The Induction of Lysosomal Enzyme Release from Leucocytes of Normal and Emphysematous Subjects and the Effects of Cigarette Smoke

1978 ◽  
Vol 54 (2) ◽  
pp. 15P-15P
Author(s):  
R. Desai ◽  
H. Baum ◽  
D. Bellamy ◽  
D. C. S. Hutchison
Keyword(s):  
Cigarette Smoke ◽  
Lysosomal Enzyme ◽  
Enzyme Release

The Induction of Lysosomal Enzyme Release from Leucocytes of Normal and Emphysematous Subjects and the Effects of Tobacco Smoke upon Phagocytosis

1980 ◽  
Vol 58 (5) ◽  
pp. 403-409 ◽  
Author(s):  
D. C. S. Hutchison ◽  
R. Desai ◽  
D. Bellamy ◽  
H. Baum
Keyword(s):  
Cigarette Smoke ◽  
Lysosomal Enzyme ◽  
Lysosomal Enzymes ◽  
Soluble Fraction ◽  
Normal Subjects ◽  
Polymorphonuclear Leucocytes ◽  
Enzyme Release ◽  
Elastic Tissue ◽  
Latex Particles ◽  
Respiratory Inhibitor

1. The lysosomal enzymes of circulating polymorphonuclear leucocytes contain a potent elastase; release of this enzyme within the lung is thought to be responsible for the destruction of elastic tissue in pulmonary emphysema. 2. The release of lysosomal enzymes from blood leucocytes of normal and emphysematous subjects during phagocytosis of particulate material was studied In vitro. Acid phosphatase and acid ribonuclease were used as markers of lysosomal enzyme release, no sufficiently sensitive assay for elastase being available. Cigarette smoke was separated into ‘particulate’ and ‘soluble’ fractions. In a preliminary study, the particulate fraction stimulated enzyme release; in the experiments reported here, latex particles were used to produce this effect. 3. Approximately one-third of the total lysosomal enzyme content was released to the exterior of the cell during phagocytosis of latex particles. In this respect there was no difference between normal and emphysematous subjects. 4. The effects of the non-particulate soluble fraction of cigarette smoke on phagocytosis-induced enzyme release were studied. This fraction inhibited enzyme release from polymorphonuclear leucocytes of normal subjects but not from those of emphysematous patients. When the ‘cigarette-smoke solution’ was replaced by the respiratory inhibitor, antimycin A, a similar inhibition of enzyme release occurred. The inhibition of phagocytosis in cells of normal subjects is presumed to be due to a respiratory inhibitor such as carbon monoxide in the soluble fraction of the smoke. We postulate that the polymorphonuclear leucocytes of emphysematous patients are adapted to hypoxic conditions so that inhibition of enzyme release does not occur.

Spinal Cord Edema, 5-Hydroxytryptamine, Lipid Peroxidation, and Lysosomal Enzyme Release After Acute Contusion and Compression Injury in Primates

1985 ◽  
Vol 2 (1) ◽  
pp. 45-58 ◽  
Author(s):  
JACOB ABRAHAM ◽  
AIYLAM S. BALASUBRAMANIAN ◽  
D.R. THEODORE ◽  
SHANMUGAM NAGARAJAN ◽  
C.A. APTE ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Lipid Peroxidation ◽  
Lysosomal Enzyme ◽  
Enzyme Release ◽  
Compression Injury ◽  
Spinal Cord Edema

scholarly journals Pertussis toxin inhibition of chemotactic factor-induced calcium mobilization and function in human polymorphonuclear leukocytes.

1985 ◽  
Vol 162 (1) ◽  
pp. 145-156 ◽  
Author(s):  
D W Goldman ◽  
F H Chang ◽  
L A Gifford ◽  
E J Goetzl ◽  
H R Bourne
Keyword(s):  
Pertussis Toxin ◽  
Lysosomal Enzyme ◽  
Polymorphonuclear Leukocytes ◽  
Regulatory Protein ◽  
Leukotriene B4 ◽  
Ionophore A23187 ◽  
Enzyme Release ◽  
Adp Ribosylation ◽  
Chemotactic Factors ◽  
Human Polymorphonuclear Leukocytes

