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Jong Eun Lee, Yone Jung Yoon, Michael E. Moseley and Midori A. Yenari

Object. Mild hypothermia is a robust neuroprotectant, and the results of prospective clinical trials have indicated that it may improve neurological outcome in certain instances. One aspect of this protection has been associated with the prevention of blood—brain barrier (BBB) disruption. Matrix metalloproteinases (MMPs) have been implicated in BBB disruption because they can degrade the extracellular matrix. In this study the authors explored the relationship between hypothermia and MMPs and whether BBB preservation resulting from mild hypothermia therapy is due to alterations in MMP expression.

Methods. Rats were subjected to middle cerebral artery occlusion for 2 hours; the animals were maintained in a state of normothermia or mild hypothermia (33°C) immediately after the onset of ischemia. The animals' brains were collected 2, 6, and 24 hours after ischemia began. Contrast-enhanced T1-weighted magnetic resonance imaging was performed at 24 hours to assess the extent of BBB disruption.

Consistent with prior reports, areas of BBB disruption detected on T1-weighted images were smaller in the brains of rats maintained in a state of hypothermia (normothermia group 8.6 ± 3% of the brain; hypothermia group 0.2 ± 0.1% of the brain; p < 0.01). Expression of both MMP-2 and MMP-9 at the transcriptional and translational levels was reduced in hypothermic brains at 6 hours and 24 hours after ischemic injury. Matrix metalloproteinase—9 was primarily localized to cells of monocytic origin but was also observed in neurons and astrocytes. Matrix metalloproteinase—2 was found in some neurons and astrocytes but not in inflammatory cells. In addition, hypothermia increased the levels of the endogenous MMP inhibitor, tissue inhibitor of metalloproteinases—2.

Conclusions. The authors conclude that mild hypothermia attenuates BBB disruption, decreases MMP expression, and suppresses MMP activity.

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Mitsutoshi Nakada, Daisuke Kita, Kazuya Futami, Junkoh Yamashita, Noboru Fujimoto, Hiroshi Sato and Yasunori Okada

, Zhang J , Iwata K , et al : A one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases-2 using monoclonal antibodies. Clin Chim Acta 220 : 31 – 45 , 1993 Fujimoto N, Zhang J, Iwata K, et al: A one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases-2 using monoclonal antibodies. Clin Chim Acta 220: 31–45, 1993 8. Giese A , Westphal M : Glioma invasion in the central nervous system. Neurosurgery 39 : 235 – 252 , 1996 Giese A, Westphal M: Glioma

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Tadashi Yamaguchi, Takeshi Miyamoto, Keiko T. Kitazato, Eiji Shikata, Izumi Yamaguchi, Masaaki Korai, Kenji Shimada, Kenji Yagi, Yoshiteru Tada, Yoshihito Matsuzaki, Yasuhisa Kanematsu and Yasushi Takagi

). Approximately 50% of aneurysms at the anterior Willis circle including the ACoA and PCA ruptured within 12 weeks after the surgical procedure. On the other hand, we observed no ruptured aneurysms at the ACA-OlfA bifurcation despite their high incidence (80%–90%) at 12 weeks postinduction. At the rupture-prone PCA, the messenger RNA (mRNA) level of matrix metalloproteinase–9 (MMP-9) was higher, the mRNA level of the tissue inhibitor of metalloproteinase2 (TIMP2) was lower, and the disequilibrium of MMP-9/TIMP2 was higher than at the ACA-OlfA bifurcation. These findings

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Christine Wild-Bode, Michael Weller and Wolfgang Wick

Object. Migration and invasion are important prerequisites for the infiltrative and destructive growth patterns of malignant gliomas. Infiltrative growth prevents complete tumor resection and causes significant neurological morbidity and mortality.

Methods. The authors assessed the expression of matrix metalloproteinases (MMPs) at messenger RNA and protein levels, MMP-2 and MMP-9 activities, and expression levels of a panel of anti- and proapoptotic proteins of the BCL-2 family. They then correlated their findings with αVβ3 integrin expression and the migratory and invasive potentials in 12 human malignant glioma cell lines.

