PECAM-1 and gelatinase B coexist in vascular cuffs of multiple sclerosis lesions
In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B/MMP‐9 and platelet endothelial cell adhesion molecule (PECAM)‐1 have both been implicated in trans‐endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We invest...
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| Veröffentlicht in: | Neuropathology and applied neurobiology Jg. 32; H. 1; S. 15 - 22 |
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Oxford, UK
Blackwell Publishing Ltd
01.02.2006
Blackwell Science |
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| Abstract | In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B/MMP‐9 and platelet endothelial cell adhesion molecule (PECAM)‐1 have both been implicated in trans‐endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We investigated the expression of gelatinase B and PECAM‐1 in post mortem brains of MS patients by immunohistochemistry. Because increased soluble PECAM‐1 serum levels have been observed in MS patients, we also tested in vitro whether this could be due to cleavage of PECAM‐1 by gelatinase B or matrilysin‐1/MMP‐7. Constitutive expression of PECAM‐1 was found on brain endothelial cells, whilst in active MS lesions cell‐bound PECAM‐1 was highly up‐regulated on foamy macrophages in perivascular infiltrates and co‐localized with gelatinase B. However, human THP‐1 monocyte‐bound or soluble recombinant PECAM‐1 were both resistant to proteolytic cleavage by gelatinase B or matrilysin‐1 in vitro, as demonstrated by Western blot analysis and flow cytometry. These results suggest that PECAM‐1 and gelatinase B may complement each other during the transmigration of the blood–brain barrier by mononuclear cells. |
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| AbstractList | In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B-MMP-9 and platelet endothelial cell adhesion molecule (PECAM)-1 have both been implicated in trans-endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We investigated the expression of gelatinase B and PECAM-1 in post mortem brains of MS patients by immunohistochemistry. Because increased soluble PECAM-1 serum levels have been observed in MS patients, we also tested in vitro whether this could be due to cleavage of PECAM-1 by gelatinase B or matrilysin-1-MMP-7. Constitutive expression of PECAM-1 was found on brain endothelial cells, whilst in active MS lesions cell-bound PECAM-1 was highly up-regulated on foamy macrophages in perivascular infiltrates and co-localized with gelatinase B. However, human THP-1 monocyte-bound or soluble recombinant PECAM-1 were both resistant to proteolytic cleavage by gelatinase B or matrilysin-1 in vitro, as demonstrated by Western blot analysis and flow cytometry. These results suggest that PECAM-1 and gelatinase B may complement each other during the transmigration of the blood-brain barrier by mononuclear cells. In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B/MMP-9 and platelet endothelial cell adhesion molecule (PECAM)-1 have both been implicated in trans-endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We investigated the expression of gelatinase B and PECAM-1 in post mortem brains of MS patients by immunohistochemistry. Because increased soluble PECAM-1 serum levels have been observed in MS patients, we also tested in vitro whether this could be due to cleavage of PECAM-1 by gelatinase B or matrilysin-1/MMP-7. Constitutive expression of PECAM-1 was found on brain endothelial cells, whilst in active MS lesions cell-bound PECAM-1 was highly up-regulated on foamy macrophages in perivascular infiltrates and co-localized with gelatinase B. However, human THP-1 monocyte-bound or soluble recombinant PECAM-1 were both resistant to proteolytic cleavage by gelatinase B or matrilysin-1 in vitro, as demonstrated by Western blot analysis and flow cytometry. These results suggest that