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Volumn 22, Issue 1, 2015, Pages 112-116

Studies on the role of goat heart galectin-1 as an erythrocyte membrane perturbing agent

Author keywords

Agglutination; Erythrocyte; Goat heart galectin 1; Hemolysis; Membrane

Indexed keywords

CAPRA HIRCUS; ORYCTOLAGUS CUNICULUS;

EID: 84919675144     PISSN: 1319562X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sjbs.2014.09.018     Document Type: Article
Times cited : (15)

References (22)
  • 1
    • 15844399859 scopus 로고    scopus 로고
    • A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins
    • Armstrong P.B., Swarnakar S., Srimal S., Misquith S., Hahn E.A., Aimes R.T., Quigley J.P. A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins. J. Biol. Chem. 1996, 271:14717-14721.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14717-14721
    • Armstrong, P.B.1    Swarnakar, S.2    Srimal, S.3    Misquith, S.4    Hahn, E.A.5    Aimes, R.T.6    Quigley, J.P.7
  • 2
    • 79551552767 scopus 로고    scopus 로고
    • Purification, characterization, sequencing and biological chemistry of galectin-1 purified from Capra hircus (goat) heart
    • Ashraf G.M., Banu N., Ahmad A., Singh L.P., Kumar R. Purification, characterization, sequencing and biological chemistry of galectin-1 purified from Capra hircus (goat) heart. Protein J. 2011, 30:39-51.
    • (2011) Protein J. , vol.30 , pp. 39-51
    • Ashraf, G.M.1    Banu, N.2    Ahmad, A.3    Singh, L.P.4    Kumar, R.5
  • 3
    • 79251582492 scopus 로고    scopus 로고
    • Glycosylation of purified buffalo heart galectin-1 plays crucial role in maintaining its structural and functional integrity
    • Ashraf G.M., Bilal N., Suhail N., Hasan S., Banu N. Glycosylation of purified buffalo heart galectin-1 plays crucial role in maintaining its structural and functional integrity. Biochemistry 2010, 75:1450-1457.
    • (2010) Biochemistry , vol.75 , pp. 1450-1457
    • Ashraf, G.M.1    Bilal, N.2    Suhail, N.3    Hasan, S.4    Banu, N.5
  • 4
    • 78449269803 scopus 로고    scopus 로고
    • Purification, characterization, structural analysis and protein chemistry of a buffalo heart galectin-1
    • Ashraf G.M., Rizvi S., Naqvi S., Suhail N., Bilal N., Hasan S., Tabish M., Banu N. Purification, characterization, structural analysis and protein chemistry of a buffalo heart galectin-1. Amino Acids 2010, 39:1321-1332.
    • (2010) Amino Acids , vol.39 , pp. 1321-1332
    • Ashraf, G.M.1    Rizvi, S.2    Naqvi, S.3    Suhail, N.4    Bilal, N.5    Hasan, S.6    Tabish, M.7    Banu, N.8
  • 5
    • 0022571049 scopus 로고
    • Leak formation in human erythrocytes by the radical-forming oxidant t-butylhydroperoxide
    • Deuticke B., Heller K.B., Haest C.W. Leak formation in human erythrocytes by the radical-forming oxidant t-butylhydroperoxide. Biochim. Biophys. Acta 1986, 854:169-183.
    • (1986) Biochim. Biophys. Acta , vol.854 , pp. 169-183
    • Deuticke, B.1    Heller, K.B.2    Haest, C.W.3
  • 6
    • 33344475311 scopus 로고    scopus 로고
    • Carbohydrate-induced modulation of cell membrane. VIII. Agglutination with mammalian lectin galectin-1 increases osmofragility and membrane fluidity of trypsinized erythrocytes
    • Gupta R.K., Pande A.H., Gulla K.C., Gabius H.-J., Hajela K. Carbohydrate-induced modulation of cell membrane. VIII. Agglutination with mammalian lectin galectin-1 increases osmofragility and membrane fluidity of trypsinized erythrocytes. FEBS Lett. 2006, 580:1691-1695.
    • (2006) FEBS Lett. , vol.580 , pp. 1691-1695
    • Gupta, R.K.1    Pande, A.H.2    Gulla, K.C.3    Gabius, H.-J.4    Hajela, K.5
  • 7
    • 34249978481 scopus 로고    scopus 로고
    • Galectins - potential targets for cancer therapy
    • Hasan S.S., Ashraf G.M., Banu N. Galectins - potential targets for cancer therapy. Cancer Lett. 2007, 253:25-33.
    • (2007) Cancer Lett. , vol.253 , pp. 25-33
    • Hasan, S.S.1    Ashraf, G.M.2    Banu, N.3
  • 8
    • 0028967311 scopus 로고
    • Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane
    • Hatakeyama T., Nagatomo H., Yamasaki N. Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane. J. Biol. Chem. 1995, 270:3560-3564.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3560-3564
    • Hatakeyama, T.1    Nagatomo, H.2    Yamasaki, N.3
  • 10
    • 84880502526 scopus 로고    scopus 로고
    • Immune-related transcriptome of Coptotermes formosanus Shiraki workers: the defense mechanism
