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W1982146541 abstract "We cloned a novel matrix metalloproteinase (MMP) called CMMP from cultured primary chicken embryo fibroblasts. The cDNA-derived CMMP sequence contains 472 amino acids including a putative 19-residue signal peptide and a unique cysteine in the catalytic domain, an insertion in a sequence motif that binds the structural (noncatalytic) zinc of MMPs. Strikingly, a homologously inserted cysteine is also found in Xenopus XMMP and human MMP19, two recently cloned novel members of the MMP family. Phylogenetic analysis suggest that XMMP and MMP19 represent founding members of the MMP family, whereas CMMP is related to collagenase MMPs. Bacterially produced recombinant CMMP (without the amino-terminal inhibition domain), which was autoproteolyzed at the carboxyl-terminal domain, digested casein and gelatin. As shown by Northern blotting, CMMP mRNA of 1.8 kilobase pairs was constitutively expressed in cultured primary chicken embryo fibroblasts and up-regulated by tumor necrosis factor-α and the phorbol ester 12-O-tetradecanoylphorbol-13-acetate, but it was not regulated by interleukin-1, basic fibroblast growth factor, or retinoic acid. CMMP mRNA of 1.8 kb was also detected in the head and body of 8-day-old chicken embryos and dramatically up-regulated in 9-day-old embryos. We cloned a novel matrix metalloproteinase (MMP) called CMMP from cultured primary chicken embryo fibroblasts. The cDNA-derived CMMP sequence contains 472 amino acids including a putative 19-residue signal peptide and a unique cysteine in the catalytic domain, an insertion in a sequence motif that binds the structural (noncatalytic) zinc of MMPs. Strikingly, a homologously inserted cysteine is also found in Xenopus XMMP and human MMP19, two recently cloned novel members of the MMP family. Phylogenetic analysis suggest that XMMP and MMP19 represent founding members of the MMP family, whereas CMMP is related to collagenase MMPs. Bacterially produced recombinant CMMP (without the amino-terminal inhibition domain), which was autoproteolyzed at the carboxyl-terminal domain, digested casein and gelatin. As shown by Northern blotting, CMMP mRNA of 1.8 kilobase pairs was constitutively expressed in cultured primary chicken embryo fibroblasts and up-regulated by tumor necrosis factor-α and the phorbol ester 12-O-tetradecanoylphorbol-13-acetate, but it was not regulated by interleukin-1, basic fibroblast growth factor, or retinoic acid. CMMP mRNA of 1.8 kb was also detected in the head and body of 8-day-old chicken embryos and dramatically up-regulated in 9-day-old embryos. Degradation and remodeling of the extracellular matrix (ECM) 1The abbreviations used are: ECM, extracellular matrix; EST, expressed sequence tag; FGF, fibroblast growth factor; IL-1, interleukin-1β; TNF, tumor necrosis factor-α; MMP, matrix metalloproteinase; MOPS, 4-morpholinepropanesulfonic acid; MT-MMP, membrane-type MMP; PCR, polymerase chain reaction; TPA, 12-O-tetradecanoylphorbol-13-acetate; bp, base pair(s); kb, kilobase pair(s). 