PECAM-1 and gelatinase B may complement each other during the transmigration of the blood-brain barrier by mononuclear cells.In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B/MMP-9 and platelet endothelial cell adhesion molecule (PECAM)-1 have both been implicated in trans-endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We investigated the expression of gelatinase B and PECAM-1 in post mortem brains of MS patients by immunohistochemistry. Because increased soluble PECAM-1 serum levels have been observed in MS patients, we also tested in vitro whether this could be due to cleavage of PECAM-1 by gelatinase B or matrilysin-1/MMP-7. Constitutive expression of PECAM-1 was found on brain endothelial cells, whilst in active MS lesions cell-bound PECAM-1 was highly up-regulated on foamy macrophages in perivascular infiltrates and co-localized with gelatinase B. However, human THP-1 monocyte-bound or soluble recombinant PECAM-1 were both resistant to proteolytic cleavage by gelatinase B or matrilysin-1 in vitro, as demonstrated by Western blot analysis and flow cytometry. These results suggest that PECAM-1 and gelatinase B may complement each other during the transmigration of the blood-brain barrier by mononuclear cells. In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B/MMP‐9 and platelet endothelial cell adhesion molecule (PECAM)‐1 have both been implicated in trans‐endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We investigated the expression of gelatinase B and PECAM‐1 in post mortem brains of MS patients by immunohistochemistry. Because increased soluble PECAM‐1 serum levels have been observed in MS patients, we also tested in vitro whether this could be due to cleavage of PECAM‐1 by gelatinase B or matrilysin‐1/MMP‐7. Constitutive expression of PECAM‐1 was found on brain endothelial cells, whilst in active MS lesions cell‐bound PECAM‐1 was highly up‐regulated on foamy macrophages in perivascular infiltrates and co‐localized with gelatinase B. However, human THP‐1 monocyte‐bound or soluble recombinant PECAM‐1 were both resistant to proteolytic cleavage by gelatinase B or matrilysin‐1 in vitro , as demonstrated by Western blot analysis and flow cytometry. These results suggest that PECAM‐1 and gelatinase B may complement each other during the transmigration of the blood–brain barrier by mononuclear cells. |
| Author | Opdenakker, G. Van Noort, J. M. Cuzner, M. L. Nelissen, I. Gveric, D. |
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| Keywords | Immunohistochemistry PECAM-1 Multiple sclerosis Nervous system diseases Enzyme Metalloendopeptidases Gelatinase B Inflammatory disease Peptidases Cuff Central nervous system disease Hydrolases Lesion MMP-7 MMP-9 |
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| References | Gveric D, Herrera B, Petzold A, Lawrence DA, Cuzner ML. Impaired fibrinolysis in multiple sclerosis: a role for tissue plasminogen activator inhibitors. Brain 2003; 126: 1590-8 Van den Steen PE, Dubois B, Nelissen I, Rudd PM, Dwek RA, Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit Rev Biochem Mol Biol 2002; 37: 375-536 Van Ranst M, Norga K, Masure S, Proost P, Vandekerckhove F, Auwerx J, Van Damme J, Opdenakker G. The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers. Cytokine 1991; 3: 231-9 Cuzner ML, Gveric D, Strand C, Loughlin AJ, Paemen L, Opdenakker G, Newcombe J. The expression of tissue-type plasminogen activator, matrix metalloproteases and endogenous inhibitors in the central nervous system in multiple sclerosis: comparison of stages in lesion evolution. J Neuropathol Exp Neurol 1996; 55: 1194-204 Niezgoda A, Losy J. Pecam-1 expression in patients with relapsing-remitting multiple sclerosis. Folia Morph (Warsz) 2002; 61: 143-5 Paemen L, Martens E, Masure S, Opdenakker G. Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity. Eur J Biochem 1995; 234: 759-65 Sun J, Williams J, Yan HC, Amin KM, Albelda SM, DeLisser HM. Platelet endothelial cell adhesion molecule-1 (PECAM-1) homophilic adhesion is mediated by immunoglobulin-like domains 1 and 2 and depends on the cytoplasmic domain and the level of surface expression. J Biol Chem 1996; 271: 18561-70 Cepinskas G, Savickiene J, Ionescu CV, Kvietys PR. PMN transendothelial migration decreases nuclear NFkappaB in IL-1beta-activated endothelial cells: role of PECAM-1. J Cell Biol 2003; 161: 641-51 Fiore E, Fusco C, Romero P, Stamenkovic I. Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity. Oncogene 2002; 21: 5213-23 Cossins JA, Clements JM, Ford J, Miller KM, Pigott R, Vos W, Van der Valk P, De Groot CJ. Enhanced expression of MMP-7 and MMP-9 in demyelinating multiple sclerosis lesions. Acta Neuropathol (Berl) 1997; 94: 590-8 Kouwenhoven M, Ozenci V, Gomes A, Yarilin D, Giedraitis V, Press R, Link H. Multiple sclerosis: elevated expression of matrix metalloproteinases in blood monocytes. J Autoimmun 2001; 16: 463-70 Chandler S, Coates R, Gearing A, Lury J, Wells G, Bone E. Matrix metalloproteinases degrade myelin basic protein. Neurosci Lett 1995; 201: 223-6 Van den Steen PE, Proost P, Wuyts A, Van Damme J, Opdenakker G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. Blood 2000; 96: 2673-81 Goldberger A, Middleton KA, Oliver JA, Paddock C, Yan HC, DeLisser HM, Albelda SM, Newman PJ. Biosynthesis and processing of the cell adhesion molecule PECAM-1 includes production of a soluble form. J Biol Chem 1994; 269: 17183-91 Cuzner ML, Opdenakker G. Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system. J Neuroimmunol 1999; 94: 1-14 Newman PJ. The biology of PECAM-1. J Clin Invest 1997; 99: 3-8 Graesser D, Solowiej A, Bruckner M, Osterweil E, Juedes A, Davis S, Ruddle NH, Engelhardt B, Madri JA. Altered vascular permeability and early onset of experimental autoimmune encephalomyelitis in PECAM-1-deficient mice. J Clin Invest 2002; 109: 383-92 Ilan N, Mohsenin A, Cheung L, Madri JA. PECAM-1 shedding during apoptosis generates a membrane-anchored truncated molecule with unique signaling characteristics. FASEB J 2001; 15: 362-72 Losy J, Niezgoda A, Wender M. Increased serum levels of soluble PECAM-1 in multiple sclerosis patients with brain gadolinium-enhancing lesions. J Neuroimmunol 1999; 99: 169-72 Liao F, Huynh HK, Eiroa A, Greene T, Polizzi E, Muller WA. Migration of monocytes across endothelium and passage through extracellular matrix involve separate domains of PECAM-1. J Exp Med 1995; 182: 1337-43 Proost P, Van Damme J, Opdenakker G. Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein. Biochem Biophys Res Commun 1993; 192: 1175-81 Gveric D, Cuzner ML, Newcombe J. Insulin-like growth factors and binding proteins in multiple sclerosis plaques. Neuropathol Appl Neurobiol 1999; 25: 215-25 Mun-Bryce S, Rosenberg GA. Gelatinase B modulates selective opening of the blood-brain barrier during inflammation. Am J Physiol 1998; 274: R1203-11 Nelissen I, Ronsse I, Van Damme J, Opdenakker G. Regulation of gelatinase B in human monocytic and endothelial cells by PECAM-1 ligation and its modulation by interferon-beta. J Leukoc Biol 2002; 71: 89-98 1991; 3 2002; 37 1997; 94 1994; 269 1997; 99 2002; 61 2002; 21 2000; 96 1999; 25 1996; 271 2003; 161 1999; 99 1995; 201 2001; 15 1995; 234 2001; 16 2002; 71 1993; 192 2002; 109 1999; 94 2003; 126 1995; 182 1998; 274 1996; 55 e_1_2_6_20_2 e_1_2_6_8_2 Niezgoda A (e_1_2_6_4_2) 2002; 61 e_1_2_6_18_2 e_1_2_6_9_2 e_1_2_6_19_2 e_1_2_6_3_2 e_1_2_6_6_2 e_1_2_6_5_2 e_1_2_6_12_2 e_1_2_6_24_2 e_1_2_6_13_2 e_1_2_6_23_2 e_1_2_6_2_2 e_1_2_6_10_2 e_1_2_6_22_2 e_1_2_6_11_2 e_1_2_6_21_2 e_1_2_6_16_2 Mun‐Bryce S (e_1_2_6_7_2) 1998; 274 e_1_2_6_17_2 e_1_2_6_14_2 e_1_2_6_15_2 e_1_2_6_25_2 |
