The potential use of MMP inhibitors to treat CNS diseases

Bibliography

• BASBAUM CB, WERB Z: Focalized proteolysis: spatialand temporal regulation of extracellular matrix degra-dation at the cell surface. Curr. Opin. Cell. Biol. (1996) 8:731–738.
   PubMed Web of Science ®Google Scholar
• PEI D, WEISS S: Transmembrane-deletion mutants ofthe membrane-type matrix metalloproteinase-1 pro-cess progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. (1996) 271:9135–9140.
   PubMed Web of Science ®Google Scholar
• IMAI K, OHUCHI E, AOKI T et al.: Membrane-type matrixmetalloproteinase 1 is a gelatinolytic enzyme and is in a complex with tissue inhibitor of metalloproteinase-2. Cancer Res. (1996) 56:2707–2710.
   PubMed Web of Science ®Google Scholar
• YONG VW, KREKOSKI CA, FORSYTH PA, BELL R, ED-WARDS DR: Matrix metalloproteinases and diseases of the central nervous system. Trends Neurosci. (1998) 21:75–80.
   PubMed Web of Science ®Google Scholar
• ••Useful and comprehensive review on MMPs in the CNS.
   Google Scholar
• NAGASE H: Activation mechanisms of matrix metallo-. Biol. Chem. (1997) 378:151–160.
   PubMed Web of Science ®Google Scholar
• ••A good review on the biochemistry of MMP activation.
   Google Scholar
• UHM JH, DOOLEY NP, VILLEMURE JG, YONG VW: Mecha-nisms of glioma invasion: role of matrix-metalloproteinases. Can. J. Neurol. Sci. (1997) 24:3–15.
   PubMed Web of Science ®Google Scholar
• WERB Z, TREMBLE P, DAMSKY CH: Regulation of extra-cellular matrix degradation by cell-extracellular ma-trix interactions. Cell. Differentiation Dev. (1990) 32:299–306.
   PubMedGoogle Scholar
• HEINO J: Biology of tumor cell invasion: interplay ofcell adhesion and matrix degradation. Int. J. Cancer (1996) 65:717–722.
   PubMed Web of Science ®Google Scholar
• GOLDBERG GI, MARMER BL, GRANT GA, EISEN AZ, WIL-HEIM S, HE C: Human 72-kilodalton Type IV collage-nase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proc. Natl. Acad. Sci. USA (1989) 86:8207–8211.
   PubMed Web of Science ®Google Scholar
• STETLER-STEVENSON WG, KRUTZSCH HC, LIOTTA L: Tis-sue inhibitor of metalloproteinase (TIMP-2). J. Biol. Chem. (1989) 264:17374–17378.
   PubMed Web of Science ®Google Scholar
• STRONGIN AY, COLLIER I, BANNIKOV G, MARMER BL, GRANT GA, GOLDBERG GI: Mechanism of cell surface activation of 72 kDa Type IV collagenase. J. Biol. Chem. (1995) 270:5331–5338.
   PubMed Web of Science ®Google Scholar
• MURPHY G, KNAUPER V: Relating matrix metalloprote-inase structure to function: why the "hemopexin" do-main? Matrix Biol. (1997) 15:511–518.
   Google Scholar
• ••A useful review on the function of the MMP domains andhow these interact with TIMPs.
   Google Scholar
• BROOKS PC, STROMBALD S, SANDERS LC et al.: Localiza-tion of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin avI33. Cell (1996) 85:683–693.
   PubMed Web of Science ®Google Scholar
• TAKAHASHI C, SHENG Z, HORAN TP et al.: Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK. Proc. Natl. Acad. Sci. USA (1998) 95:13221–13226.
   PubMed Web of Science ®Google Scholar
• ROMANIC AM, MADRI JA: Extracellular matrix-degrading proteinases in the nervous system. Brain Pathol. (1994) 4:145–156.
   PubMed Web of Science ®Google Scholar
• CHAMBERS AF, MATRISIAN LM: Changing views of the role of matrix metalloproteinases in metastasis. J. Natl. Cancer Inst. (1997) 89:1260–1270.