1The abbreviations used are: ECM, extracellular matrix; EST, expressed sequence tag; FGF, fibroblast growth factor; IL-1, interleukin-1β; TNF, tumor necrosis factor-α; MMP, matrix metalloproteinase; MOPS, 4-morpholinepropanesulfonic acid; MT-MMP, membrane-type MMP; PCR, polymerase chain reaction; TPA, 12-O-tetradecanoylphorbol-13-acetate; bp, base pair(s); kb, kilobase pair(s). is thought to play important morphogenic roles during growth and development. ECM degradation is largely controlled by a superfamily of zinc-dependent endopeptidases called matrix metalloproteinases (MMPs). At present, 18 different MMPs have been cloned and characterized (1Woessner Jr., J.F. FASEB J. 1991; 5: 2145-2154Crossref PubMed Scopus (3072) Google Scholar, 2Matrisian L.M. BioEssays. 1992; 6: 121-125Google Scholar, 3Werb Z. Alexander C.M. Kelley W.M. Harris Jr., E.D. Ruddy S. Sledge C.B. Textbook of Rheumatology. 4th Ed. W. B. Saunders Co., Philadelphia1994: 248-268Google Scholar, 4Birkedal-Hansen H. Curr. Opin. Cell Biol. 1995; 7: 728-735Crossref PubMed Scopus (974) Google Scholar, 5Cossins J. Dudgeon T.J. Catlin G. Gearing A.J.H. Clements J.M. Biochem. Biophys. Res. Commun. 1996; 228: 494-498Crossref PubMed Scopus (102) Google Scholar, 6Stolov M.A. Bauzon D.D. Li J. Sedgwick T. Liang V.C.-T. Sang Q.A. Shi Y.-B. Mol. Biol. Cell. 1996; 7: 1471-1483Crossref PubMed Scopus (125) Google Scholar, 7Bartlett J.D. Simmer J.P. Xue J. Margolis H.C. Moreno E.C. Gene ( Amst. ). 1996; 183: 123-128Crossref PubMed Scopus (176) Google Scholar, 8Pendas A.M. Knauper V. Puente X.S. Llano E. Mattei M.-G. Apte S. Murphy G. Lopez-Otin C. J. Biol. Chem. 1997; 272: 4281-4286Abstract Full Text Full Text PDF PubMed Scopus (180) Google Scholar), including a novel MMP that we cloned from the frog Xenopus laevis embryos (9Yang M. Murray M.T. Kurkinen M. J. Biol. Chem. 1997; 272: 13527-13533Abstract Full Text Full Text PDF PubMed Scopus (45) Google Scholar). MMPs share similar domains with distinct structure and function, have wide and often overlapping substrate specificities, and are usually grouped as collagenases, gelatinases, stromelysins, and membrane-type MMPs.Collagenases are the only enzymes that can cleave the triple helical regions of interstitial fibrillar collagens such as collagen types I, II, and III, the most abundant proteins in the body. The cleavage occurs at one specific peptide bond, Gly775–Ile776 (Leu776 in the α2(I)-chain) in type I collagen and leads to unfolding and denaturation of the fibrillar collagens. Gelatinases A and B, also known as 72- and 92-kDa type IV collagenases, digest denatured collagen (gelatin) and components of basement membranes, a special type of ECM of epithelial, endothelial, fat, muscle, and peripheral nerve cells (10Martin G.R. Timpl R. Kuhn K. Adv. Prot. Chem. 1988; 39: 1-50Crossref PubMed Scopus (114) Google Scholar). Stromelysins are three different MMPs with wide substrate specificity, and stromelysin-1 can degrade almost any ECM component including cartilage proteoglycans (11Bonassar L.J. Frank E.H. Murray J.C. Paguio C.G. Moore V.L. Lark M.W. Sandy J.D. Wu J.J. Eyre D.R. Grodzinsky A.J. Arthritis Rheum. 1995; 38: 173-183Crossref PubMed Scopus (140) Google Scholar). Recently, four new members of the MMP family called membrane-type MMPs (MT-MMPs) were cloned (12Sato H. Takino T. Okada Y. Cao J. Shinagawa A. Yamamoto E. Seiki M. Nature. 1994; 370: 61-65Crossref PubMed Scopus (2365) Google Scholar, 13Okada A. Bellocq J.-P. Royer N. Chenard M.-P. Rio M.-C. Chambon P. Basset P. Proc. Natl. Acad. Sci. U. S. A. 1995; 92: 2730-2734Crossref PubMed Scopus (486) Google Scholar, 14Will H. Hinzmann B. Eur. J. Biochem. 