메뉴 건너뛰기




Volumn 29, Issue 10, 1999, Pages 883-897

Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta

Author keywords

Epithelia; Extracellular matrix; Morphogenesis; Multiple domains; Proteinase inhibitor

Indexed keywords

IMMUNOGLOBULIN; LACUNIN PROTEIN; MONOCLONAL ANTIBODY; SCLEROPROTEIN; SERINE PROTEINASE INHIBITOR; THROMBOSPONDIN 1;

EID: 0033214761     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(99)00064-8     Document Type: Article
Times cited : (63)

References (43)
  • 1
    • 0030589664 scopus 로고    scopus 로고
    • The extracellular matrix in epithelial biology: Shared molecules and common themes in distant phyla
    • Ashkenas J., Muschler J., Bissell M.J. The extracellular matrix in epithelial biology: shared molecules and common themes in distant phyla. Dev. Biol. 180:1996;433-444.
    • (1996) Dev. Biol. , vol.180 , pp. 433-444
    • Ashkenas, J.1    Muschler, J.2    Bissell, M.J.3
  • 2
    • 0025705858 scopus 로고
    • Syndecan, a developmentally regulated cell surface proteoglycan that binds extracellular matrix and growth factors
    • Bernfield M., Sanderson R.D. Syndecan, a developmentally regulated cell surface proteoglycan that binds extracellular matrix and growth factors. Phil. Trans. R. Soc. Lond. B 327:1990;171-186.
    • (1990) Phil. Trans. R. Soc. Lond. , vol.327 , pp. 171-186
    • Bernfield, M.1    Sanderson, R.D.2
  • 3
    • 0002830044 scopus 로고
    • Remodeling of the basement membrane as a mechanism of morphogenetic tissue interaction
    • R.L. Trelstad. New York: Alan R. Liss
    • Bernfield M., Banerjee S.D., Koda J.E., Rapraeger A.C. Remodeling of the basement membrane as a mechanism of morphogenetic tissue interaction. Trelstad R.L. The Role of Extracellular Matrix in Development. 1984;545-572 Alan R. Liss, New York.
    • (1984) The Role of Extracellular Matrix in Development , pp. 545-572
    • Bernfield, M.1    Banerjee, S.D.2    Koda, J.E.3    Rapraeger, A.C.4
  • 5
    • 0011832293 scopus 로고
    • Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins
    • Bourdon M.A., Krusius T., Campbell S., Schwartz N.B., Ruoslahti E. Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins. Proc. Natl. Acad. Sci. USA. 84:1987;3194-3198.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3194-3198
    • Bourdon, M.A.1    Krusius, T.2    Campbell, S.3    Schwartz, N.B.4    Ruoslahti, E.5
  • 6
    • 0025832875 scopus 로고
    • Quantitative staging of embryonic development of the tobacco hawkmoth Manduca sexta
    • Broadie K.S., Bate M., Tublitz N.J. Quantitative staging of embryonic development of the tobacco hawkmoth Manduca sexta. Roux's Arch. Dev. Biol. 199:1991;327-334.
    • (1991) Roux's Arch. Dev. Biol. , vol.199 , pp. 327-334
    • Broadie, K.S.1    Bate, M.2    Tublitz, N.J.3
  • 7
    • 0031051846 scopus 로고    scopus 로고
    • Neuroglian is expressed on cells destined to form the prothoracic glands of Manduca embryos as they segregate from surrounding cells and rearrange during morphogenesis
    • Chen C.-L., Lampe D.J., Robertson H.M., Nardi J.B. Neuroglian is expressed on cells destined to form the prothoracic glands of Manduca embryos as they segregate from surrounding cells and rearrange during morphogenesis. Dev. Biol. 181:1997;1-13.
    • (1997) Dev. Biol. , vol.181 , pp. 1-13
    • Chen, C.-L.1    Lampe, D.J.2    Robertson, H.M.3    Nardi, J.B.4
  • 8
    • 0030959540 scopus 로고    scopus 로고
    • CDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    • Colige A., Li S.W., Sieron A.L., Nusgens B.V., Prockop D.J., Lapiere C.M. cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc. Natl. Acad. Sci. USA. 94:1997;2374-2379.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2374-2379