   PubMed Web of Science ®Google Scholar
• ••This is a good review on MMPs in cancer.
   Google Scholar
• STETLER-STEVENSON WG, AZNAVOORIAN S, LIOTTA LA: cell interactions with the extracellular matrix during invasion and metastasis. Ann. Rev. Cell Biol. (1993) 9:541–573.
   PubMed Web of Science ®Google Scholar
• KAWAMATA H, KAMEYAMA S, KAWAI K et al.: Marked ac- of the metastatic phenotype of a rat bladder carcinoma cell line by the expression of human gelati-nase A. Int. J. Cancer (1995) 63:568–575.
   PubMed Web of Science ®Google Scholar
• SEHGAL G, HUA J, BERNHARD EJ, SEHGAL I, THOMPSON TC, MUSCHEL RJ: Requirement for matrix metalloproteinase-9 (gelatinase B) expression in me-tastasis by murine prostate carcinoma. Am. J. Pathol. (1998) 152:591–596.
   PubMed Web of Science ®Google Scholar
• KHOKHA R: Suppression of the tumorigenic and meta-static abilities of murine B16-F10 melanoma cells in vivo by the overexpression of the tissue inhibitor of metalloproteinase-1. J. Natl. Cancer Inst. (1994) 86:299–304.
   PubMed Web of Science ®Google Scholar
• IMREN S, KOHN DB, SHIMADA H, BLAVIER L, DECLERKYA : Overexpression of tissue inhibitor of metalloproteinases-2 retroviral-mediated gene trans-fer in vivo inhibits tumor growth and invasion. Cancer Res. (1996) 56:2891–2895.
   PubMed Web of Science ®Google Scholar
• ITOH T, TANIOKA M, YOSHIDA H, NISHIMOTO H, ITO-HARA S: Reduced angiogenesis and tumor progression in gelatinase A-deficient mice. Cancer Res. (1998) 58:1048–1051.
   PubMed Web of Science ®Google Scholar
• SHAPIRO SD: Matrix metalloproteinases degradationof extracellular matrix: biological consequences. Curr. Opin. Cell. Biol. (1998) 10:602–608.
   PubMed Web of Science ®Google Scholar
• WILSON CL, HEPPNER KJ, LABOSKY PA, HOGAN BLM, MATRISIAN LM: Intestinal tumorigenesis is suppressed in mice lacking the metalloproteinase matrilysin. Proc. Natl. Acad. Sci. USA (1997) 94:1402–1407.
   PubMed Web of Science ®Google Scholar
• SREENATH T, MATRISIAN LM, STETLER-STEVENSON W,GATTONI-CELLI S, POZZATTI RO: Expression of matrix metalloproteinase genes in transformed rat cell lines of high and low metastatic potential. Cancer Res. (1992) 52:4942–4947.
   PubMed Web of Science ®Google Scholar
• MASSON R, LEFEBVRE 0, NOEL A et al.: In vivo evidencethat the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy. J. Cell Biol. (1998) 140:1535–1541.
   Google Scholar
• HEPPNER KJ, MATRISIAN LM, JENSEN RA, RODGERS WH: Expression of most matrix metalloproteinase family members in breast cancer represents a tumor-induced host response. Am. J. Pathol (1996) 149:273–282.
   PubMed Web of Science ®Google Scholar
• SEGAIN JP, HARB J, GREGOIRE M, MEFLAH K, MENAN-TEAU J: Induction of fibroblast gelatinase B expression by direct contact with cell lines derived from primary tumor but not from metastases. Cancer Res. (1996) 56:5506–5512.
   PubMed Web of Science ®Google Scholar
• GUO H, ZUCKER S, GORDON MK, TOOLE BP, BISWAS C: Stimulation of matrix metalloproteinase production by recombinant extracellular matrix metalloprote-inase inducer from transfected Chinese hamster ovary cells. J. Biol. Chem. (1997) 272:24–27.