    • Hussain A., Li Y.-F., Cheng Y., Liu Y., Chen C.-C., Wen S.-Y. Immune-related transcriptome of Coptotermes formosanus Shiraki workers: the defense mechanism. PLoS One 2013, 8.
    • (2013) PLoS One , vol.8
    • Hussain, A.1    Li, Y.-F.2    Cheng, Y.3    Liu, Y.4    Chen, C.-C.5    Wen, S.-Y.6
  • 11
    • 0017750496 scopus 로고
    • Refinement of the fluid-mosaic model of membrane structure
    • Israelachvili J.N. Refinement of the fluid-mosaic model of membrane structure. Biochim. Biophys. Acta 1977, 469:221-225.
    • (1977) Biochim. Biophys. Acta , vol.469 , pp. 221-225
    • Israelachvili, J.N.1
  • 12
    • 84898428911 scopus 로고    scopus 로고
    • Identification of immunity-related genes in Ostrinia furnacalis against entomopathogenic fungi by RNA-seq analysis
    • Liu Y., Shen D., Zhou F., Wang G., An C. Identification of immunity-related genes in Ostrinia furnacalis against entomopathogenic fungi by RNA-seq analysis. PLoS One 2014, 9.
    • (2014) PLoS One , vol.9
    • Liu, Y.1    Shen, D.2    Zhou, F.3    Wang, G.4    An, C.5
  • 13
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • Lowe J.B., Marth J.D. A genetic approach to mammalian glycan function. Annu. Rev. Biochem. 2003, 72:643-691.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 15
    • 0032079989 scopus 로고    scopus 로고
    • Carbohydrate induced modulation of cell membrane VII. Binding of exogenous lectin increases osmofragility of erythrocytes
    • Pande A.H., Sumati, Hajela N., Hajela K. Carbohydrate induced modulation of cell membrane VII. Binding of exogenous lectin increases osmofragility of erythrocytes. FEBS Lett. 1998, 427:21-24.
    • (1998) FEBS Lett. , vol.427 , pp. 21-24
    • Pande, A.H.1    Sumati, H.N.2    Hajela, K.3
  • 16
    • 0019453914 scopus 로고
    • Lectin-like activities associated with human and murine neoplastic cells
    • Raz A., Lotan R. Lectin-like activities associated with human and murine neoplastic cells. Cancer Res. 1981, 41:3642-3647.
    • (1981) Cancer Res. , vol.41 , pp. 3642-3647
    • Raz, A.1    Lotan, R.2
  • 18
    • 84897479520 scopus 로고    scopus 로고
    • A galectin from the kuruma shrimp (Marsupenaeus japonicus) functions as an opsonin and promotes bacterial clearance from hemolymph
    • Shi X.-Z., Wang L., Xu S., Zhang X.-W., Zhao X.-F., Vasta G.R., Wang J.-X. A galectin from the kuruma shrimp (Marsupenaeus japonicus) functions as an opsonin and promotes bacterial clearance from hemolymph. PLoS ONE 2014, 9:12-15.
    • (2014) PLoS ONE , vol.9 , pp. 12-15
    • Shi, X.-Z.1    Wang, L.2    Xu, S.3    Zhang, X.-W.4    Zhao, X.-F.5    Vasta, G.R.6    Wang, J.-X.7
  • 19
    • 80655125508 scopus 로고    scopus 로고
    • Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4
    • St-Pierre C., Manya H., Ouellet M., Clark G.F., Endo T., Tremblay M.J., Sato S. Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4. J. Virol. 2011, 85:11742-11751.
    • (2011) J. Virol. , vol.85 , pp. 11742-11751
    • St-Pierre, C.1    Manya, H.2    Ouellet, M.3    Clark, G.F.4    Endo, T.5    Tremblay, M.J.6    Sato, S.7
  • 20
    • 0030801111 scopus 로고    scopus 로고
    • Unusual structural stability and ligand induced alterations in oligomerization of a galectin
    • Surolia A., Swaminathan C.P., Ramkumar R., Podder S.K. Unusual structural stability and ligand induced alterations in oligomerization of a galectin. FEBS Lett. 1997, 409:417-420.
    • (1997) FEBS Lett. , vol.409 , pp. 417-420
    • Surolia, A.1    Swaminathan, C.P.2    Ramkumar, R.3    Podder, S.K.4
  • 21
    • 84899723735 scopus 로고    scopus 로고
    • Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-Helices to a β-barrel during the transmembrane pore formation process
    • Unno H., Goda S., Hatakeyama T. Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-Helices to a β-barrel during the transmembrane pore formation process. J. Biol. Chem. 2014, 289:12805-12812.
    • (2014) J. Biol. Chem. , vol.289 , pp. 12805-12812
    • Unno, H.1    Goda, S.2    Hatakeyama, T.3
  • 22
    • 0037013214 scopus 로고    scopus 로고
    • Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation
    • Yu F., Finley R.L., Raz A., Kim H.-R.C. Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation. J. Biol. Chem. 2002, 277:15819-15827.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15819-15827
    • Yu, F.1    Finley, R.L.2    Raz, A.3    Kim, H.-R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.