메뉴 건너뛰기




Volumn 436, Issue 1, 2011, Pages 61-70

Function of the CysD domain of the gel-forming MUC2 mucin

Author keywords

C mannosylation; Disulfide bonds; Mass spectrometry (MS); Mucus; Non covalent dimer

Indexed keywords

MUCIN 2;

EID: 79955537785     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20102066     Document Type: Article
Times cited : (77)

References (42)
  • 1
    • 0033527547 scopus 로고    scopus 로고
    • The structure and assembly of secreted mucins
    • Perez-Vilar, J. and Hill, R. L. (1999) The structure and assembly of secreted mucins. J. Biol. Chem. 274, 31751-31754
    • (1999) J. Biol. Chem. , vol.274 , pp. 31751-31754
    • Perez-Vilar, J.1    Hill, R.L.2
  • 2
    • 43549093774 scopus 로고    scopus 로고
    • Structure and function of the polymeric mucins in airways mucus
    • DOI 10.1146/annurev.physiol.70.113006.100702
    • Thornton, D. J., Rousseau, K. and McGuckin, M. A. (2008) Structure and function of the polymeric mucins in airways mucus. Annu. Rev. Physiol. 70, 459-486 (Pubitemid 351738188)
    • (2008) Annual Review of Physiology , vol.70 , pp. 459-486
    • Thornton, D.J.1    Rousseau, K.2    McGuckin, M.A.3
  • 4
    • 0028106680 scopus 로고
    • Molecular cloning of human intestinal mucin (MUC2) cDNA. Identification of the amino terminus and overall sequence similarity to prepro-von Willebrand factor
    • Gum, J. R., Hicks, J. W., Toribara, N. W., Siddiki, B. and Kim, Y. S. (1994) Molecular cloning of human intestinal mucin (MUC2) cDNA. Identification of the amino terminus and overall sequence similarity to prepro-von Willebrand factor. J. Biol. Chem. 269, 2440-2446
    • (1994) J. Biol. Chem. , vol.269 , pp. 2440-2446
    • Gum, J.R.1    Hicks, J.W.2    Toribara, N.W.3    Siddiki, B.4    Kim, Y.S.5
  • 5
    • 0032549673 scopus 로고    scopus 로고
    • Cloning of the amino-terminal and 5'-flanking region of the human MUC5AC mucin gene and transcriptional up-regulation by bacterial exoproducts
    • DOI 10.1074/jbc.273.12.6812
    • Li, D., Gallup, M., Fan, N., Szymkowski, D. E. and Basbaum, C. B. (1998) Cloning of the amino-terminal and 5'-flanking region of the human MUC5AC mucin gene and transcriptional up-regulation by bacterial exoproducts. J. Biol. Chem. 273, 6812-6820 (Pubitemid 28160344)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 6812-6820
    • Li, D.1    Gallup, M.2    Fan, N.3    Szymkowski, D.E.4    Basbaum, C.B.5
  • 8
    • 80051619654 scopus 로고    scopus 로고
    • Cloning and characterization of human MUC19 gene
    • doi:101165/rcmb.2010-0312OC
    • Zhu, L., Lee, P., Yu, D., Tao, S. and Chen, Y. (2010) Cloning and characterization of human MUC19 gene. Am. J. Respir. Cell Mol. Biol., doi:101165/rcmb.2010-0312OC
    • (2010) Am. J. Respir. Cell Mol. Biol
    • Zhu, L.1    Lee, P.2    Yu, D.3    Tao, S.4    Chen, Y.5
  • 9
    • 0027317061 scopus 로고
    • Molecular cloning, sequence, and specificity of expression of the gene encoding the low molecular weight human salivary mucin (MUC7)
    • Bobek, L., Tsai, H., Biesbrock, A. and Levine, M. (1993) Molecular cloning, sequence, and specificity of expression of the gene encoding the low molecular weight human salivary mucin (MUC7). J. Biol. Chem. 268, 20563-20569 (Pubitemid 23278970)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.27 , pp. 20563-20569
    • Bobek, L.A.1    Tsai, H.2    Biesbrock, A.R.3    Levine, M.J.4
  • 11
    • 0032563128 scopus 로고    scopus 로고
    • Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus
    • DOI 10.1074/jbc.273.30.18857