   PubMed Web of Science ®Google Scholar
• SLEDGE GW JR, QULALI M, GOULET R, BONE EA, FIFE R: Effect of matrix metalloproteinase inhibitor batimas-tat on breast cancer regrowth and metastasis in athymic mice. J. Natl. Cancer Inst. (1995) 87:1546–1550.
   PubMed Web of Science ®Google Scholar
• WATSON SA, MORRIS TM, ROBINSON G, CRIMMIN MJ, BROWN PD, HARDCASTLE JD: Inhibition of organ inva-sion by the matrix metalloproteinase inhibitor bati-mastat (BB-94) in two human colon carcinoma metastasis models. Cancer Res. (1995) 55:29–33.
   Google Scholar
• WANG X, FU X, CRIMMIN MJ, HOFFMAN RM: Matrix met-alloproteinase inhibitor BB-94 (batimastafi inhibits human colon tumor growth and spread in a patient-like orthotopic model in nude mice. Cancer Res. (1994) 54:4726–4728.
   PubMed Web of Science ®Google Scholar
• BEATTIE GJ, SMYTH JF: Phase I study of intraperitoneal metalloproteinase inhibitor BB94 in patients with ma-lignant ascites. Gun. Cancer Res. (1998) 4:1899–1902.
   Web of Science ®Google Scholar
• WOJTOWICZ-PRAGA S, TORRI J, JOHNSON M et al.: Phase I trial of marimastat, a novel matrix metalloproteinase inhibitor, administered orally to patients with ad-vanced lung cancer. J. Clin. Oncol. (1998) 16:2150–2156.
   PubMed Web of Science ®Google Scholar
• EMUNAITIS J, POOLE C, PRIMROSE J et al.: Combined analysis of studies of the effects of the matrix metallo-proteinase inhibitor marimastat on serum tumor markers in advanced cancer: selection of a biologically active and tolerable dose for longer-term studies. Clin. Cancer Res. (1998) 4:1101–1109.
   PubMed Web of Science ®Google Scholar
• ABE T, MORI T, KOHNO K et al.: Expression of 72 kDa Type IV collagenase and invasion activity of human glioma cells. Clin. Exp. Metastasis (1994) 12:296–304.
   PubMed Web of Science ®Google Scholar
• UHM JH, DOOLEY NP, VILLEMURE JG, YONG VW: Glioma invasion in vitro: regulation by matrix metalloprotease-2 and protein kinase C. Clin. Exp. Me-tastasis (1996) 14:421–433.
   PubMed Web of Science ®Google Scholar
• DERYUGINA El, LUO GX, REISFELD RA, BOURDON MA, STRONGIN A: Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2. Anticancer Res. (1997) 17:3201–3210.
   PubMed Web of Science ®Google Scholar
• MATUZAWA K, FUKUYAMA K, HUBBARD SL, DIRKS PB, RUTKA JT: Transfection of an invasive human astrocy-toma cell line with a TIMP-1 cDNA: modulation of as-trocytoma invasive potential. J. Neuropath. Exp. Neurol (1996) 55:88–96.
   PubMed Web of Science ®Google Scholar
• MOHANAM S, WANG SW, RAYFORD A et al.: Expression of tissue inhibitors of metalloproteinases: negative regulators of human glioblastoma invasion in viva Clin. Exp. Metastasis (1995) 13:57–62.
   PubMed Web of Science ®Google Scholar
• SAWAYA RE, YAMAMOTO M, GOKASLAN ZL et al.: Ex-pression and localization of 72 kDa Type IV collage-nase (MMP-2) in human malignant gliomas in vivo. Clin. Exp. Metastasis (1996) 14:35–42.
   PubMed Web of Science ®Google Scholar
• YAMAMOTO M, MOHANAM S, SAWAYA R et al: Differen-tial expression of membrane-type matrix metallopro-teinase and its correlation with gelatinase A activation in human malignant brain tumours in vivo and in vi-tro. Cancer Res. (1996) 56:384–392.
   PubMed Web of Science ®Google Scholar
• LAMPERT K, MACHEIN U, MACHEIN MR, CONCA W, PE-TER HH, VOLK B: Expression of matrix metalloprote-inases and their tissue inhibitors in human brain tumors. Am. J. Pathol. (1998) 153:429–437.
