¹,

Malchow²

1974

Vox Sanguinis

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Isolated polymorphonuclear leukocytes induce alterations of the antigen receptor mosaic of autologous red cell surfaces in vitro. Such alterations are represented by decreased expression or loss of MN receptors and the ‘appearance’ of HLe^b- and Le^a-like receptor activities, which can be demonstrated by means of reactions of leukocyteexposed erythrocytes with anti-H lectins and heterologous anti-Le sera and by specific inhibition of these reactions. Since the receptor changes observed were most pronounced on the surfaces of secretar erythrocytes and since demonstrable Lewis-type modifications could not be created on erythrocytes of nonsecretors in these investigations, the antigenic polymorphism unmasked by contact of red cells with polymorphonuclear leukocytes was genetically limited to some extent. These limitations are perhaps due to restricted antigenic variability of the nonsecretor erythrocyte membrane components. The receptormodifying activity is confined to particle fractions of polymorphonuclear leukocytes; it is thermostable up to 70 °C, destroyed at 80 °C, blocked by α(1)-antitrypsin and other natural protease inhibitors, and reaches its peak at physiological pH values between 7.2 and 7.4. These properties correspond with those of the particulate neutral protease of human polymorphonuclear leukocytes. However, glycosidases probably also play a role.

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“…Lysozyme mucopeptide N-acetylmuramylhydrolase Rabbit [1,17,18], horse [53], human [43,48,50,51] probably hydrolyzes ß-1,4-links between N-acetylmuramic acid and 2-acetamido-2-deoxy-D-glucose residues in a mucopolysaccharide or mucopeptide Rabbit [17], human [44,113] Active on synthetic substrates [17,44,113], but not on lactose [113]. w Rabbit [1,17,18,106], human [43][44][45][46][47][48][49][50][51], cattle [107], horse [53], rat [111] Rabbit [1,[120][121][122], human [126][127][128] hydrolyzes peptides. Its specificity is somewhat similar to that of pepsin ( …”

Section: Lysozymementioning

confidence: 99%

“…o Neutral proteinase Rabbit [115,125], human [116,[126][127][128][129][130] hydrolyzes peptides [136], This enzyme, which has a pH optimum of 8.5, clearly differs from pancreatic elastase in its sensitivity to inhibitors and still has strong elastolytic activity in weak acid media [134], Following partial purification, PMN elastase showed hydrolytic activity in vitro against pre parations of basement membrane and cartilage [133][134][135], and readily pro duced local hemorrhagic reactions in vivo [134].…”

mentioning

confidence: 99%

The Enzymes of the Granules of Polymorphonuclear Leukocytes and Their Functions

Baggiolini¹

1972

Enzyme

100

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Polymorphonuclear leukocytes from the rabbit are known to possess two types of granules - azurophils containing lysosomal hydrolases together with myeloperoxidase and other microbicidal agents, and specifics containing alkaline phosphatase, lysozyme and lactoferrin but lacking common lysosomal enzymes. The presently available data strongly suggest that a comparable situation is encountered in polymorphonuclear leukocytes of other species including man. The known leukocyte granule enzymes are listed together with their properties, and their possible functions are also described.

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Distribution Patterns of Proteolytic Enzymes in Normal and Leukaemic Human Leucocytes

Cited by 26 publications

References 10 publications

Fibrinolytic Activity of Leucocytes in Smears of Bone Marrow and Peripheral Blood

Fibrinolytic Activity of Leucocytes in Smears of Bone Marrow and Peripheral Blood

Antigenic Alteration of Red Cell Surfaces Exposed to Enzymatic Actions of Autologous Polymorphonuclear Leukocytes

The Enzymes of the Granules of Polymorphonuclear Leukocytes and Their Functions

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