    • Asker, N., Axelsson, M. A., Olofsson, S. O. and Hansson, G. C. (1998) Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation- dependent transfer of the mono- and dimers to the Golgi apparatus. J. Biol. Chem. 273, 18857-18863 (Pubitemid 28366272)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 18857-18863
    • Asker, N.1    Axelsson, M.A.B.2    Olofsson, S.-O.3    Hansson, G.C.4
  • 12
    • 0038677022 scopus 로고    scopus 로고
    • The recombinant C-terminus of the human MUC2 mucin forms dimers in Chinese-hamster ovary cells and heterodimers with full-length MUC2 in LS 174T cells
    • DOI 10.1042/BJ20030003
    • Lidell, M. E., Johansson, M. E., Morgelin, M., Asker, N., Gum, Jr, J. R., Kim, Y. S. and Hansson, G. C. (2003) The recombinant C-terminus of the human MUC2 mucin forms dimers in Chinese-hamster ovary cells and heterodimers with full-length MUC2 in LS 174T cells. Biochem. J. 372, 335-345 (Pubitemid 36723879)
    • (2003) Biochemical Journal , vol.372 , Issue.2 , pp. 335-345
    • Lidell, M.E.1    Johansson, M.E.V.2    Morgelin, M.3    Asker, N.4    Gum Jr., J.R.5    Kim, Y.S.6    Hansson, G.C.7
  • 14
    • 0035884708 scopus 로고    scopus 로고
    • Human mucin gene MUC5AC: Organization of its 5'-region and central repetitive region
    • DOI 10.1042/0264-6021:3580763
    • Escande, F., Aubert, J. P., Porchet, N. and Buisine, M. P. (2001) Human mucin gene MUC5AC: organization of its 5'-region and central repetitive region. Biochem. J. 358, 763-772 (Pubitemid 32896964)
    • (2001) Biochemical Journal , vol.358 , Issue.3 , pp. 763-772
    • Escande, F.1    Aubert, J.-P.2    Porchet, N.3    Buisine, M.-P.4
  • 15
    • 0031023179 scopus 로고    scopus 로고
    • Human mucin gene MUC5B, the 10.7-kb large central exon encodes various alternate subdomains resulting in a super-repeat. Structural evidence for a 11p15.5 gene family
    • Desseyn, J. L., Guyonnet-Dupérat, V., Porchet, N., Aubert, J. P. and Laine, A. (1997) Human mucin gene MUC5B, the 10.7-kb large central exon encodes various alternate subdomains resulting in a super-repeat. Structural evidence for a 11p15.5 gene family. J. Biol. Chem. 272, 3168-3178
    • (1997) J. Biol. Chem. , vol.272 , pp. 3168-3178
    • Desseyn, J.L.1    Guyonnet-Dupérat, V.2    Porchet, N.3    Aubert, J.P.4    Laine, A.5
  • 17
    • 0032483377 scopus 로고    scopus 로고
    • Cloning and deduced amino acid sequence of a novel cartilage protein (CILP) identifies a proform including a nucleotide pyrophosphohydrolase
    • DOI 10.1074/jbc.273.36.23469
    • Lorenzo, P., Neame, P., Sommarin, Y. and Heinegård, D. (1998) Cloning and deduced amino acid sequence of a novel cartilage protein (CILP) identifies a proform including a nucleotide pyrophosphohydrolase. J. Biol. Chem. 273, 23469-23475 (Pubitemid 28417538)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.36 , pp. 23469-23475
    • Lorenzo, P.1    Neame, P.2    Sommarin, Y.3    Heinegard, D.4
  • 18
    • 0035827662 scopus 로고    scopus 로고
    • Molecular patterning of the oikoplastic epithelium of the larvacean tunicate Oikopleura dioica
    • Spada, F., Steen, H., Troedsson, C., Kallesoe, T., Spriet, E., Mann, M. and Thompson, E. M. (2001) Molecular patterning of the oikoplastic epithelium of the larvacean tunicate Oikopleura dioica. J. Biol. Chem. 276, 20624-20632
    • (2001) J. Biol. Chem. , vol.276 , pp. 20624-20632
    • Spada, F.1    Steen, H.2    Troedsson, C.3    Kallesoe, T.4    Spriet, E.5    Mann, M.6    Thompson, E.M.7
  • 19
    • 9544222719 scopus 로고    scopus 로고
    • Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms
    • DOI 10.1021/bi9610515
    • Löftier, A., Doucey, M. A., Jansson, A. M., Müller, D. R., de Beer, T., Hess, D., Meldal, M., Richter, W. J., Vliegenthart, J. F. and Hofsteenge, J. (1996) Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms. Biochemistry 35, 12005-12014 (Pubitemid 26313671)
    • (1996) Biochemistry , vol.35 , Issue.37 , pp. 12005-12014
    • Loffler, A.1    Doucey, M.-A.2    Jansson, A.M.3    Muller, D.R.4    De Beer, T.5    Hess, D.6    Meldal, M.7    Richter, W.J.8    Vliegenthart, J.F.G.9    Hofsteenge, J.10
  • 20
    • 2442519149 scopus 로고    scopus 로고
    • C-Mannosylation of MUC5AC and MUC5B Cyssubdomains
    • Perez-Vilar, J., Randell, S. H. and Boucher, R. C. (2004) C-Mannosylation of MUC5AC and MUC5B Cyssubdomains. Glycobiology 14, 325-337
    • (2004) Glycobiology , vol.14 , pp. 325-337
    • Perez-Vilar, J.1    Randell, S.H.2    Boucher, R.C.3
  • 22
    • 0019493512 scopus 로고
    • Selection of specific wheat germ agglutinin-resistant (Wga(R)) phenotypes from Chinese hamster ovary cell populations containing numerous lec(R) genotypes
    • Stanley, P. (1981) Selection of specific wheat germ agglutinin-resistant (WgaR) phenotypes from Chinese hamster ovary cell populations containing numerous lecR genotypes. Mol. Cell. Biol. 1, 687-696 (Pubitemid 11055766)
    • (1981) Molecular and Cellular Biology , vol.1 , Issue.8 , pp. 687-696
    • Stanley, P.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Lümmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Lümmli, U.K.1
  • 25
    • 0029075044 scopus 로고
    • A silver stain protocol for proteins yielding high resolution and transparent background in sodium dodecyl sulfate-polyacrylamide gels
    • Swain, M. and Ross, N. W. (1995) A silver stain protocol for proteins yielding high resolution and transparent background in sodium dodecyl sulfate-polyacrylamide gels. Electrophoresis 16, 948-951
    • (1995) Electrophoresis , vol.16 , pp. 948-951
    • Swain, M.1    Ross, N.W.2
  • 27
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schügger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schügger, H.1    Von Jagow, G.2
  • 28
    • 34247371926 scopus 로고    scopus 로고
    • Large scale identification of proteins, mucins and their O-glycosylation in the endocervical mucus during the menstrual cycle
    • DOI 10.1074/mcp.M600439-MCP200
    • Andersch-Bjürkman, Y., Thomsson, K. A., Holmén Larsson, J. M., Ekerhovd, E. and Hansson, G. C. (2007) Large scale identification of proteins, mucins, and their O-glycosylation in the endocervical mucus during the menstrual cycle. Mol. Cell. Proteomics 6, 708-716 (Pubitemid 46630103)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.4 , pp. 708-716
    • Andersch-Bjorkman, Y.1    Thomsson, K.A.2    Holmen Larsson, J.M.3    Ekerhovd, E.4    Hansson, G.C.5
  • 29
    • 77952027769 scopus 로고    scopus 로고
    • XComb: A cross-linked peptide database approach to protein-protein interaction analysis
    • Panchaud, A., Singh, P., Shaffer, S. A. and Goodlett, D. R. (2010) xComb: a cross-linked peptide database approach to protein-protein interaction analysis. J. Proteome Res. 9, 2508-2515
    • (2010) J. Proteome Res. , vol.9 , pp. 2508-2515
    • Panchaud, A.1    Singh, P.2    Shaffer, S.A.3    Goodlett, D.R.4
  • 30
    • 0031017896 scopus 로고    scopus 로고
    • Refined structure of an intact IgG2a monoclonal antibody
    • DOI 10.1021/bi962514+
    • Harris, L. J., Larson, S. B., Hasel, K. W. and McPherson, A. (1997) Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 36, 1581-1597 (Pubitemid 27086254)
