Human Pathology

1994

DOI: 10.1016/0046-8177(94)90271-2

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The association of mast cells and atherosclerosis: A morphologic study of early atherosclerotic lesions in young people

James B. Atkinson

¹

,

Charles W. Harlan

²

,

Gretel C. Harlan

³

et al.

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Additional New Observations From Pday Studies1

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Cited by 109 publications

(67 citation statements)

References 23 publications

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“…Although previous studies have found increased numbers of mast cells 19,[21][22][23]33 ; MMP-1-, MMP-3-, and MMP-9 -immunopositive cells; and net MMP activity [12][13][14] in the shoulder regions of atherosclerotic plaques, no direct collocation or involvement of mast cells in MMP activation has been reported.…”

Section: Discussionmentioning

confidence: 81%

“…[3][4][5] It has been suggested that mast cells contribute to this process by releasing neutral proteases such as tryptase and chymase. 19,[21][22][23]33 These enzymes, which are released from mast cells by degranulation, may act indirectly by activation of . Caseinolytic in situ zymography in the presence of antipain and chymostatin.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Activation of Matrix-Degrading Metalloproteinases by Mast Cell Proteases in Atherosclerotic Plaques

¹

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²

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et al. 1998

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Abstract-Recent studies suggest that mast cell-derived neutral proteases can activate matrix-degrading metalloproteinases (MMPs). We have investigated the role of the mast cell proteases tryptase and chymase in the activation of MMPs in human carotid endarterectomy specimens (atherosclerotic, nϭ32) and postmortem carotid arteries (control, nϭ17). In vitro degranulation of mast cells in atherosclerotic carotid arteries by compound 48/80 caused a significant increase in MMP activity. Addition of the nonselective tryptase inhibitor antipain, the specific trypsinlike protease inhibitor 4-amidinophenylmethanesulfonyl fluoride, and the chymase inhibitor chymostatin reduced this increase in MMP activity by 30Ϯ6%, 23Ϯ6%, and 9Ϯ2%, respectively. Immunocytochemistry identified significantly higher numbers of tryptase-containing cells (mast cells) and cells expressing MMP-1 and MMP-3 in the "shoulder" regions of atherosclerotic artery lesions compared with the tunica media of control arteries. Dual immunocytochemistry showed collocation of MMP-1 and MMP-3 with mast cells in the shoulder regions. Degranulation was observed in 78Ϯ5% (meanϮSEM) of mast cells in this area, whereas nonactivated mast cells were observed in all other areas. In situ zymography revealed caseinolytic and gelatinolytic activity in these areas. In conclusion, in vitro mast cell degranulation, which releases mast cell proteases, in carotid arteries increases MMP activity. Furthermore, elevated MMP-1 and MMP-3 expression is collocated with increased numbers of degranulated mast cells and with greater MMP activity in the shoulder regions of atherosclerotic plaques. Activation of MMPs by mast cell-derived proteases may be an important mechanism in atherosclerotic plaque destabilization. (Arterioscler Thromb Vasc Biol. 1998;18:1707-1715.)

“…Although previous studies have found increased numbers of mast cells 19,[21][22][23]33 ; MMP-1-, MMP-3-, and MMP-9 -immunopositive cells; and net MMP activity [12][13][14] in the shoulder regions of atherosclerotic plaques, no direct collocation or involvement of mast cells in MMP activation has been reported.…”

Section: Discussionmentioning

confidence: 81%

“…[3][4][5] It has been suggested that mast cells contribute to this process by releasing neutral proteases such as tryptase and chymase. 19,[21][22][23]33 These enzymes, which are released from mast cells by degranulation, may act indirectly by activation of . Caseinolytic in situ zymography in the presence of antipain and chymostatin.…”

Section: Discussionmentioning

confidence: 99%

Activation of Matrix-Degrading Metalloproteinases by Mast Cell Proteases in Atherosclerotic Plaques