1995; 231: 602-608Crossref PubMed Scopus (317) Google Scholar, 15Takino T. Sato H. Shinagawa A. Seiki M. J. Biol. Chem. 1995; 270: 23013-23020Abstract Full Text Full Text PDF PubMed Scopus (447) Google Scholar, 16Puente X.S. Pendas A.M. Liano E. Velasco G. Lopez-Otin C. Cancer Res. 1996; 56: 944-949PubMed Google Scholar, 17Yang M. Hayashi K. Hayashi M. Fujii J.T. Kurkinen M. J. Biol. Chem. 1996; 271: 25548-25554Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar). They are not secreted extracellularly but remain on the cell surface through their carboxyl-terminal transmembrane domain. Recently, however, Matsumoto et al. (18Matsumoto S. Katoh M. Saito S. Watanabe T. Masuho Y. Biochim. Biophys. Acta. 1997; 1354: 159-170Crossref PubMed Scopus (87) Google Scholar) characterized a secreted form of MT3-MMP encoded by an alternatively spliced mRNA. MT-MMPs degrade ECM components, proteolytically cleave and activate 72-kDa type IV collagenase, and therefore may regulate pericellular matrix degradation at the cell surface (19Pei D. Weiss S.J. J. Biol. Chem. 1996; 271: 9135-9140Abstract Full Text Full Text PDF PubMed Scopus (364) Google Scholar, 20Cao J. Rehemtulla A. Bahou W. Zucker S. J. Biol. Chem. 1996; 271: 30174-30180Abstract Full Text Full Text PDF PubMed Scopus (101) Google Scholar, 21Ohuchi E. Imai K. Fujii Y. Sato H. Seiki M. Okada Y. J. Biol. Chem. 1997; 272: 2446-2451Abstract Full Text Full Text PDF PubMed Scopus (827) Google Scholar).MMPs are produced as inactive precursors, which are activated by proteolytic removal of their amino-terminal domain, a 78–178-residue-long propeptide (22Strongin A.Y. Collier I. Bannikov G. Marmer B.L. Grant G.A. Goldberg G.I. J. Biol. Chem. 1995; 270: 5331-5338Abstract Full Text Full Text PDF PubMed Scopus (1434) Google Scholar, 23Pei D. Weiss S.J. Nature. 1995; 375: 244-247Crossref PubMed Scopus (530) Google Scholar, 24Benbow U. Butticé G. Nagase H. Kurkinen M. J. Biol. Chem. 1996; 271: 10715-10722Abstract Full Text Full Text PDF PubMed Scopus (24) Google Scholar). Thus, it is striking that stromelysin-1 (MMP3) proteolytically activates at least five other members of the MMP family including interstitial collagenase-1 (MMP1), matrilysin (MMP7), neutrophil collagenase-2 (MMP8), 92-kDa type IV collagenase (MMP9), and collagenase-3 (MMP13), suggesting that stromelysin-1 plays a special “upstream” role in ECM degradation and remodeling (25Murphy G. Cockett M.I. Stephens P.E. Smith B.J. Docherty A.J.P. Biochem. J. 1987; 248: 265-268Crossref PubMed Scopus (390) Google Scholar, 26Ogata Y. Enghild J.J. Nagase H. J. Biol. Chem. 1992; 267: 3581-3584Abstract Full Text PDF PubMed Google Scholar, 27Imai K. Yokohama Y. Nakanishi I. Ohuchi E. Fujii Y. Nakai N. Okada Y. J. Biol. Chem. 1995; 270: 6691-6697Abstract Full Text Full Text PDF PubMed Scopus (264) Google Scholar, 28Knauper V. Wilhelm S.M. Seperack P.K. DeClerck Y.A. Langley K.E. Osthues A. Tschesche H. Biochem. J. 1993; 295: 581-586Crossref PubMed Scopus (152) Google Scholar, 29Knauper V. Lopez-Otin C. Smith B. Knight G. Murphy G. J. Biol. Chem. 1996; 271: 1544-1558Abstract Full Text Full Text PDF PubMed Scopus (782) Google Scholar). Recently, Okamoto et al. (30Okamoto T. Akaike T. Suga M. Tanase S. Horie H. Miyajima S. Ando M. Ichinose Y. Maeda H. J. Biol. Chem. 1997; 272: 6059-6066Abstract Full Text Full Text PDF PubMed Scopus (139) Google Scholar) reported that various bacterial proteinases can also activate MMP1, MMP2, and MMP9.MMPs are expressed widely during embryogenesis, often