   PubMed Web of Science ®Google Scholar
• ••To date, this is the most thorough study of MMPs and TIMPsin gliomas.
   Google Scholar
• RAO JS, STECK PA, MOHANAM S, STETLER-STEVENSON WG, LIOTTA LA, SAWAYA R: Elevated levels of Mr 92,000 Type IV collagenase in human brain tumors. Cancer Res. (1993) 53:2208–2211.
   PubMed Web of Science ®Google Scholar
• CUZNER ML, DAVISON AN, RUDGE P: Proteolytic en-zyme activity of blood leukocytes and cerebrospinal fluid in multiple sclerosis. Ann. Neurol. (1978) 4:337–344.
   PubMed Web of Science ®Google Scholar
• CRAMMER W, BLOOM BR, NORTON WT, GORDON S: Degradation of basic protein in myelin by neutral pro-teases secreted by stimulated macrophages: a possible mechanism of inflammatory demyelination. Proc. Natl. Acad. ScL USA (1978) 75:1554–1558.
   PubMed Web of Science ®Google Scholar
• ALVORD EC JR., HRUBY S, SIRES LR: Degradation of mye-lin basic protein by cerebrospinal fluid: preservation of antigenic determinants under physiological condi-tions. Ann. Neurol. (1979) 6:474–482.
   PubMed Web of Science ®Google Scholar
• GIJBELS K, MASURE S, CARTON H, OPDENAKKER G: Gela-tinase in the cerebrospinal fluid of patients with multi-ple sclerosis and other inflammatory neurological disorders. J. Neuroimmunol. (1992) 44:29–34.
   Google Scholar
• PAEMAN L, OLSSON T, SODERSTROM M, VAN DAMME J, OPDENAKKER G: Evaluation of gelatinases and IL-6 in the cerebrospinal fluid of patients with optic neuritis, multiple sclerosis and other inflammatory neurologi-cal diseases. Eur. j Neurol. (1994) 1:55–63.
   PubMedGoogle Scholar
• LEPPERT D, FORD J, STABLER G et al.: Metalloproteinase-9 (gelatinase 13) is selectively ele-vated in CSF during relapses and stable phases of mul-tiple sclerosis. Brain (1998) 121:2327–2334.
   PubMed Web of Science ®Google Scholar
• ROSENBERG GA, DENCOFF JE, CORREA N, REINERS M, FORD CC: Effects of steroids on CSF matrix metallo-poroteinases in multiple sclerosis: relation to blood-brain barrier injury. Neurol (1996) 46:1626–1632.
   PubMed Web of Science ®Google Scholar
• MAEDA A, SOBEL RA: Matrix metalloproteinases in the normal human central nervous system, microglial nodules, and multiple sclerosis lesions. J. Neuropath. Exp. Neurol. (1996) 55:300–309.
   PubMed Web of Science ®Google Scholar
• CUZNER ML, GVERIC D, STRABD C et al: The expression of tissue-type plasminogen activator, matrix metallo-proteases and endogenous inhibitors in the central nervous system in multiple sclerosis: comparison of stages in lesion formation. J. Neuropath. Exp. Neurol. (1996) 55:1194–1204.
   PubMed Web of Science ®Google Scholar
• COSSINS JA, CLEMENTS JM, FORD J et al.: Enhanced ex-pression of MMP-7 and MMP-9 in demyelinating multi-ple sclerosis lesions. Acta Neuropath. (1997) 94:590–598.
   PubMed Web of Science ®Google Scholar
• ANTHONY DC, FERGUSON B, MATYZAK MK, MILLER KM, ESIRI MM, PERRY VH: Differential matrix metalloprote-inase expression in cases of multiple sclerosis and stroke. Neuropathol. Appl. Neurobiol. (1997) 23:406–415.
   PubMed Web of Science ®Google Scholar
• CLEMENTS JM, COSSINS JA, WELLS GM et al.: Matrix met-alloproteinase expression during experimental auto-immune encephalomyelitis and effects of a combined matrix metalloproteinase and tumor necrosis fac - tor-cc inhibitor. J. Neuroimmunol. (1997) 74:85–94.
