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

Experimental Spinal Cord Injury: Spatiotemporal Characterization of Elemental Concentrations and Water Contents in Axons and Neuroglia

1999 ◽  
Vol 82 (5) ◽  
pp. 2143-2153 ◽  
Author(s):  
Richard M. LoPachin ◽  
Christopher L. Gaughan ◽  
Ellen J. Lehning ◽  
Yoshiro Kaneko ◽  
Thomas M. Kelly ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Spinal Cord Injury ◽  
Water Content ◽  
Severely Injured ◽  
Channel Blockade ◽  
Compression Injury ◽  
Ion Distribution ◽  
Elemental Concentrations ◽  
Cord Injury ◽  
Spinal Segments

To examine the role of axonal ion deregulation in acute spinal cord injury (SCI), white matter strips from guinea pig spinal cord were incubated in vitro and were subjected to graded focal compression injury. At several postinjury times, spinal segments were removed from incubation and rapidly frozen. X-ray microanalysis was used to measure percent water and dry weight elemental concentrations (mmol/kg) of Na, P, Cl, K, Ca, and Mg in selected morphological compartments of myelinated axons and neuroglia from spinal cord cryosections. As an index of axon function, compound action potentials (CAP) were measured before compression and at several times thereafter. Axons and mitochondria in epicenter of severely compressed spinal segments exhibited early (5 min) increases in mean Na and decreases in K and Mg concentrations. These elemental changes were correlated to a significant reduction in CAP amplitude. At later postcompression times (15 and 60 min), elemental changes progressed and were accompanied by alterations in compartmental water content and increases in mean Ca. Swollen axons were evident at all postinjury times and were characterized by marked element and water deregulation. Neuroglia and myelin in severely injured epicenter also exhibited significant disruptions. In shoulder areas (adjacent to epicenter) of severely injured spinal strips, axons and mitochondria exhibited modest increases in mean Na in conjunction with decreases in K, Mg, and water content. Following moderate compression injury to spinal strips, epicenter axons exhibited early (10 min postinjury) element and water deregulation that eventually recovered to near control values (60 min postinjury). Na+ channel blockade by tetrodotoxin (TTX, 1 μM) perfusion initiated 5 min after severe crush diminished both K loss and the accumulation of Na, Cl, and Ca in epicenter axons and neuroglia, whereas in shoulder regions TTX perfusion completely prevented subcellular elemental deregulation. TTX perfusion also reduced Na entry in swollen axons but did not affect K loss or Ca gain. Thus graded compression injury of spinal cord produced subcellular elemental deregulation in axons and neuroglia that correlated with the onset of impaired electrophysiological function and neuropathological alterations. This suggests that the mechanism of acute SCI-induced structural and functional deficits are mediated by disruption of subcellular ion distribution. The ability of TTX to reduce elemental deregulation in compression-injured axons and neuroglia implicates a significant pathophysiological role for Na+ influx in SCI and suggests Na+ channel blockade as a pharmacotherapeutic strategy.

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

Effects of α-Phenyl-N-tert-butyl Nitrone (PBN) on Compression Injury of Rat Spinal Cord

1997 ◽  
Vol 27 (2) ◽  
pp. 187-196 ◽  
Author(s):  
Gw Lin Li ◽  
Mohammad Farooque ◽  
Anders Holtz ◽  
Yngve Olson
Keyword(s):  
Spinal Cord ◽  
Rat Spinal Cord ◽  
Compression Injury ◽  
Tert Butyl

Lipid Peroxidation in Late Radiation Injury of the Rat Spinal Cord

1991 ◽  
pp. 165-171
Author(s):  
K. J. Levin ◽  
P. H. Gutin ◽  
M. W. Mcdermott ◽  
G. Y. Ross ◽  
N. Hooper ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Lipid Peroxidation ◽  
Radiation Injury ◽  
Rat Spinal Cord

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.

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