in a highly tissue- and cell-specific pattern, suggesting distinct roles for MMPs in growth and development (17Yang M. Hayashi K. Hayashi M. Fujii J.T. Kurkinen M. J. Biol. Chem. 1996; 271: 25548-25554Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar, 31Brenner C.A. Adler R.R. Rappolee D.A. Pedersen R.A. Werb Z. Genes Dev. 1989; 3: 848-859Crossref PubMed Scopus (239) Google Scholar, 32Mattot V. Raes M.B. Henriet P. Eeckhout Y. Stehelin D. Vandenbunder B. Desbiens X. J. Cell Sci. 1995; 108: 529-535Crossref PubMed Google Scholar, 33Gack S. Vallon R. Schmidt J. Grigoriadis A. Tuckermann J. Schenkel J. Wiher H. Wagner E.F. Angel P. Cell Growth Differ. 1995; 6: 759-767PubMed Google Scholar, 34Witty J.P. Wright J.H. Matrisian L.M. Mol. Biol. Cell. 1995; 6: 1287-1303Crossref PubMed Scopus (169) Google Scholar, 35Reponen P. Sahlberg C. Munaut C. Thesleff I. Tryggvason K. J. Cell Biol. 1994; 124: 1091-1102Crossref PubMed Scopus (249) Google Scholar, 36Canete-Soler R. Gui Y.-H. Linask K.K. Muschel R.J. Dev. Dyn. 1995; 204: 30-40Crossref PubMed Scopus (54) Google Scholar, 37Sato T. del Carmen Ovejero M. Heegaard A.-M. Kumegawa M. Foged N.T. Delaisse J.-M. J. Cell Sci. 1997; 110: 589-596Crossref PubMed Google Scholar). In adult life, MMPs are rarely expressed except in rapidly remodeling tissues such as the term placenta, menstrual endometrium, and involuting mammary glands and during wound healing and inflammation (38Belaaouaj A. Shipley J.M. Kobayashi D.K. Zimonjic D.B. Popescu N. Silverman G.A. Shapiro S.D. J. Biol. Chem. 1995; 270: 14568-14575Abstract Full Text Full Text PDF PubMed Scopus (137) Google Scholar, 39Boudreau N. Sympson C.J. Werb Z. Bissell M.J. Science. 1995; 267: 891-893Crossref PubMed Scopus (1113) Google Scholar, 40Kokorine I. Marbaix E. Henriet P. Okada Y. Donnez J. Eeckhout Y. Courtoy P.J. J. Cell Sci. 1996; 109: 2151-21608PubMed Google Scholar, 41Rodgers W.H. Matrisian L.M. Giudice L.L. Dsupin N. Cannon P. Svitek C. Gorstein F. Osteen K.G. J. Clin. Invest. 1994; 94: 946-953Crossref PubMed Scopus (358) Google Scholar, 42Okada A. Tomasetto C. Lutz Y. Bellocq J.-P. Rio M.-C. Basset P. J. Cell Biol. 1997; 137: 67-77Crossref PubMed Scopus (192) Google Scholar). MMPs are also thought to play a critical role in tumor growth and metastasis (43Stetler-Stevenson W.G. Aznavoorian S. Liotta L.A. Annu. Rev. Cell Biol. 1993; 9: 541-573Crossref PubMed Scopus (1515) Google Scholar, 44MacDougall J.R. Matrisian L.M. Cancer Metastasis Rev. 1995; 14: 351-362Crossref PubMed Scopus (400) Google Scholar) and in the progression of other diseases such as arthritis, atherosclerosis, and aneurysm (3Werb Z. Alexander C.M. Kelley W.M. Harris Jr., E.D. Ruddy S. Sledge C.B. Textbook of Rheumatology. 4th Ed. W. B. Saunders Co., Philadelphia1994: 248-268Google Scholar, 45Newman K.M. Ogata Y. Malon A.M. Irizarry E. Gandhi R.H. Nagase H. Tilson M.D. Arterioscler. Thromb. 1994; 14: 1315-1320Crossref PubMed Google Scholar, 46Vincenti M.P. Clark I.M. Brinckerhoff C.E. Arthritis Rheum. 