    • Colige, A.1    Li, S.W.2    Sieron, A.L.3    Nusgens, B.V.4    Prockop, D.J.5    Lapiere, C.M.6
  • 9
    • 84940914843 scopus 로고
    • Teratocytes: Developmental and biochemical characteristics
    • N.E. Beckage, S.N. Thompson, & B.A. Federici. San Diego: Academic Press
    • Dahlman D.L., Vinson S.B. Teratocytes: developmental and biochemical characteristics. Beckage N.E., Thompson S.N., Federici B.A. Parasites and Pathogens of Insects. 1993;145-165 Academic Press, San Diego.
    • (1993) Parasites and Pathogens of Insects , pp. 145-165
    • Dahlman, D.L.1    Vinson, S.B.2
  • 10
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle R.F. The multiplicity of domains in proteins. Annu. Rev. Biochem. 64:1995;287-314.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 11
    • 0031560771 scopus 로고    scopus 로고
    • Solution structure of R-elafin, a specific inhibitor of elastase
    • Francart C., Dauchez M., Alix A.J., Lippens G. Solution structure of R-elafin, a specific inhibitor of elastase. J. Mol. Biol. 268:1997;666-677.
    • (1997) J. Mol. Biol. , vol.268 , pp. 666-677
    • Francart, C.1    Dauchez, M.2    Alix, A.J.3    Lippens, G.4
  • 12
    • 0023741662 scopus 로고
    • Properdin, the terminal complement components, thrombospondin and the circumsporozoite protein of malaria parasites contain similar motifs
    • Goundis D., Reid K.B.M. Properdin, the terminal complement components, thrombospondin and the circumsporozoite protein of malaria parasites contain similar motifs. Nature. 335:1988;82-85.
    • (1988) Nature , vol.335 , pp. 82-85
    • Goundis, D.1    Reid, K.B.M.2
  • 13
    • 0024277922 scopus 로고
    • Growth cone guidance in insects: Fasciclin II is a member of the immunoglobulin superfamily
    • Harrelson A.L., Goodman C.S. Growth cone guidance in insects: Fasciclin II is a member of the immunoglobulin superfamily. Science. 242:1988;700-708.
    • (1988) Science , vol.242 , pp. 700-708
    • Harrelson, A.L.1    Goodman, C.S.2
  • 14
    • 0023188637 scopus 로고
    • Accelerated evolution in the reactive centre regions of serine protease inhibitors
    • Hill R.E., Hastie N.D. Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature. 326:1987;96-99.
    • (1987) Nature , vol.326 , pp. 96-99
    • Hill, R.E.1    Hastie, N.D.2
  • 15
    • 0030273263 scopus 로고    scopus 로고
    • The L1 family of neural cell adhesion molecules: Old proteins performing new tricks
    • Hortsch M. The L1 family of neural cell adhesion molecules: old proteins performing new tricks. Neuron. 17:1996;587-593.
    • (1996) Neuron , vol.17 , pp. 587-593
    • Hortsch, M.1
  • 16
    • 0028960136 scopus 로고
    • Antibodies against domain E3 of laminin-1 and integrin 6 subunit perturb branching epithelial morphogenesis of submandibular gland, but by different modes
    • Kadoya Y., Kadoya K., Durbeej M., Holmvall K., Sorokin L., Ekblom P. Antibodies against domain E3 of laminin-1 and integrin 6 subunit perturb branching epithelial morphogenesis of submandibular gland, but by different modes. J. Cell Biol. 129:1995;521-534.
    • (1995) J. Cell Biol. , vol.129 , pp. 521-534
    • Kadoya, Y.1    Kadoya, K.2    Durbeej, M.3    Holmvall, K.4    Sorokin, L.5    Ekblom, P.6
  • 17
    • 0026348132 scopus 로고
    • Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15
    • Kiefer M.C., Tucker J.E., Joh R., Landsberg K.E., Saltman D., Barr P.J. Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15. DNA Cell Biol. 10:1991;757-769.
    • (1991) DNA Cell Biol. , vol.10 , pp. 757-769
    • Kiefer, M.C.1    Tucker, J.E.2    Joh, R.3    Landsberg, K.E.4    Saltman, D.5    Barr, P.J.6
  • 18
    • 0031036524 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene
    • Kuno K., Kanada N., Nakashima E., Fujiki F., Ichimura F., Matsushima K. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J. Biol. Chem. 272:1997;556-562.