Chemotactic factors stimulate a rapid increase in the cytosolic concentration of intracellular calcium ions ([Ca2+]in) in human polymorphonuclear leukocytes (PMNL), which may be an event that is critical to the expression of chemotaxis and other PMNL functions. Treatment of PMNL with pertussis toxin catalyzes ADP-ribosylation of a protein similar or identical to the inhibiting regulatory protein of adenylate cyclase, Gi, and suppresses the increase in [Ca2+]in elicited by leukotriene B4(LTB4) and formyl-methionyl-leucyl-phenylalanine. Chemotactic migration and lysosomal enzyme release elicited by chemotactic factors were inhibited by pertussis toxin with a concentration-dependence similar to that for inhibition of the increase in [Ca2+]in, without an effect on lysosomal enzyme release induced by the ionophore A23187 and phorbol myristate acetate. Activated pertussis toxin catalyzed the [32P]ADP-ribosylation of a 41 kD protein in homogenates of PMNL. The extent of [32P]ADP-ribosylation of this protein was reduced 59% by pretreatment of intact PMNL with pertussis toxin. Pertussis toxin selectively decreased the number of high-affinity receptors for LTB4 on PMNL by 60% without altering the number or binding properties of the low-affinity subset of receptors. Pertussis toxin modification of a membrane protein of PMNL analogous to Gi thus simultaneously alters chemotactic receptors and attenuates the changes in cytosolic calcium concentration and PMNL function caused by chemotactic factors.

Lung injury and lung lysosomal enzyme release during endotoxemia

1981 ◽  
Vol 30 (2) ◽  
pp. 135-141 ◽  
Author(s):  
Robert H. Demling ◽  
Richard Proctor ◽  
Jeffrey Grossman ◽  
Nguyen Duy ◽  
James Starling
Keyword(s):  
Lung Injury ◽  
Lysosomal Enzyme ◽  
Enzyme Release

Stobadine inhibits lysosomal enzyme release in vivo and in vitro

Life Sciences ◽  
1999 ◽  
Vol 65 (18-19) ◽  
pp. 1905-1907 ◽  
Author(s):  
Jana Navarová ◽  
Tatiana Mačičková ◽  
Katarina Horáková ◽  
Miroslava Urbančíková
Keyword(s):  
Lysosomal Enzyme ◽  
Enzyme Release

scholarly journals Monoclonal antibody AHN-1 inhibits phagocytosis by human neutrophils

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 333-339
Author(s):  
KM Skubitz ◽  
DJ Weisdorf ◽  
PK Peterson
Keyword(s):  
Monoclonal Antibody ◽  
Lysosomal Enzyme ◽  
Surface Proteins ◽  
Superoxide Production ◽  
Human Neutrophils ◽  
Enzyme Release ◽  
Specific Monoclonal Antibody ◽  
Normal Human ◽  
Major Surface

The granulocyte-specific monoclonal antibody, AHN-1, immunoprecipitates two major surface-iodinated proteins of 105,000 and 145,000 to 150,000 daltons from normal human neutrophils. In this study, the effect of AHN- 1 on a number of neutrophil functions was evaluated in vitro. Both complement- and antibody-mediated phagocytosis were inhibited when human neutrophils were pretreated with AHN-1 and opsonized bacteria were used as targets. The inhibition of phagocytosis was specific, in that lysosomal enzyme release and chemotaxis were not altered by treatment with AHN-1. AHN-1 did inhibit superoxide production by neutrophils in response to particulate stimuli, but not in response to the soluble stimulus, 12-O-tetradecanoylphorbol-13-acetate. The data indicate that one or both of these surface proteins may be important in the process of phagocytosis. AHN-1 should be useful in isolating and further characterizing the nature of these molecules.

Slowed lysosomal enzyme release and its normalization by drugs in adjuvant-induced polyarthritis

1971 ◽  
Vol 20 (10) ◽  
pp. 2821-2824 ◽  
Author(s):  
N.H. Grant ◽  
M.E. Rosenthale ◽  
H.E. Alburn ◽  
A.C. Singer
Keyword(s):  
Lysosomal Enzyme ◽  
Enzyme Release

scholarly journals Bradykinin stimulates bone resorption and lysosomal-enzyme release in cultured mouse calvaria

1984 ◽  
Vol 219 (1) ◽  
pp. 329-332 ◽  
Author(s):  
G T Gustafson ◽  
U Lerner
Keyword(s):  
Bone Resorption ◽  
Bone Tissue ◽  
Lysosomal Enzyme ◽  
Enzyme Release ◽  
Newborn Mouse ◽  
Mouse Calvaria ◽  
Stable Calcium

The effect of bradykinin on bone resorption was studied in cultures of newborn-mouse calvaria. Bradykinin (0.03 microM, 1 microM) stimulated the release of 45Ca2+ from bones dissected out from mice prelabelled in vivo with 45Ca. Bradykinin (1 microM) also augmented the release of stable calcium (40Ca), Pi and the lysosomal enzyme beta-glucuronidase. The stimulatory effect of bradykinin on mineral mobilization and lysosmal -enzyme release could be blocked by indomethacin. It is speculated that concomitant generation of thrombin and bradykinin in areas of trauma and inflammation may induce resorption of nearby bone tissue.

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