1994; 37: 1115-1126Crossref PubMed Scopus (189) Google Scholar, 47Ye S. Eriksson P. Hamsten A. Kurkinen M. Humphries S.E. Henney A.M. J. Biol. Chem. 1996; 271: 13055-13060Abstract Full Text Full Text PDF PubMed Scopus (438) Google Scholar).To study the role of ECM degradation and remodeling in early vertebrate development, we are cloning MMPs and tissue inhibitors of metalloproteinases from chicken embryos and cultured cells (17Yang M. Hayashi K. Hayashi M. Fujii J.T. Kurkinen M. J. Biol. Chem. 1996; 271: 25548-25554Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar). Here we describe the cloning and characterization of a novel member of the MMP family, called CMMP, from cultured primary chicken embryo fibroblasts. A cDNA-derived CMMP sequence contains 472 amino acids including a putative 19-residue signal peptide and a unique cysteine in the catalytic domain. A homologously placed cysteine is found only inXenopus XMMP and human MMP19, two recently cloned novel MMPs (5Cossins J. Dudgeon T.J. Catlin G. Gearing A.J.H. Clements J.M. Biochem. Biophys. Res. Commun. 1996; 228: 494-498Crossref PubMed Scopus (102) Google Scholar, 8Pendas A.M. Knauper V. Puente X.S. Llano E. Mattei M.-G. Apte S. Murphy G. Lopez-Otin C. J. Biol. Chem. 1997; 272: 4281-4286Abstract Full Text Full Text PDF PubMed Scopus (180) Google Scholar, 9Yang M. Murray M.T. Kurkinen M. J. Biol. Chem. 1997; 272: 13527-13533Abstract Full Text Full Text PDF PubMed Scopus (45) Google Scholar).Note Added in ProofWe have now found that the bacteria produced and activated full-length CMMP, and XMMP, cleave native fibrillar type I collagen into the characteristic three-quarter and one-quarter products (data not shown). Degradation and remodeling of the extracellular matrix (ECM) 1The abbreviations used are: ECM, extracellular matrix; EST, expressed sequence tag; FGF, fibroblast growth factor; IL-1, interleukin-1β; TNF, tumor necrosis factor-α; MMP, matrix metalloproteinase; MOPS, 4-morpholinepropanesulfonic acid; MT-MMP, membrane-type MMP; PCR, polymerase chain reaction; TPA, 12-O-tetradecanoylphorbol-13-acetate; bp, base pair(s); kb, kilobase pair(s). 1The abbreviations used are: ECM, extracellular matrix; EST, expressed sequence tag; FGF, fibroblast growth factor; IL-1, interleukin-1β; TNF, tumor necrosis factor-α; MMP, matrix metalloproteinase; MOPS, 4-morpholinepropanesulfonic acid; MT-MMP, membrane-type MMP; PCR, polymerase chain reaction; TPA, 12-O-tetradecanoylphorbol-13-acetate; bp, base pair(s); kb, kilobase pair(s). is thought to play important morphogenic roles during growth and development. ECM degradation is largely controlled by a superfamily of zinc-dependent endopeptidases called matrix metalloproteinases (MMPs). At present, 18 different MMPs have been cloned and characterized (1Woessner Jr., J.F. FASEB J. 1991; 5: 2145-2154Crossref PubMed Scopus (3072) Google Scholar, 2Matrisian L.M. BioEssays. 1992; 6: 121-125Google Scholar, 3Werb Z. Alexander C.M. Kelley W.M. Harris Jr., E.D. Ruddy S. Sledge C.B. Textbook of Rheumatology. 4th Ed. W. B. Saunders Co., Philadelphia1994: 248-268Google Scholar, 4Birkedal-Hansen H. Curr. Opin. Cell Biol. 1995; 7: 728-735Crossref PubMed Scopus (974) Google Scholar, 5Cossins J. Dudgeon T.J. Catlin G. Gearing A.J.H. Clements J.M. Biochem. Biophys. Res. Commun. 1996; 228: 494-498Crossref PubMed Scopus (102) Google Scholar, 6Stolov M.A. Bauzon D.D. Li J. Sedgwick T. Liang V.C.-T. Sang Q.A. Shi Y.-B. Mol. Biol. Cell. 1996; 7: 1471-1483Crossref PubMed Scopus (125) Google Scholar, 7Bartlett J.D. Simmer J.P. Xue J. Margolis H.C. Moreno E.C. Gene ( Amst. ). 1996; 183: 123-128Crossref PubMed Scopus (176) Google Scholar, 8Pendas A.M. Knauper V. Puente X.S. Llano E. Mattei M.