    • (1997) J. Biol. Chem. , vol.272 , pp. 556-562
    • Kuno, K.1    Kanada, N.2    Nakashima, E.3    Fujiki, F.4    Ichimura, F.5    Matsushima, K.6
  • 20
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49:1980;593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 22
    • 0027274628 scopus 로고
    • CDNA structure of the mouse and rat subtilisin/kexin-like PC5: A candidate proprotein convertase expressed in endocrine and nonendocrine cells
    • Lusson J., Vieau D., Hamelin J., Day R., Chretien M., Seidah N.G. cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells. Proc. Natl. Acad. Sci. USA. 90:1993;6691-6695.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6691-6695
    • Lusson, J.1    Vieau, D.2    Hamelin, J.3    Day, R.4    Chretien, M.5    Seidah, N.G.6
  • 23
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian L.M. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genetics. 6:1990;121-125.
    • (1990) Trends Genetics , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 24
    • 0028934970 scopus 로고
    • Changing distributions of extracellular matrix components during early wing morphogenesis in Drosophila
    • Murray M.A., Fessler L.I., Palka J. Changing distributions of extracellular matrix components during early wing morphogenesis in Drosophila. Dev. Biol. 168:1995;50-165.
    • (1995) Dev. Biol. , vol.168 , pp. 50-165
    • Murray, M.A.1    Fessler, L.I.2    Palka, J.3
  • 25
    • 0031589004 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • Nagase T., Ishikawa K., Nakajima D., Ohira D., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 4:1997;141-150.
    • (1997) DNA Res. , vol.4 , pp. 141-150
    • Nagase, T.1    Ishikawa, K.2    Nakajima, D.3    Ohira, D.4    Seki, N.5    Miyajima, N.6    Tanaka, A.7    Kotani, H.8    Nomura, N.9    Ohara, O.10
  • 26
    • 0032574043 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 5:1998;31-39.
    • (1998) DNA Res. , vol.5 , pp. 31-39
    • Nagase, T.1    Ishikawa, K.2    Miyajima, N.3    Tanaka, A.4    Kotani, H.5    Nomura, N.6    Ohara, O.7
  • 27
    • 0022553522 scopus 로고
    • Collagenase inhibitor stimulates cleft formation during early morphogenesis of mouse salivary gland
    • Nakanishi Y., Sugiura F., Kishi J.-I., Hayakawa T. Collagenase inhibitor stimulates cleft formation during early morphogenesis of mouse salivary gland. Dev. Biol. 113:1986;201206.
    • (1986) Dev. Biol. , vol.113 , pp. 201206
    • Nakanishi, Y.1    Sugiura, F.2    Kishi, J.-I.3    Hayakawa, T.4
  • 28
    • 38249039316 scopus 로고
    • Formation of scale spacing patterns in a moth wing. I. Epithelial feet may mediate cell rearrangement
    • Nardi J.B., Magee-Adams S.M. Formation of scale spacing patterns in a moth wing. I. Epithelial feet may mediate cell rearrangement. Dev. Biol. 116:1986;278-290.
    • (1986) Dev. Biol. , vol.116 , pp. 278-290
    • Nardi, J.B.1    Magee-Adams, S.M.2
  • 29
    • 0000563590 scopus 로고
    • Hemocytes contribute to both the formation and breakdown of the basal lamina in developing wings of Manduca sexta
    • Nardi J.B., Miklasz S.D. Hemocytes contribute to both the formation and breakdown of the basal lamina in developing wings of Manduca sexta. Tissue Cell. 21:1989;559-567.
    • (1989) Tissue Cell , vol.21 , pp. 559-567
    • Nardi, J.B.1    Miklasz, S.D.2
  • 30
    • 0027327807 scopus 로고
    • Modulated expression of a surface epitope on migrating germ cells of Manduca sexta embryos
    • Nardi J.B. Modulated expression of a surface epitope on migrating germ cells of Manduca sexta embryos. Development. 118:1993;967-975.
    • (1993) Development , vol.118 , pp. 967-975
    • Nardi, J.B.1
  • 31