   PubMed Web of Science ®Google Scholar
• KIESEIER BC, KIEFER R, CLEMENTS JM et al.: Matrix metalloproteinase-9 and -7 are regulated in autoimmune encephalomyelitis. Brain (1998) 121:159–166.
   PubMed Web of Science ®Google Scholar
• PAGENSTECHER A, STADLER AK, KINCAID AL, SHAPIROSD, CAMPBELL IL: Differential expression of matrix metalloproteinase and tissue inhibitor of matrix met-alloproteinase genes in the mouse central nervous sys-tem in normal and inflammatory states. Am. J. Pathol (1998) 152:729–741.
   PubMed Web of Science ®Google Scholar
• LEPPERT D, WAUBANT E, GALARDY R, BUNNETT NW,HAUSER SL: T cell gelatinases mediate basement mem-brane transmigration in vitro. J. Immunol. (1995) 154:4379–4389.
   PubMed Web of Science ®Google Scholar
• XIA M, LEPPERT D, HAUSER SL et al.: Stimulus specificityof matrix metalloproteinase dependence of human T cell migration through a model basement membrane. Immunol. (1996) 156:160–167.
   Web of Science ®Google Scholar
• SHIPLEY JM, WESSELSCHMIDT RL, KOBAYASHI DK, LEY TJ, SHAPIRO SD: Metalloelastase is required for macrophage-mediated proteolysis and matrix inva-sion in mice. Proc. Natl. Acad. ScL USA (1996) 93:3942–3946.
   PubMed Web of Science ®Google Scholar
• ••This paper provides evidence that leukocytes utilise MMPsto penetrate across basement membrane in vivo.
   Google Scholar
• GRASSER D, MAHOOTI S, HAAS T, DAVIS S, CLARK RB, JA: The interrelationship of a4 integrin and ma-trix metalloproteinase-2 in the pathogenesis of ex-perimental autoimmune encephalomyelitis. Lab. Invest. (1998) 78:1445–1458.
   PubMed Web of Science ®Google Scholar
• ROSENBERG GA, KORNFELD M, ESTRADA E, KELLEY RO, LIOTTA LA, STETLER-STEVENSON WG: TIMP-2 reduces proteolytic opening of blood-brain barrier by Type IV collagenases. Brain Res. (1992) 576:203–207.
   PubMed Web of Science ®Google Scholar
• CHANDLER S, MILLER KM, CLEMENTS JM et al: Matrix metalloproteinases, tumor necrosis factor and multi-ple sclerosis: an overview. J. Neuroimmunol. (1997) 72:155–161.
   PubMed Web of Science ®Google Scholar
• ANTHONY DC, MILLER KM, FEARN S et al.: Matrix metal- expression in an experimentally-induced DTH model of multiple sclerosis in the rat CNS. J. Neuroimmunol. (1998) 87:62–72.
   PubMed Web of Science ®Google Scholar
• ••A well done study on the role of MMPs in inflammation andmyelin destruction.
   Google Scholar
• MATYSZAK MK, PERRY VH: Delayed-type hypersensitiv-ity lesions in the central nervous system are prevented by inhibitors of matrix metalloproteinases. J. Neuroim-munol. (1996) 69:141–149.
   PubMed Web of Science ®Google Scholar
• OPDENAKKER G, VAN DAMME J: Cytokine-regulated proteases in autoimmune diseases. Immunol. Today (1994) 15:103–107.
   PubMedGoogle Scholar
• CHANDLER S, COATES R, GEARING A, LURY J, WELLS G, BONE E: Matrix metalloproteinases degrade myelin ba-sic protein. Neurosci. Lett. (1995) 201:223–226.
   PubMed Web of Science ®Google Scholar
• CHANDLER S, COSSINS J, LURY J, WELLS G: Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumor necrosis factor-alpha fusion protein. Biochem. Biophys. Res. Commun. (1996) 228:421–429.