-G. Apte S. Murphy G. Lopez-Otin C. J. Biol. Chem. 1997; 272: 4281-4286Abstract Full Text Full Text PDF PubMed Scopus (180) Google Scholar), including a novel MMP that we cloned from the frog Xenopus laevis embryos (9Yang M. Murray M.T. Kurkinen M. J. Biol. Chem. 1997; 272: 13527-13533Abstract Full Text Full Text PDF PubMed Scopus (45) Google Scholar). MMPs share similar domains with distinct structure and function, have wide and often overlapping substrate specificities, and are usually grouped as collagenases, gelatinases, stromelysins, and membrane-type MMPs. Collagenases are the only enzymes that can cleave the triple helical regions of interstitial fibrillar collagens such as collagen types I, II, and III, the most abundant proteins in the body. The cleavage occurs at one specific peptide bond, Gly775–Ile776 (Leu776 in the α2(I)-chain) in type I collagen and leads to unfolding and denaturation of the fibrillar collagens. Gelatinases A and B, also known as 72- and 92-kDa type IV collagenases, digest denatured collagen (gelatin) and components of basement membranes, a special type of ECM of epithelial, endothelial, fat, muscle, and peripheral nerve cells (10Martin G.R. Timpl R. Kuhn K. Adv. Prot. Chem. 1988; 39: 1-50Crossref PubMed Scopus (114) Google Scholar). Stromelysins are three different MMPs with wide substrate specificity, and stromelysin-1 can degrade almost any ECM component including cartilage proteoglycans (11Bonassar L.J. Frank E.H. Murray J.C. Paguio C.G. Moore V.L. Lark M.W. Sandy J.D. Wu J.J. Eyre D.R. Grodzinsky A.J. Arthritis Rheum. 1995; 38: 173-183Crossref PubMed Scopus (140) Google Scholar). Recently, four new members of the MMP family called membrane-type MMPs (MT-MMPs) were cloned (12Sato H. Takino T. Okada Y. Cao J. Shinagawa A. Yamamoto E. Seiki M. Nature. 1994; 370: 61-65Crossref PubMed Scopus (2365) Google Scholar, 13Okada A. Bellocq J.-P. Royer N. Chenard M.-P. Rio M.-C. Chambon P. Basset P. Proc. Natl. Acad. Sci. U. S. A. 1995; 92: 2730-2734Crossref PubMed Scopus (486) Google Scholar, 14Will H. Hinzmann B. Eur. J. Biochem. 1995; 231: 602-608Crossref PubMed Scopus (317) Google Scholar, 15Takino T. Sato H. Shinagawa A. Seiki M. J. Biol. Chem. 1995; 270: 23013-23020Abstract Full Text Full Text PDF PubMed Scopus (447) Google Scholar, 16Puente X.S. Pendas A.M. Liano E. Velasco G. Lopez-Otin C. Cancer Res. 1996; 56: 944-949PubMed Google Scholar, 17Yang M. Hayashi K. Hayashi M. Fujii J.T. Kurkinen M. J. Biol. Chem. 1996; 271: 25548-25554Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar). They are not secreted extracellularly but remain on the cell surface through their carboxyl-terminal transmembrane domain. Recently, however, Matsumoto et al. (18Matsumoto S. Katoh M. Saito S. Watanabe T. Masuho Y. Biochim. Biophys. Acta. 1997; 1354: 159-170Crossref PubMed Scopus (87) Google Scholar) characterized a secreted form of MT3-MMP encoded by an alternatively spliced mRNA. MT-MMPs degrade ECM components, proteolytically cleave and activate 72-kDa type IV collagenase, and therefore may regulate pericellular matrix degradation at the cell surface (19Pei D. Weiss S.J. J. Biol. Chem. 1996; 271: 9135-9140Abstract Full Text Full Text PDF PubMed Scopus (364) Google Scholar, 20Cao J. Rehemtulla A. Bahou W. Zucker S. J. Biol. Chem. 1996; 271: 30174-30180Abstract Full Text Full Text PDF PubMed Scopus (101) Google Scholar, 21Ohuchi E. Imai K. Fujii Y. Sato H. Seiki M. Okada Y. J. Biol. Chem. 1997; 272: 2446-2451Abstract Full Text Full Text PDF PubMed Scopus (827) Google Scholar). MMPs are produced as inactive precursors, which are activated by proteolytic removal of their amino-terminal domain, a 78–178-residue-long propeptide (22Strongin A.Y. Collier I. Bannikov G. Marmer B.L. Grant G.A. Goldberg G.I. J. Biol. Chem. 1995; 270: 5331-5338Abstract Full Text Full Text PDF PubMed Scopus (1434) Google Scholar, 23Pei D. Weiss S.J. Nature. 