    • 0028215280 scopus 로고
    • Rearrangement of epithelial cell types in an insect wing monolayer is accompanied by differential expression of a cell surface protein
    • Nardi J.B. Rearrangement of epithelial cell types in an insect wing monolayer is accompanied by differential expression of a cell surface protein. Dev. Dynamics. 199:1994;315-325.
    • (1994) Dev. Dynamics , vol.199 , pp. 315-325
    • Nardi, J.B.1
  • 32
    • 0024245150 scopus 로고
    • Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo
    • O'Shea K.S., Dixit V.M. Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo. J. Cell Biol. 107:1988;2737-2748.
    • (1988) J. Cell Biol. , vol.107 , pp. 2737-2748
    • O'Shea, K.S.1    Dixit, V.M.2
  • 33
    • 0024542077 scopus 로고
    • Extracellular protease production by Drosophila imaginal discs
    • Pino-Heiss S., Schubiger G. Extracellular protease production by Drosophila imaginal discs. Dev. Biol. 132:1989;282-291.
    • (1989) Dev. Biol. , vol.132 , pp. 282-291
    • Pino-Heiss, S.1    Schubiger, G.2
  • 34
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S., Wells R., Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science. 234:1986;364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 35
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E., Pierschbacher M.D. New perspectives in cell adhesion: RGD and integrins. Science. 238:1987;491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 37
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions
    • Sage E.H., Bornstein P. Extracellular proteins that modulate cell-matrix interactions. J. Biol. Chem. 266:1991;14831-14834.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 38
    • 0001655851 scopus 로고
    • Biology and mechanisms of insect-cuticle invasion by deuteromycete fungal pathogens
    • N.E. Beckage, S.N. Thompson, & B.A. Federici. San Diego: Academic Press
    • St. Leger R. Biology and mechanisms of insect-cuticle invasion by deuteromycete fungal pathogens. Beckage N.E., Thompson S.N., Federici B.A. Parasites and Pathogens of Insects. 1993;211-229 Academic Press, San Diego.
    • (1993) Parasites and Pathogens of Insects , pp. 211-229
    • St. Leger, R.1
  • 39
    • 0021856417 scopus 로고
    • Signal sequences: The limits of variation
    • von Heijne G. Signal sequences: the limits of variation. J. Mol. Biol. 184:1985;99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 41
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily - Domains for cell surface recognition
    • Williams A.F., Barclay A.N. The immunoglobulin superfamily - domains for cell surface recognition. Annu. Rev. Immunol. 6:1988;381-405.
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 42
    • 77957074520 scopus 로고    scopus 로고
    • Internal protein sequencing of SDS-PAGE-separated proteins: Optimization of an in-gel digest protocol
    • D. Marshak. San Diego: Academic Press
    • Williams K.R., LoPresti M., Stone K.L. Internal protein sequencing of SDS-PAGE-separated proteins: Optimization of an in-gel digest protocol. Marshak D. Techniques VIII. 1997;79-90 Academic Press, San Diego.
    • (1997) Techniques VIII , pp. 79-90
    • Williams, K.R.1    Lopresti, M.2    Stone, K.L.3
  • 43
    • 77957100662 scopus 로고
    • In gel digestion of SDS-PAGE-separated proteins: Observations from internal sequencing of 25 proteins
    • J.W. Crabb. Orlando: Academic Press
    • Williams K.R., Stone K.L. In gel digestion of SDS-PAGE-separated proteins: observations from internal sequencing of 25 proteins. Crabb J.W. Techniques in Protein Chemistry VI. 1995;143-152 Academic Press, Orlando.
    • (1995) Techniques in Protein Chemistry VI , pp. 143-152
    • Williams, K.R.1    Stone, K.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.