    • (1997) Biochemistry , vol.36 , Issue.7 , pp. 1581-1597
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    McPherson, A.4
  • 31
    • 0013801195 scopus 로고
    • The gel-filtration behaviour of proteins related to their molecular weights over a wide range
    • Andrews, P. (1965) The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem. J. 96, 595-606
    • (1965) Biochem. J. , vol.96 , pp. 595-606
    • Andrews, P.1
  • 32
    • 0018098440 scopus 로고
    • Gel filtration of sialoglycoproteins
    • Alhadeff, J. A. (1978) Gel filtration of sialoglycoproteins. Biochem. J. 173, 315-319 (Pubitemid 8368306)
    • (1978) Biochemical Journal , vol.173 , Issue.1 , pp. 315-319
    • Alhadeff, J.A.1
  • 33
    • 70450286979 scopus 로고    scopus 로고
    • Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan
    • Wang, L. W., Leonhard-Melief, C., Haltiwanger, R. S. and Apte, S. S. (2009) Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan. J. Biol. Chem. 284, 30004-300015
    • (2009) J. Biol. Chem. , vol.284 , pp. 30004-300015
    • Wang, L.W.1    Leonhard-Melief, C.2    Haltiwanger, R.S.3    Apte, S.S.4
  • 34
    • 1842413048 scopus 로고    scopus 로고
    • C-mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells
    • DOI 10.1074/jbc.272.42.26687
    • Krieg, J., Glüsner, W., Vicentini, A., Doucey, M. A., Löffler, A., Hess, D. and Hofsteenge, J. (1997) C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells. J. Biol. Chem. 272, 26687-26692 (Pubitemid 27458894)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.42 , pp. 26687-26692
    • Krieg, J.1    Glasner, W.2    Vicentini, A.3    Doucey, M.-A.4    Loffler, A.5    Hess, D.6    Hofsteenge, J.7
  • 36
    • 0031941594 scopus 로고    scopus 로고
    • Mechanism of acidification of the trans-Golgi network (TGN): In situ measurements of pH using retrieval of TGN38 and furin from the cell surface
    • DOI 10.1074/jbc.273.4.2044
    • Demaurex, N., Furuya, W., D'Souza, S., Bonifacino, J. S. and Grinstein, S. (1998) Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface. J. Biol. Chem. 273, 2044-2051 (Pubitemid 28069251)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 2044-2051
    • Demaurex, N.1    Furuya, W.2    D'Souza, S.3    Bonifacino, J.S.4    Grinstein, S.5
  • 37
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • DOI 10.1038/28190
    • Miesenbock, G., De Angelis, D. A. and Rothman, J. E. (1998) Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394, 192-195 (Pubitemid 28325974)
    • (1998) Nature , vol.394 , Issue.6689 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 40
    • 0026802436 scopus 로고
    • The human MUC2 intestinal mucin has cysteine-rich subdomains located both upstream and downstream of its central repetitive region
    • Gum, Jr, J. R., Hicks, J. W., Toribara, N. W., Rothe, E. M., Lagace, R. E. and Kim, Y. S. (1992) The human MUC2 intestinal mucin has cysteine-rich subdomains located both upstream and downstream of its central repetitive region. J. Biol. Chem. 267, 21375-21383
    • (1992) J. Biol. Chem. , vol.267 , pp. 21375-21383
    • Gum Jr., J.R.1    Hicks, J.W.2    Toribara, N.W.3    Rothe, E.M.4    Lagace, R.E.5    Kim, Y.S.6
  • 42
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • Hollingsworth, M. A. and Swanson, B. J. (2004) Mucins in cancer: protection and control of the cell surface. Nat. Rev. Cancer 4, 45-60 (Pubitemid 38082153)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.1 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.