¹

,

²

,

³

et al. 1998

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Abstract-Recent studies suggest that mast cell-derived neutral proteases can activate matrix-degrading metalloproteinases (MMPs). We have investigated the role of the mast cell proteases tryptase and chymase in the activation of MMPs in human carotid endarterectomy specimens (atherosclerotic, nϭ32) and postmortem carotid arteries (control, nϭ17). In vitro degranulation of mast cells in atherosclerotic carotid arteries by compound 48/80 caused a significant increase in MMP activity. Addition of the nonselective tryptase inhibitor antipain, the specific trypsinlike protease inhibitor 4-amidinophenylmethanesulfonyl fluoride, and the chymase inhibitor chymostatin reduced this increase in MMP activity by 30Ϯ6%, 23Ϯ6%, and 9Ϯ2%, respectively. Immunocytochemistry identified significantly higher numbers of tryptase-containing cells (mast cells) and cells expressing MMP-1 and MMP-3 in the "shoulder" regions of atherosclerotic artery lesions compared with the tunica media of control arteries. Dual immunocytochemistry showed collocation of MMP-1 and MMP-3 with mast cells in the shoulder regions. Degranulation was observed in 78Ϯ5% (meanϮSEM) of mast cells in this area, whereas nonactivated mast cells were observed in all other areas. In situ zymography revealed caseinolytic and gelatinolytic activity in these areas. In conclusion, in vitro mast cell degranulation, which releases mast cell proteases, in carotid arteries increases MMP activity. Furthermore, elevated MMP-1 and MMP-3 expression is collocated with increased numbers of degranulated mast cells and with greater MMP activity in the shoulder regions of atherosclerotic plaques. Activation of MMPs by mast cell-derived proteases may be an important mechanism in atherosclerotic plaque destabilization. (Arterioscler Thromb Vasc Biol. 1998;18:1707-1715.)

“…[1][2][3] Mast cell activation is involved in atherogenesis and coronary artery disease. 4,5 Indeed, an elevated number of mast cells has been observed in coronary atherectomy specimens from culprit lesions, eliciting acute coronary syndromes. 6 Furthermore, an increased number of mast cells at the site of plaque erosion or rupture was found in patients who died of myocardial infarction.…”

mentioning

confidence: 99%

Histamine Induces Tissue Factor Expression

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³

et al. 2005

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Background— Histamine can induce coronary vasospasm, leading to variant angina and acute myocardial infarction. However, the role of histamine in thrombus formation is ill defined. Hence, this study investigates whether histamine induces tissue factor (TF) expression in vascular cells. Methods and Results— Histamine (10 −8 to 10 −5 mol/L) induced TF expression in a concentration-dependent manner in human aortic endothelial and vascular smooth muscle cells, whereas TF pathway inhibitor expression remained unaffected. RT-PCR and Northern blotting revealed that histamine stimulated TF mRNA transcription, peaking at 1 hour. Protein expression increased 18-fold ( P <0.02) with a maximum at 5 hours, which was paralleled by a 4-fold augmentation in surface activity ( P <0.01). These effects were completely prevented by pretreatment with the H 1 receptor antagonists mepyramine ( P <0.0001), chlorpheniramine, and diphenhydramine but not the H 2 receptor antagonist cimetidine ( P =NS). Histamine induced a time-dependent, H 1 receptor–mediated activation of p38 MAP kinase (p38), p44/42 MAP kinase (ERK), and c-jun terminal NH 2 kinase (JNK). Blocking of p38, ERK, or JNK with SB203580 ( P <0.0001), PD98059 ( P <0.0001), or SP600125 ( P <0.0001), respectively, impaired histamine-induced TF expression in a concentration-dependent manner. In contrast, histamine-stimulated TF expression was increased by phosphatidylinositol 3-kinase inhibition with LY294002 or wortmannin, whereas it was not affected by Rho-kinase inhibition with Y-27632 or hydroxyfasudil. Conclusions— Histamine induces expression of TF, but not TF pathway inhibitor, in vascular cells via activation of the H 1 , but not H 2 , receptor. This effect is mediated by the MAP kinases p38, ERK, and JNK. This observation may open novel perspectives in the treatment of variant angina and acute coronary syndromes.

“…As a component of the immune system, mast cells are widely distributed throughout the body and have an important role in defending hosts against pathogens. In the cardiovascular tissues, this type of cell is present at the intima of normal/fatty streak (Kaartinen et al 1994), whereas it is more prominent at the adventitia of atherosclerotic aorta (Atkinson et al 1994) and in the vulnerable plaques of atherosclerotic coronary and carotid arteries (Kaartinen et al 1998;Jeziorska et al 1997). Our data support a previous study (Kaartinen et al 1994) which shows that mast cells at the intima decreased according to the degree of atherosclerosis, assuming that a loss of endogenous heparin production by mast cells stimulates pro-coagulant activity on atherosclerotic plaques.…”

Section: Discussionmentioning

confidence: 99%

Mast cell density and distribution in human abdominal aortic aneurysm

et al. 2011

Etiology, Pathogenesis and Pathophysiology of Aortic Aneurysms and Aneurysm Rupture

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