   PubMed Web of Science ®Google Scholar
• GIJBELS K, GALARDY RE, STEINMAN L: Reversal of ex- autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteases. J. Clin. Invest. (1994) 94:2177–2182.
   PubMed Web of Science ®Google Scholar
• ••This is the first report indicating that targeting MMPs can al-leviate EAE.
   Google Scholar
• HEWSON AK, SMITH T, LEONARD JP, CUZNER ML: Sup-pression of experimental allergic encephalomyelitis in the Lewis rat by the matrix metalloproteinase in-hibitor Ro31-9790. Inflammation Res. (1995) 44:345–349.
   PubMed Web of Science ®Google Scholar
• LIEDTKE W, CANNELLA B, MAZZACCARO RJ et aLEffec-five treatment of models of multiple sclerosis by ma-trix metalloproteinase inhibitors. Ann. Neurol. (1998) 44:35–46.
   PubMed Web of Science ®Google Scholar
• YONG VW, CHABOT S, STUVE 0, WILLIAMS G: Inter-feron beta in the treatment of multiple sclerosis: mechanisms of action. Neurol (1998) 51:682–689.
   PubMed Web of Science ®Google Scholar
• STUVE 0, DOOLEY NP, UHM JH, ANTEL JP, WILLIAMS G, YONG VW: Interferon-6 decreases the migration of T lymphocytes in vitro: effects on matrix metalloproteinase-9. Ann. Neurol. (1996) 40:853–863.
   PubMed Web of Science ®Google Scholar
• ••Together with reference 75, this article provides data that aplausible explanation for the efficacy of interferon-6 in mul-tiple sclerosis is through attenuating MMP production by, and inhibiting the migration of, T-lymphocytes.
   Google Scholar
• LEPPERT D, WAUBANT E, BURK MR, OKSENBERG JR, HAUSER SL: Interferon beta-lb inhibits gelatinase se-cretion and in vivo migration of human T cells: A possi-ble mechanism for treatment efficacy in multiple sclerosis. Ann. Neurol. (1996) 40:846–852.
   PubMed Web of Science ®Google Scholar
• STUVE 0, CHABOT S, JUNG SS, WILLIAMS G, YONG VW: Chemokine-enhanced migration of T lymphocytes is antagonized by interferon beta-lb through an effect on matrix metalloproteinase-9. J. Neuroimmunol (1997) 80:38–46.
   PubMed Web of Science ®Google Scholar
• MCGEEHAN GM, BECHERER JD, BAST JR. RC et al: Regula-tion of tumour necrosis factor-a processing by a metal-loproteinase inhibitor. Nature (1994) 370:558–560.
   Google Scholar
• GEARING AJH, BECKETT P, CHRISTODOULOU M et al: Processing of tumour necrosis factor-a precursor by metalloproteinases. Nature (1994) 370: 555–557.
   PubMed Web of Science ®Google Scholar
• MOSS ML, JIN SLC, MILLA ME et al.: Cloning of a disin-tegrin metalloproteinase that processes precursor tumour-necrosis factor-a. Nature (1997) 385:733–736.
   PubMed Web of Science ®Google Scholar
• BLACK RA, RAUCH CT, KOZLOAKY CJ et al.: A metallo-proteinase disintegrin that releases tumour-necrosis factor-a from cells. Nature (1997) 385:729–733.
   PubMed Web of Science ®Google Scholar
• ARMOUR A, SLOCOMBE PM, WEBSTER A et al: TNF-a converting enzyme ('FACE) is inhibited by TIMP-3. FEBS Lett. (1998) 435:39–44.
   PubMed Web of Science ®Google Scholar
• LEPAGE RN, FOSANG AJ, FULLER SJ et al.: Gelatinase A possesses a 6-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease. FEBS Lett. (1995) 377:267–270.
   PubMed Web of Science ®Google Scholar
• BACKSTROM JR, MILLER CA, TOKES ZA: Characteriza-tion of neutral proteinases from Alzheimer-affected and control brain specimens: identification of-dependent metalloproteinases from the hip-pocampus. J. Neurochem. (1992) 58:983–992.
