Oxidative dissociation of human alpha 2-macroglobulin tetramers into dysfunctional dimers.

Reddy, Vidyavathi; Desorchers, P E; Pizzo, Salvatore V.; Gonias, S L; Sahakian, Julie A.; Levine, Rodney L.; Weiss, Stephen J.

doi:10.1016/s0021-9258(17)41830-8

Cited by 104 publications

(22 citation statements)

References 66 publications

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“…␣ 2 -Macroglobulin Capture Assay [ 35 S]Methionine-labeled ST3-N was generated through in vitro translation as above and used in the ␣ 2 -macroglobulin ( ␣ 2 M) capture assay as described (Reddy et al, 1994;Pei et al, 1994). 1 l of the in vitro translation product was mixed with 5 l of the reaction buffer (150 mM NaCl, 1 mM CaCl 2 , 1 mM MgCl 2 , 0.1 mM ZnCl 2 , 20 mM Tris-HCl, pH 6.8) and 2 l PBS containing the indicated amount of anti-ST3 or preimmune serum to reach the final concentration of 0-1%.…”

Section: Generation Of Antibody Against St3 Catalytic Domain and Western Blot Analysismentioning

confidence: 99%

Requirement for Matrix Metalloproteinase Stromelysin-3 in Cell Migration and Apoptosis during Tissue Remodeling in Xenopus laevis

Ishizuya‐Oka

Amano

et al. 2000

The Journal of Cell Biology

112

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The matrix metalloproteinase (MMP) stromelysin-3 (ST3) was originally discovered as a gene whose expression was associated with human breast cancer carcinomas and with apoptosis during organogenesis and tissue remodeling. It has been shown previously, in our studies as well as those by others, that ST3 mRNA is highly upregulated during apoptotic tissue remodeling during Xenopus laevis metamorphosis. Using a function-blocking antibody against the catalytic domain of Xenopus ST3, we demonstrate here that ST3 protein is specifically expressed in the cells adjacent to the remodeling extracellular matrix (ECM) that lies beneath the apoptotic larval intestinal epithelium in X. laevis in vivo, and during thyroid hormone–induced intestinal remodeling in organ cultures. More importantly, addition of this antibody, but not the preimmune antiserum or unrelated antibodies, to the medium of intestinal organ cultures leads to an inhibition of thyroid hormone–induced ECM remodeling, apoptosis of the larval epithelium, and the invasion of the adult intestinal primodia into the connective tissue, a process critical for adult epithelial morphogenesis. On the other hand, the antibody has little effect on adult epithelial cell proliferation. Furthermore, a known MMP inhibitor can also inhibit epithelial transformation in vitro. These results indicate that ST3 is required for cell fate determination and cell migration during morphogenesis, most likely through ECM remodeling.

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Section: Generation Of Antibody Against St3 Catalytic Domain and Western Blot Analysismentioning

confidence: 99%

Requirement for Matrix Metalloproteinase Stromelysin-3 in Cell Migration and Apoptosis during Tissue Remodeling in Xenopus laevis

Ishizuya‐Oka

Amano

et al. 2000

The Journal of Cell Biology

112

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“…PMN may locally degrade matrix macromolecules in the presence of inhibitors, in part, through oxidative inactivation of proteinase inhibitors in the pericellular environment. Both reactive oxygen species and metalloproteinases have been shown to inactivate eq-proteinase inhibitor (13,14,22,65) and other physiologic proteinase inhibitors (22,23,39,53). PMN release oxidants locally at the site of their contact with a surface (64), and activated PMN secrete metalloproteinases (4,24,45).…”

mentioning

confidence: 99%

Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases.

Owen

Campbell

Sannes

et al. 1995

The Journal of Cell Biology

357

321

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Abstract. Serine proteinases of human polymorphonuclear neutrophils play an important role in neutrophilmediated proteolytic events; however, the non-oxidative mechanisms by which the cells can degrade extracellular matrix in the presence of proteinase inhibitors have not been elucidated. Herein, we provide the first report that human neutrophils express persistently active cell surface-bound human leukocyte elastase and cathepsin G on their cell surface. Unstimulated neutrophils have minimal cell surface expression of these enzymes; however, phorbol ester induces a 30-fold increase. While exposure of neutrophils to chemoattractants (fMLP and C5a) stimulates modest (two-to threefold) increases in cell surface expression of serine proteinases, priming with concentrations of lipopolysaccharide as low as 100 fg/ml leads to striking (up to 10-fold) increase in chemoattractant-induced cell surface expression, even in the presence of serum proteins. LPSprimed and fMLP-stimulated neutrophils have ~100 ng of cell surface human leukocyte elastase activity per 106 cells. Cell surface-bound human leukocyte elastase is catalytically active, yet is remarkably resistant to inhibition by naturally occurring proteinase inhibitors. These data indicate that binding of serine proteinases to the cell surface focuses and preserves their catalytic activity, even in the presence of proteinase inhibitors. Upregulated expression of persistently active cell surfacebound serine proteinases on activated neutrophils provides a novel mechanism to facilitate their egress from the vasculature, penetration of tissue barriers, and recruitment into sites of inflammation. Dysregulation of the cell surface expression of these enzymes has the potential to cause tissue destruction during inflammation.

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“…Treatment with methionine reductase restored anti-elastase activity suggesting that the functional impairment was directly related to the methionine oxidation (Carp et al, 1983). Similarly, the proteinase inhibitor -2 macroglobulin has been shown to possess oxidisable methionine residues (Reddy et al, 1994) though their oxidation in this case did not appear to result in a loss of antiprotease function. Instead their oxidation appeared to spare the oxidation of a critical tryptophan residue related to the protein function suggesting that in certain proteins methionine may have protective antioxidant functions.…”

Section: Methionine Oxidationmentioning

confidence: 82%

Protein oxidation at the air-lung interface

2003

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Whilst performing its normal functions the lung is required to deal with a range of toxic insults. Whether these are infectious agents, allergens or air pollutants they subject the lung to a range of direct and indirect oxidative stresses. In many instances these challenges lead to oxidative alterations of peptides and proteins within the lung. Measurement of protein oxidation products permits the degree of oxidative stress to be assessed and indicates that endogenous antioxidant defences are overwhelmed. The range of protein oxidation products observed is diverse and the nature and extent of specific oxidation products may inform us about the nature of the damaging ROS and NOS. Recently, there has been a significant shift away from the measurement of these oxidation products simply to establish the presence of oxidative stress, to a focus on identifying specific proteins sensitive to oxidation and establishing the functional consequences of these modifications. In addition the identification of specific enzyme systems to repair these oxidative modifications has lead to the belief that protein function may be regulated through these oxidation reactions. In this review we focus primarily on the soluble protein components of within the surface liquid layer in the lung and the consequence of their undue oxidation.

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Oxidative dissociation of human alpha 2-macroglobulin tetramers into dysfunctional dimers.

Cited by 104 publications

References 66 publications

Requirement for Matrix Metalloproteinase Stromelysin-3 in Cell Migration and Apoptosis during Tissue Remodeling in Xenopus laevis

Requirement for Matrix Metalloproteinase Stromelysin-3 in Cell Migration and Apoptosis during Tissue Remodeling in Xenopus laevis

Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases.

Protein oxidation at the air-lung interface

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