Multiple MMPs were expressed by most cell lines. The levels of MMP-2 and MMP-3 and the activities of MMP-2 and MMP-9 correlated with tumor cell invasion. Migration and invasion were also correlated. Although the expression levels of αVβ3 integrin did not predict migration or invasion, a neutralizing αVβ3 integrin antibody inhibited migration and invasion selectively in cell lines that contained a high level of αVβ3 integrin expression, thus indicating the important role of αVβ3 integrin for migration and invasion in this subset of cell lines. An expression pattern of BCL-2 family proteins that favor resistance to apoptosis was associated with enhanced migration, invasion, and MMP activity. Wild-type p53 cell lines migrated farther than mutant p53 cell lines.

Conclusions. Activities of MMP-2 and MMP-9 are the best predictors of glioma cell invasion. The αVβ3 integrin mediates migration and invasion in a subset of glioma cell lines, but these processes do not depend on αVβ3 integrin expression. Antiapoptotic BCL-2 family protein expression is a predictor of efficient migration and invasion.

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William T. Couldwell and V. W. Yong

, Whitehead IP , et al : Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K. Nature 390 : 632 – 636 , 1997 Keely PJ, Westwick JK, Whitehead IP, et al: Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K. Nature 390: 632–636, 1997 4. Nakada M , Kita D , Futami K , et al : Roles of membrane type 1 matrix metalloproteinase and tissue inhibitor of metalloproteinases 2 in invasion and dissemination of human malignant glioma. J Neurosurg 94

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.2005.103.2.0275 Coexpression of erythropoietin and its receptor in endolymphatic sac tumors Timothy W. A. Vogel Alexander O. Vortmeyer Irina A. Lubensky Youn-Soo Lee Makoto Furuta Barbara Ikejiri H. Jeffrey Kim Russell R. Lonser Edward H. Oldfield Zhengping Zhuang August 2005 103 2 284 288 10.3171/jns.2005.103.2.0284 Reduction in levels of matrix metalloproteinases and increased expression of tissue inhibitor of metalloproteinase2 in response to mild hypothermia therapy in experimental stroke Jong

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metalloproteinase and tissue inhibitor of metalloproteinases 2 in invasion and dissemination of human malignant glioma Mitsutoshi Nakada Daisuke Kita Kazuya Futami Junkoh Yamashita Noboru Fujimoto Hiroshi Sato Yasunori Okada March 2001 94 3 464 473 10.3171/jns.2001.94.3.0464 Enhancement of antitumor immune response in glioma models in mice by genetically modified dendritic cells pulsed with Semliki Forest virus—mediated complementary DNA Ryuya Yamanaka Susan A. Zullo Ryuichi Tanaka Michael Blaese Kleanthis

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İlker Coven, Ozge Ozer, Ozlem Ozen, Feride İffet Şahin and Nur Altinors

, Tungaria A , Kawal P : Matrix metalloproteinase-2 gene polymorphism is not associated with increased glioblastoma multiforme susceptibility: an Indian institutional experience . Neurol India 59 : 236 – 240 , 2011 9 Maes L , Lippens E , Kalala JPO , de Ridder L : The hTERT-protein and Ki-67 labelling index in recurrent and non-recurrent meningiomas . Cell Prolif 38 : 3 – 12 , 2005 10 Miyake H , Hara I , Gohji K , Yamanaka K , Hara S , Arakawa S , : Relative expression of matrix metalloproteinase-2 and tissue inhibitor of

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Atsuhisa Nakano, Eiichi Tani, Kaoru Miyazaki, Yoshihiro Yamamoto and Jun-ichi Furuyama

macrophages. J Clin Invest 80: 1644–1650, 1987 20. Hibi M , Murakami M , Saito M , et al : Molecular cloning and expression of an IL-6 signal transducer, gp130. Cell 63 : 1149 – 1157 , 1990 Hibi M, Murakami M, Saito M, et al: Molecular cloning and expression of an IL-6 signal transducer, gp130. Cell 63: 1149–1157, 1990 21. Howard EW , Bullen EC , Banda MJ : Preferential inhibition of 72- and 92-kDa gelatinases by tissue inhibitor of metalloproteinases-2. J Biol Chem 266 : 13070