Biocompatibility assessment of type-II collagen and its polypeptide for tissue engineering: effect of collagen's molecular weight and glycoprotein content on tumor necrosis factor (Fas/Apo-1) receptor activation in human acute T-lymphocyte leukemia cell line

RSC Advances ◽  
2016 ◽  
Vol 6 (17) ◽  
pp. 14236-14246 ◽  
Author(s):  
E. Jeevithan ◽  
Z. Jingyi ◽  
B. Bao ◽  
W. Shujun ◽  
R. JeyaShakila ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Leukemia Cell ◽  
Death Receptor ◽  
Type Ii Collagen ◽  
Receptor Activation ◽  
Leukemia Cell Line ◽  
Low Molecular Weight ◽  
Type Ii ◽  
Line P ◽  
Necrosis Factor

Fas cell surface death receptor activation by low molecular weight (57, 40 and 25 kDa) collagens was investigated based on MW and glycoprotein content.

scholarly journals Shiga Toxin 1 Induces Apoptosis in the Human Myelogenous Leukemia Cell Line THP-1 by a Caspase-8-Dependent, Tumor Necrosis Factor Receptor-Independent Mechanism

2005 ◽  
Vol 73 (8) ◽  
pp. 5115-5126 ◽  
Author(s):  
Sang-Yun Lee ◽  
Rama P. Cherla ◽  
Isa Caliskan ◽  
Vernon L. Tesh
Keyword(s):  
Tumor Necrosis ◽  
Leukemia Cell ◽  
Death Receptor ◽  
Myelogenous Leukemia ◽  
Leukemia Cell Line ◽  
Caspase 8 ◽  
Independent Mechanism ◽  
Caspase 6 ◽  
Induced Apoptosis ◽  
Necrosis Factor

ABSTRACT Shiga toxins (Stxs) induce apoptosis in a variety of cell types. Here, we show that Stx1 induces apoptosis in the undifferentiated myelogenous leukemia cell line THP-1 in the absence of tumor necrosis factor alpha (TNF-α) or death receptor (TNF receptor or Fas) expression. Caspase-8 and -3 inhibitors blocked, and caspase-6 and -9 inhibitors partially blocked, Stx1-induced apoptosis. Stx1 induced the mitochondrial pathway of apoptosis, as activation of caspase-8 triggered the (i) cleavage of Bid, (ii) disruption of mitochondrial membrane potential, and (iii) release of cytochrome c into the cytoplasm. Caspase-8, -9, and -3 cleavage and functional activities began 4 h after toxin exposure and peaked after 8 h of treatment. Caspase-6 may also contribute to Stx1-induced apoptosis by directly acting on caspase-8. It appears that functional Stx1 holotoxins must be transported to the endoplasmic reticulum to initiate apoptotic signaling through the ribotoxic stress response. These data suggest that Stxs may activate monocyte apoptosis via a novel caspase-8-dependent, death receptor-independent mechanism.

scholarly journals Effects of Low Molecular Weight Chondroitin Sulfate on Type II Collagen-Induced Arthritis in DBA/1J Mice

2004 ◽  
Vol 27 (1) ◽  
pp. 47-51 ◽  
Author(s):  
So Yean Cho ◽  
Joon-Soo Sim ◽  
Choon Sik Jeong ◽  
Seung Yeup Chang ◽  
Don Woong Choi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Chondroitin Sulfate ◽  
Type Ii Collagen ◽  
Low Molecular Weight ◽  
Type Ii ◽  
Collagen Induced Arthritis

scholarly journals Synthesis of a low molecular weight collagen by chondrocytes from the presumptive calcification region of the embryonic chick sterna: the influence of culture with collagen gels.

1984 ◽  
Vol 99 (1) ◽  
pp. 208-216 ◽  
Author(s):  
G J Gibson ◽  
B W Beaumont ◽  
M H Flint
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Collagen Synthesis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Morphological Features ◽  
Low Molecular Weight ◽  
Type Ii ◽  
Embryonic Chick ◽  
Collagen Gels ◽  
Discrete Populations