1995; 375: 244-247Crossref PubMed Scopus (530) Google Scholar, 24Benbow U. Butticé G. Nagase H. Kurkinen M. J. Biol. Chem. 1996; 271: 10715-10722Abstract Full Text Full Text PDF PubMed Scopus (24) Google Scholar). Thus, it is striking that stromelysin-1 (MMP3) proteolytically activates at least five other members of the MMP family including interstitial collagenase-1 (MMP1), matrilysin (MMP7), neutrophil collagenase-2 (MMP8), 92-kDa type IV collagenase (MMP9), and collagenase-3 (MMP13), suggesting that stromelysin-1 plays a special “upstream” role in ECM degradation and remodeling (25Murphy G. Cockett M.I. Stephens P.E. Smith B.J. Docherty A.J.P. Biochem. J. 1987; 248: 265-268Crossref PubMed Scopus (390) Google Scholar, 26Ogata Y. Enghild J.J. Nagase H. J. Biol. Chem. 1992; 267: 3581-3584Abstract Full Text PDF PubMed Google Scholar, 27Imai K. Yokohama Y. Nakanishi I. Ohuchi E. Fujii Y. Nakai N. Okada Y. J. Biol. Chem. 1995; 270: 6691-6697Abstract Full Text Full Text PDF PubMed Scopus (264) Google Scholar, 28Knauper V. Wilhelm S.M. Seperack P.K. DeClerck Y.A. Langley K.E. Osthues A. Tschesche H. Biochem. J. 1993; 295: 581-586Crossref PubMed Scopus (152) Google Scholar, 29Knauper V. Lopez-Otin C. Smith B. Knight G. Murphy G. J. Biol. Chem. 1996; 271: 1544-1558Abstract Full Text Full Text PDF PubMed Scopus (782) Google Scholar). Recently, Okamoto et al. (30Okamoto T. Akaike T. Suga M. Tanase S. Horie H. Miyajima S. Ando M. Ichinose Y. Maeda H. J. Biol. Chem. 1997; 272: 6059-6066Abstract Full Text Full Text PDF PubMed Scopus (139) Google Scholar) reported that various bacterial proteinases can also activate MMP1, MMP2, and MMP9. MMPs are expressed widely during embryogenesis, often in a highly tissue- and cell-specific pattern, suggesting distinct roles for MMPs in growth and development (17Yang M. Hayashi K. Hayashi M. Fujii J.T. Kurkinen M. J. Biol. Chem. 1996; 271: 25548-25554Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar, 31Brenner C.A. Adler R.R. Rappolee D.A. Pedersen R.A. Werb Z. Genes Dev. 1989; 3: 848-859Crossref PubMed Scopus (239) Google Scholar, 32Mattot V. Raes M.B. Henriet P. Eeckhout Y. Stehelin D. Vandenbunder B. Desbiens X. J. Cell Sci. 1995; 108: 529-535Crossref PubMed Google Scholar, 33Gack S. Vallon R. Schmidt J. Grigoriadis A. Tuckermann J. Schenkel J. Wiher H. Wagner E.F. Angel P. Cell Growth Differ. 1995; 6: 759-767PubMed Google Scholar, 34Witty J.P. Wright J.H. Matrisian L.M. Mol. Biol. Cell. 1995; 6: 1287-1303Crossref PubMed Scopus (169) Google Scholar, 35Reponen P. Sahlberg C. Munaut C. Thesleff I. Tryggvason K. J. Cell Biol. 1994; 124: 1091-1102Crossref PubMed Scopus (249) Google Scholar, 36Canete-Soler R. Gui Y.-H. Linask K.K. Muschel R.J. Dev. Dyn. 1995; 204: 30-40Crossref PubMed Scopus (54) Google Scholar, 37Sato T. del Carmen Ovejero M. Heegaard A.-M. Kumegawa M. Foged N.T. Delaisse J.