| References_xml | – reference: Niezgoda A, Losy J. Pecam-1 expression in patients with relapsing-remitting multiple sclerosis. Folia Morph (Warsz) 2002; 61: 143-5 – reference: Sun J, Williams J, Yan HC, Amin KM, Albelda SM, DeLisser HM. Platelet endothelial cell adhesion molecule-1 (PECAM-1) homophilic adhesion is mediated by immunoglobulin-like domains 1 and 2 and depends on the cytoplasmic domain and the level of surface expression. J Biol Chem 1996; 271: 18561-70 – reference: Cuzner ML, Opdenakker G. Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system. J Neuroimmunol 1999; 94: 1-14 – reference: Van den Steen PE, Proost P, Wuyts A, Van Damme J, Opdenakker G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. Blood 2000; 96: 2673-81 – reference: Gveric D, Herrera B, Petzold A, Lawrence DA, Cuzner ML. Impaired fibrinolysis in multiple sclerosis: a role for tissue plasminogen activator inhibitors. Brain 2003; 126: 1590-8 – reference: Fiore E, Fusco C, Romero P, Stamenkovic I. Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity. Oncogene 2002; 21: 5213-23 – reference: Paemen L, Martens E, Masure S, Opdenakker G. Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity. Eur J Biochem 1995; 234: 759-65 – reference: Gveric D, Cuzner ML, Newcombe J. Insulin-like growth factors and binding proteins in multiple sclerosis plaques. Neuropathol Appl Neurobiol 1999; 25: 215-25 – reference: Cuzner ML, Gveric D, Strand C, Loughlin AJ, Paemen L, Opdenakker G, Newcombe J. The expression of tissue-type plasminogen activator, matrix metalloproteases and endogenous inhibitors in the central nervous system in multiple sclerosis: comparison of stages in lesion evolution. J Neuropathol Exp Neurol 1996; 55: 1194-204 – reference: Cossins JA, Clements JM, Ford J, Miller KM, Pigott R, Vos W, Van der Valk P, De Groot CJ. Enhanced expression of MMP-7 and MMP-9 in demyelinating multiple sclerosis lesions. Acta Neuropathol (Berl) 1997; 94: 590-8 – reference: Cepinskas G, Savickiene J, Ionescu CV, Kvietys PR. PMN transendothelial migration decreases nuclear NFkappaB in IL-1beta-activated endothelial cells: role of PECAM-1. J Cell Biol 2003; 161: 641-51 – reference: Chandler S, Coates R, Gearing A, Lury J, Wells G, Bone E. Matrix metalloproteinases degrade myelin basic protein. Neurosci Lett 1995; 201: 223-6 – reference: Losy J, Niezgoda A, Wender M. Increased serum levels of soluble PECAM-1 in multiple sclerosis patients with brain gadolinium-enhancing lesions. J Neuroimmunol 1999; 99: 169-72 – reference: Goldberger A, Middleton KA, Oliver JA, Paddock C, Yan HC, DeLisser HM, Albelda SM, Newman PJ. Biosynthesis and processing of the cell adhesion molecule PECAM-1 includes production of a soluble form. J Biol Chem 1994; 269: 17183-91 – reference: Liao F, Huynh HK, Eiroa A, Greene T, Polizzi E, Muller WA. Migration of monocytes across endothelium and passage through extracellular matrix involve separate domains of PECAM-1. J Exp Med 1995; 182: 1337-43 – reference: Van den Steen PE, Dubois B, Nelissen I, Rudd PM, Dwek RA, Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit Rev Biochem Mol Biol 2002; 37: 375-536 – reference: Ilan N, Mohsenin A, Cheung L, Madri JA. PECAM-1 shedding during apoptosis generates a membrane-anchored truncated molecule with unique signaling characteristics. 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| SubjectTerms | Biological and medical sciences Blotting, Western Brain - blood supply Brain - metabolism Brain - pathology Cell Movement - physiology Cells, Cultured Endothelial Cells - metabolism Flow Cytometry Human viral diseases Humans Immunohistochemistry Infectious diseases Leukocytes, Mononuclear - metabolism Malformations of the nervous system Matrix Metalloproteinase 9 - metabolism Medical sciences MMP-7 MMP-9 multiple sclerosis Multiple Sclerosis - metabolism Multiple Sclerosis - pathology Neurology PECAM-1 Platelet Endothelial Cell Adhesion Molecule-1 - metabolism Viral diseases Viral diseases of the lymphoid tissue and the blood. Aids |
| Title | PECAM-1 and gelatinase B coexist in vascular cuffs of multiple sclerosis lesions |
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