The mature chick sternum is divisible almost equally into cephalic calcified and caudal cartilagenous regions. Isolation and culture of cells derived from embryonic precursors of these regions has revealed two discrete populations of cells with distinct morphological features and synthetic capabilities. Both cell populations grew well in culture within or upon collagen gels or upon plastic and maintained morphologies similar to those observed in the parent tissue. Polyacrylamide gel electrophoresis of radiolabeled proteins synthesized by the cells in culture demonstrated large differences in the types of collagens synthesized. Both chondrocyte populations synthesized type II and minor cartilage collagens but only chondrocytes isolated from the presumptive calcification region synthesized the previously identified, low molecular weight collagen, termed G collagen. Synthesis of G collagen was stimulated by culture within or upon collagen gels such that it represented an average of 65% of the total collagen synthesized by presumptive calcification region chondrocytes after 7 d of culture within collagen gels. Light and scanning electron microscopy demonstrated that the two chondrocyte types exhibited distinct morphological features and accumulated different extracellular matrices in culture.

scholarly journals Tumor necrosis factor induces tissue factor-like activity in human leukemia cell line U937 and peripheral blood monocytes

Blood ◽  
1988 ◽  
Vol 72 (1) ◽  
pp. 128-133 ◽  
Author(s):  
PR Conkling ◽  
CS Greenberg ◽  
JB Weinberg
Keyword(s):  
Tumor Necrosis Factor ◽  
Tissue Factor ◽  
Tumor Necrosis ◽  
Leukemia Cell ◽  
Time Dependent ◽  
Leukemia Cell Line ◽  
U937 Cells ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Necrosis Factor

Abstract The induction of procoagulant activity (PCA) by human recombinant tumor necrosis factor (rTNF) was studied in human monoblastic leukemia cell line U937 and human peripheral blood monocytes. Using a one-step recalcificating clotting assay, PCA in cell lysates or whole cell preparations was measured by comparison to a rabbit brain thromboplastin standard. There was a dose- and time-dependent increase in PCA when U937 cells were cultured with rTNF. The effect of rTNF was not enhanced by recombinant human interferon-gamma (rIFN gamma). Cycloheximide inhibited the expression of PCA by U937 cells, showing that protein synthesis was necessary to mediate the effects of rTNF. Whole cell preparations demonstrated that greater than 80% of the PCA was expressed on the surface of the cells. The PCA functioned as a tissue factor-like substance, since it required coagulation factor VII and factor X. rTNF also increased PCA in human monocytes in a dose- and time-dependent manner. This effect was abrogated by boiling the rTNF for ten minutes, and was not inhibited by adding polymyxin-B to the cultures, making it unlikely that endotoxin accounted for the observed effects. These results suggest that TNF-induced expression of tissue factor by mononuclear phagocytes may modulate immunologic, inflammatory, and hemostatic processes.

scholarly journals The C-terminal Tails of Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) and Fas Receptors Have Opposing Functions in Fas-associated Death Domain (FADD) Recruitment and Can Regulate Agonist-specific Mechanisms of Receptor Activation

2004 ◽  
Vol 279 (50) ◽  
pp. 52479-52486 ◽  
Author(s):  
Lance R. Thomas ◽  
Ronald L. Johnson ◽  
John C. Reed ◽  
Andrew Thorburn
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Molecular Mechanisms ◽  
Death Receptor ◽  
Receptor Activation ◽  
Death Domain ◽  
Absolute Requirement ◽  
Trail Receptors ◽  
Domain Interactions ◽  
Necrosis Factor

Members of the tumor necrosis factor (TNF) superfamily of receptors such as Fas/CD95 and the TNF-related apoptosis-inducing ligand (TRAIL) receptors DR4 and DR5 induce apoptosis by recruiting adaptor molecules and caspases. The central adaptor molecule for these receptors is a death domain-containing protein, FADD, which binds to the activated receptor via death domain-death domain interactions. Here, we show that in addition to the death domain, the C-terminal tails of DR4 and DR5 positively regulate FADD binding, caspase activation and apoptosis. In contrast, the corresponding region in the Fas receptor has the opposite effect and inhibits binding to the receptor death domain. Replacement of wild-type or mutant DR5 molecules into DR5-deficient BJAB cells indicates that some agonistic antibodies display an absolute requirement for the C-terminal tail for FADD binding and signaling while other antibodies can function in the absence of this mechanism. These data demonstrate that regions outside the death domains of DR4 and DR5 have opposite effects to that of Fas in regulating FADD recruitment and show that different death receptor agonists can use distinct molecular mechanisms to activate signaling from the same receptor.

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