   PubMed Web of Science ®Google Scholar
• PERESS N, PERILLO E, ZUCKER S: Localization of tissueinhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain. J. Neuropath. Exp. Neurol (1995) 54:16–22.
   PubMedGoogle Scholar
• MOK SS, EVIN G, LI QX eta].: A novel metalloprotease inrat brain cleaves the amyloid precursor protein of Alz-heimer's disease generating amyloidogenic frag-ments. Biochem. (1997) 36:156–163.
   Google Scholar
• QIU WQ, YE Z, KHOLODENKO D, SEUBERT P, SELKOE DJ:Degradation of amyloid 6-protein by a metalloprote-inase secreted by microglia and other neural and non-neural cells. J. Biol. Chem. (1997) 272:6641–6646.
   PubMed Web of Science ®Google Scholar
• MENTLEIN R, LUDWIG R, MARTENSEN I: Proteolytic deg-radation of Alzheimer's disease amyloid 6-peptide by a metalloproteinase from microglia cells. J. Neurochem. (1998) 70:721–726.
   PubMed Web of Science ®Google Scholar
• ROSENBERG GA, NAVRATIL M, BARONE F, FEUERSTEINGZ: Proteolytic cascade enzymes increase in focal cere-bral ischemia in rat. J. Cereb. Blood Flow Metab. (1996) 16:360–366.
   PubMed Web of Science ®Google Scholar
• WANG X, BARONE FC, WHITE RF, FEUERSTEIN GZ: Sub-tractive cloning identifies tissue inhibitor of matrix metalloproteinase-1 (TIIVIP-1) increased gene expres-sion following focal stroke. Stroke (1998) 29:516–520.
   PubMed Web of Science ®Google Scholar
• CLARK AW, KREKOSKI CA, BOU SS, CHAPMAN KR, ED-WARDS DR: Increased gelatinase A (MMP-2) and gelati-nase B (MMP-9) activities in human brain after focal ischemia. NeuroscL Lett. (1997) 238:53–58.
   PubMed Web of Science ®Google Scholar
• ROMANIC AM, WHITE RF, ARLETH AJ, OHLSTEIN EH, BARONE FC: Matrix metalloproteinase expression in-creases after cerebral focal ischemia in rats. Inhibition of matrix metalloproteinase-9 reduces infarct size. Stroke (1998) 29:1020–1030.
   Google Scholar
• ••This is the first paper that describes the reduction of infarctsize when MMP inhibitors are employed. It is expected to be the first of many.
   Google Scholar
• LIM GP, BACKSTROM JR, CULLEN MJ, MILLER CA, ATKIN-SON RD, TOKES ZA: Matrix metalloproteinases in the neocortex and spinal cord of amyotrophic lateral scle-rosis patients. J. Neurochem. (1996) 67:251–259.
   PubMed Web of Science ®Google Scholar
• RIVERA S, TREMBLAY E, TIMSIT S, BEN-ARI Y, KHREST-CHATISKY M: Tissue inhibitor of metalloproteinases-1 (TIMP-1) is differentially induced in neurons and as-trocytes after seizures: evidence for developmental, immediate early gene, and lesion response. J. NeuroscL (1997) 17:4223–4235.
   PubMed Web of Science ®Google Scholar
• PAUL R, LORENZL S, KOEDEL U et al.: Matrix metallopro-teinases contribute to the blood-brain barrier disrup-tion during bacterial meningitis. Ann. Neurol. (1998) 44:592–600.
   PubMed Web of Science ®Google Scholar
• KOLB SA, LAHRTZ F, PAUL R: Matrix metalloproteinasesand tissue inhibitors of metalloproteinases in viral meningitis: upregulation of MMP-9 and TIMP-1 in cere-brospinal fluid. J. Neuroimmunol. (1998) 84:143–150.
   PubMed Web of Science ®Google Scholar
• SUGUIRA Y, SHIMADA H, SEEGER RC, LAUG WE, DE-CLERK YA: Matrix metalloproteinases-2 and -9 are ex-pressed in human neuroblastoma: contribution of stromal cells to their production and correlation with metastasis. Cancer Res. (1998) 58:2209–2216.
