Intracellular organelle motility and membrane fusion processes in human neutrophils upon cell activation

Mollinedo, Faustino; Schneider, Donald L.

doi:10.1016/0014-5793(87)80655-5

Cited by 29 publications

(20 citation statements)

References 15 publications

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“…Because MMP-9 protein is synthesized in the neutrophil early in its development and is stored in tertiary granules, very little mRNA for MMP-9 is seen in the neutrophil once it enters the circulation. 20,21 In contrast to the MMP-9 in the lymph, MMP-9 is activated in the myocardium, as demonstrated by both gelatin zymography and in situ zymography. The neutrophil is also the source of early MMP-9 appearance in the myocardium.…”

Section: Mmp-9 Levels In Vivomentioning

confidence: 98%

“…Thus, neutrophils can easily be activated by chemotactic factors to secrete MMP-9 from the tertiary granules. 20,21,24 Additional or greater stimulation is required for degranulation of neutrophil primary granules, which contain the neutrophil proteases that might activate MMP-9. A greater sensitivity to chemotactic factors occurs when neu- Figure 6.…”

Section: Mmp-9 Levels In Vivomentioning

confidence: 99%

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Matrix-Dependent Mechanism of Neutrophil-Mediated Release and Activation of Matrix Metalloproteinase 9 in Myocardial Ischemia/Reperfusion

Lindsey

Wedin²,

Brown³

et al. 2001

Circulation

223

150

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Background-A key component of reperfusion of myocardial infarction is an immediate inflammatory response, which enhances tissue repair. Matrix turnover is crucial to tissue repair, and matrix metalloproteinases (MMPs) are key enzymes involved in matrix degradation. The hypothesis tested is that one inflammation-based effector of tissue repair is the secretion and activation of MMP-9 by infiltrating neutrophils. Methods and Results-Cardiac lymph and tissue were assayed for latent and active MMP-2 and MMP-9 by zymography and immunochemistry. Dual-labeling immunofluorescence determined the cellular source of MMP-9 protein. Isolated canine neutrophils were incubated with preischemic and postischemic cardiac lymph in the presence and absence of collagen-fibronectin pads, and the supernatants were assayed for latent and active MMP-9. MMP-9 increased during the first hours of reperfusion in both lymph supernatants and myocardial extracts, and this increase was of neutrophil origin. MMP-9 in the cardiac lymph remained latent but was activatable. In contrast, MMP-9 in the myocardium was in both latent and active forms. In situ zymography demonstrated that activated MMP-9 surrounded the infiltrated neutrophils. When postischemic cardiac lymph was incubated with neutrophils in vitro, MMP-9 secretion and activation occurred only in the presence of a collagen-fibronectin substrate; preischemic cardiac lymph did not induce significant secretion or activation. Conclusions-Infiltrating neutrophils are an early source of MMP-9 after reperfusion, and a portion of MMP-9 in the myocardium is active. Infiltrating neutrophils may localize MMP-9 activation by secreting MMP-9 and as a source of activating proteases.

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Section: Mmp-9 Levels In Vivomentioning

confidence: 98%

Section: Mmp-9 Levels In Vivomentioning

confidence: 99%

Matrix-Dependent Mechanism of Neutrophil-Mediated Release and Activation of Matrix Metalloproteinase 9 in Myocardial Ischemia/Reperfusion

Lindsey

Wedin²,

Brown³

et al. 2001

Circulation

223

150

View full text Add to dashboard Cite

show abstract

“…1C, lane 7 vs lane 8). The MMP differences between LH vs 9NC plasma could be caused by differential release of MMPs from, e.g., platelets and leukocytes, with a changed MMP content/profile depending on the anticoagulant used (6,8 ).…”

Section: To the Editormentioning

confidence: 99%

Effect of Anticoagulants and Cell Separation Media as Preanalytical Determinants on Zymographic Analysis of Plasma Matrix Metalloproteinases

Mannello

Luchetti²,

Canonico

et al. 2003

Clinical Chemistry

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“…This recovery could be due either to the release of immature neutrophils from bone marrow or to recirculation of neutrophiis expressing lower CD45 ieveis from lung capillaries [25]. We have previously demonstrated that CD45 molecules arc stored in resting neutrophils on membranes from the readily translocatabie tertiary secretory granuies, as weli as in that from specific granules [9], and it is known that intraceilular compartmcntaiization of these organelles is regulated during neutrophil activation [26].…”

Section: Discussionmentioning

confidence: 99%

Biochemical and functional characterization of the leucocyte tyrosine phosphatase CD4S (CD4SRO, 180 kD) from human neutrophils. In vivo upregulation of CD45RO plasma membrane expression on patients undergoing haemodialysis

Pulido

Álvarez

Mollinedo

et al. 1992

Clinical and Experimental Immunology

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SUMMARYThe biochemical and functional characterization, and the regulation of plasma membrane expression of the leucocyte tyrosine phosphatase CD45. have been investigated in neutrophils from healthy donors and patients undergoing haemodialysis. CD45 proteins of 180 kD and 130-150 kD were precipitated from neutrophils from both healthy subjects and haemodialysed patients. Prolonged storing, as well as trypsin treatment of satnples containing the 180-kD CD45 protein, generated the 130-150-kD polypeptides. The 130-150-kD CD45 polypeptides carried extracellular CD45 epitopes. including the sialic acid-related UCHLI epitope (CD45RO). Furthermore, these trypsin-generated CD45 polypeptides did not possess phosphatase activity, which could be detected on the 180-kD protein. A remarkable quantitative increase o^ cell surface expression of the neutrophil CD45 components was detected both afler in vitro neutrophil activation and after dialysis treatment with neutropenic membranes. The CD45 biochemical pattern did not qualitatively ehange upon either in vitro or in vivo dialysis-induced neutrophil activation. The upreguiated expression of CD45 on neutrophils from dialysed patients correlated with the neutropenic effect induced by the different dialyser membranes. Maximal upregulation ofC045 expression was observed alter ISminofdialysis with neutropenic membranes, and norrnal expression levels were restored after 1 h. By contrast, increase of CD45 plasma mernbrane expression induced in vitro by treatment of normal neutrophils with thedegranulatory agents fMLPor Ca-^ ionophore was maintained. These results demonstrate that neutrophil cell surface expression ofthe 180-kD CD45 protein is upregulated during the in vivo haemodialysis process, and suggest that a proteotytic activity could regulate the enzymatic activity of CD45 by degranulation of its cytoplasmic phosphatase domains.

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Intracellular organelle motility and membrane fusion processes in human neutrophils upon cell activation

Cited by 29 publications

References 15 publications

Matrix-Dependent Mechanism of Neutrophil-Mediated Release and Activation of Matrix Metalloproteinase 9 in Myocardial Ischemia/Reperfusion

Matrix-Dependent Mechanism of Neutrophil-Mediated Release and Activation of Matrix Metalloproteinase 9 in Myocardial Ischemia/Reperfusion

Effect of Anticoagulants and Cell Separation Media as Preanalytical Determinants on Zymographic Analysis of Plasma Matrix Metalloproteinases

Biochemical and functional characterization of the leucocyte tyrosine phosphatase CD4S (CD4SRO, 180 kD) from human neutrophils. In vivo upregulation of CD45RO plasma membrane expression on patients undergoing haemodialysis

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