-M. J. Cell Sci. 1997; 110: 589-596Crossref PubMed Google Scholar). In adult life, MMPs are rarely expressed except in rapidly remodeling tissues such as the term placenta, menstrual endometrium, and involuting mammary glands and during wound healing and inflammation (38Belaaouaj A. Shipley J.M. Kobayashi D.K. Zimonjic D.B. Popescu N. Silverman G.A. Shapiro S.D. J. Biol. Chem. 1995; 270: 14568-14575Abstract Full Text Full Text PDF PubMed Scopus (137) Google Scholar, 39Boudreau N. Sympson C.J. Werb Z. Bissell M.J. Science. 1995; 267: 891-893Crossref PubMed Scopus (1113) Google Scholar, 40Kokorine I. Marbaix E. Henriet P. Okada Y. Donnez J. Eeckhout Y. Courtoy P.J. J. Cell Sci. 1996; 109: 2151-21608PubMed Google Scholar, 41Rodgers W.H. Matrisian L.M. Giudice L.L. Dsupin N. Cannon P. Svitek C. Gorstein F. Osteen K.G. J. Clin. Invest. 1994; 94: 946-953Crossref PubMed Scopus (358) Google Scholar, 42Okada A. Tomasetto C. Lutz Y. Bellocq J.-P. Rio M.-C. Basset P. J. Cell Biol. 1997; 137: 67-77Crossref PubMed Scopus (192) Google Scholar). MMPs are also thought to play a critical role in tumor growth and metastasis (43Stetler-Stevenson W.G. Aznavoorian S. Liotta L.A. Annu. Rev. Cell Biol. 1993; 9: 541-573Crossref PubMed Scopus (1515) Google Scholar, 44MacDougall J.R. Matrisian L.M. Cancer Metastasis Rev. 1995; 14: 351-362Crossref PubMed Scopus (400) Google Scholar) and in the progression of other diseases such as arthritis, atherosclerosis, and aneurysm (3Werb Z. Alexander C.M. Kelley W.M. Harris Jr., E.D. Ruddy S. Sledge C.B. Textbook of Rheumatology. 4th Ed. W. B. Saunders Co., Philadelphia1994: 248-268Google Scholar, 45Newman K.M. Ogata Y. Malon A.M. 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A cDNA-derived CMMP sequence contains 472 amino acids including a putative 19-residue signal peptide and a unique cysteine in the catalytic domain. A homologously placed cysteine is found only inXenopus XMMP and human MMP19, two recently cloned novel MMPs (5Cossins J. Dudgeon T.J. Catlin G. Gearing A.J.H. Clements J.M. Biochem. Biophys. Res. Commun. 1996; 228: 494-498Crossref PubMed Scopus (102) Google Scholar, 8Pendas A.M. Knauper V. Puente X.S. Llano E. Mattei M.-G. Apte S. Murphy G. Lopez-Otin C. J. Biol. Chem. 1997; 272: 4281-4286Abstract Full Text Full Text PDF PubMed Scopus (180) Google Scholar, 9Yang M. Murray M.T. Kurkinen M. J. Biol. Chem. 1997; 272: 13527-13533Abstract Full Text Full Text PDF PubMed Scopus (45) Google Scholar). Note Added in ProofWe have now found that the bacteria produced and activated full-length CMMP, and XMMP, cleave native fibrillar type I collagen into the characteristic three-quarter and one-quarter products (data not shown). We have now found that the bacteria produced and activated full-length CMMP, and XMMP, cleave native fibrillar type I collagen into the characteristic three-quarter and one-quarter products (data not shown). We thank Michael Hagen for the synthesis of many oligodeoxynucleotides; Amy Sang for the sequence ofXenopus collagenase-4 prior to publication; and Irina Massova, Shahriar Mobashery, Minoru S. H. Ko, and Hideaki Nagase for help and comments on the manuscript. Special thanks are due to Anton Scott Goustin for helpful discussions and for Fig. 4." @default.
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W1982146541 date "1998-07-01" @default.
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W1982146541 title "Cloning and Characterization of a Novel Matrix Metalloproteinase (MMP), CMMP, from Chicken Embryo Fibroblasts" @default.
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