   PubMed Web of Science ®Google Scholar
• ARA T, FUKUZAWA M, KUSAFUKA T eta].: Immunohisto-chemical expression of MMP-2, MMP-9 and TIMP-2 in neuroblastoma: association with tumor progression and clinical outcome. J. Pediatr. Surg. (1998) 33:1272–1278.
   Google Scholar
• MCGUIRE PG, SEEDS NW: Degradation of underlying extracellular matrix by sensory neurons during neu-rite outgrowth. Neuron (1990) 4:633–642.
   PubMed Web of Science ®Google Scholar
• MUIR D: Metalloproteinase-dependent neurite out-growth within a synthetic extracellular matrix is in-duced by nerve growth factor. Exp. Cell Res. (1994) 210:243–252.
   PubMed Web of Science ®Google Scholar
• NORDSTROM LA, LOCHNER J, YEUNG W, CIMENT G: The metalloproteinase stromelysin-1 (transin) mediates PC12 cell growth cone invasiveness through basal laminae. Mol. Cell. Neurosci. (1995) 6:56–68.
   PubMed Web of Science ®Google Scholar
• SHEFFEILD JB, KRASNOPOLSKY V, DEHLINGER E: Inhibi-tion of retinal growth cone activity by specific metallo-proteinase inhibitors in vitro. Dev. Dynamics (1994) 200:79–88.
   PubMed Web of Science ®Google Scholar
• MACHIDA CM, RODLAND KD, MATRISIAN L, MAGUN BE, CIMENT G: NGF induction of the gene encoding the protease transin accompanies neuronal differentia-tion in PC12 cells. Neuron (1989) 2:1587–1596.
   PubMed Web of Science ®Google Scholar
• AMBERGER VR, AVELLANA-ADALID V, HENSEL T, BARON-VAN EVERCOOREN A, SCHWAB ME: Oligodendrocyte-type 2 astrocyte progenitors use a metalloendoprotease to spread and migrate on CNS myelin. Eur.J. Neurosci. (1997) 9:151–162.
   PubMed Web of Science ®Google Scholar
• UHM JH, DOOLEY NP, OH LYS, YONG VW: Oligodendro-cytes utilize a matrix metalloproteinase, MMP-9, to ex-tend processes along an astrocyte extracellular matrix. Glia (1998) 22:53–63.
   PubMed Web of Science ®Google Scholar
• ZUO J, FERGUSON TA, HERNANDEZ YJ, STETLER-STEVENSON WG, MUIR D: Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan. J. Neurosci. (1998) 18:5203–5211.
   PubMed Web of Science ®Google Scholar
• ••An elegant manuscript that provides a link between MMPsand permissive/non-permissive substratum for neurite elongation
   Google Scholar
• BECKETT RP, DAVIDSON AH, DRUMMOND AH, HUXLEY P, WHITTAKER M: Recent advances in matrix metallo-proteinase inhibitor research. Drug Discov. Today (1995) 1:16–26.
   Web of Science ®Google Scholar
• BLACK RA, WHITE JM: ADAMS: Focus on the protease domain. Curr. Opin. Cell Biol. (1998) 10:654–659.
   PubMed Web of Science ®Google Scholar
• PAN D, RUBIN GM: Kuzbanian controls proteolytic processing of notch and mediates lateral inhibition during drosophila and vertebrate neurogenesis. Cell (1997) 90:271–280.
   PubMed Web of Science ®Google Scholar
• FARMBROUGH D, PAN D, RUBIN G, GOODMAN CS: The cell surface metalloproteinase/disintegrin kuzbanian is required for axonal extension in drosophila. Proc. Nati Acad. Sci. USA (1996) 93:13233-13238. Wee Yong and Cancer Research Groups, of Oncology and Clinical Neurosciences, of Calgary, 3330 Hospital Drive NW, Calgary, Alberta2N 4N1, Canada.: +1 403 220 3544; Fax: +1 403 283 8731;:[email protected]
   Google Scholar