메뉴 건너뛰기




Volumn 12, Issue 3, 2013, Pages 3110-3123

Structure and immune expression analysis of hemoglobin genes from the blood clam tegillarca granosa

Author keywords

Gene structure; Hemoglobins; Immune response; qRT PCR; Tegillarca granosa

Indexed keywords

COMPLEMENTARY DNA; HEMOGLOBIN; HEMOGLOBIN I; HEMOGLOBIN IIA; HEMOGLOBIN IIB; LIPOPOLYSACCHARIDE; MESSENGER RNA; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

EID: 84882979383     PISSN: None     EISSN: 16765680     Source Type: Journal    
DOI: 10.4238/2013.February.28.5     Document Type: Article
Times cited : (23)

References (29)
  • 1
    • 38149088861 scopus 로고    scopus 로고
    • Assessment of arsenic and heavy metal contents in cockles (Anadara granosa) using multivariate statistical techniques
    • Abbas Alkarkhi FM, Ismail N and Easa AM (2008). Assessment of arsenic and heavy metal contents in cockles (Anadara granosa) using multivariate statistical techniques. J. Hazard. Mater. 150: 783-789.
    • (2008) J. Hazard. Mater , vol.150 , pp. 783-789
    • Abbas Alkarkhi, F.M.1    Ismail, N.2    Easa, A.M.3
  • 2
    • 79961023255 scopus 로고    scopus 로고
    • Hemoglobin of the bloody clam Tegillarca granosa (Tg-HbI) is involved in the immune response against bacterial infection
    • Bao Y, Wang Q and Lin Z (2011a). Hemoglobin of the bloody clam Tegillarca granosa (Tg-HbI) is involved in the immune response against bacterial infection. Fish. Shellfish. Immunol. 31: 517-523.
    • (2011) Fish. Shellfish. Immunol , vol.31 , pp. 517-523
    • Bao, Y.1    Wang, Q.2    Lin, Z.3
  • 3
    • 79551636497 scopus 로고    scopus 로고
    • A small HSP gene of bloody clam (Tegillarca granosa) involved in the immune response against Vibrio parahaemolyticus and lipopolysaccharide
    • Bao Y, Wang Q, Liu H and Lin Z (2011b). A small HSP gene of bloody clam (Tegillarca granosa) involved in the immune response against Vibrio parahaemolyticus and lipopolysaccharide. Fish. Shellfish. Immunol. 30: 729-733.
    • (2011) Fish. Shellfish. Immunol , vol.30 , pp. 729-733
    • Bao, Y.1    Wang, Q.2    Liu, H.3    Lin, Z.4
  • 4
    • 0019873707 scopus 로고
    • Dimeric and tetrameric hemoglobins from the mollusc Scapharca inaequivalvis.Structural and functional properties
    • Chiancone E, Vecchini P, Verzili D, Ascoli F, et al. (1981). Dimeric and tetrameric hemoglobins from the mollusc Scapharca inaequivalvis. Structural and functional properties. J. Mol. Biol. 152: 577-592.
    • (1981) J. Mol. Biol , vol.152 , pp. 577-592
    • Chiancone, E.1    Vecchini, P.2    Verzili, D.3    Ascoli, F.4
  • 5
    • 0032754453 scopus 로고    scopus 로고
    • Functional modulation of the Thr72→Ile mutant from Scapharca inaequivalvis homodimeric hemoglobin
    • Coletta M, Gambacurta A, Clementi ME, Erba F, et al. (1999). Functional modulation of the Thr72→Ile mutant from Scapharca inaequivalvis homodimeric hemoglobin. J. Biol. Inorg. Chem. 4: 678-683.
    • (1999) J. Biol. Inorg. Chem , vol.4 , pp. 678-683
    • Coletta, M.1    Gambacurta, A.2    Clementi, M.E.3    Erba, F.4
  • 6
    • 0037443093 scopus 로고    scopus 로고
    • Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi
    • DeWilde S, Angelini E, Kiger L, Marden MC, et al. (2003). Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi. Biochem. J. 370: 245-253.
    • (2003) Biochem. J , vol.370 , pp. 245-253
    • Dewilde, S.1    Angelini, E.2    Kiger, L.3    Marden, M.C.4
  • 7
    • 78649480773 scopus 로고    scopus 로고
    • The globin gene family of the cephalochordate amphioxus: Implications for chordate globin evolution
    • Ebner B, Panopoulou G, Vinogradov SN, Kiger L, et al. (2010). The globin gene family of the cephalochordate amphioxus: implications for chordate globin evolution. BMC Evol. Biol. 10: 370.
    • (2010) BMC Evol. Biol , vol.10 , pp. 370
    • Ebner, B.1    Panopoulou, G.2    Vinogradov, S.N.3    Kiger, L.4
  • 8
    • 0031595787 scopus 로고    scopus 로고
    • Scapharca inaequivalvis tetrameric hemoglobin A and B genes: Evidence for a minigene
    • Gambacurta A, Piro MC and Ascoli F (1998). Scapharca inaequivalvis tetrameric hemoglobin A and B genes: evidence for a minigene. J. Mol. Evol. 47: 167-171.
    • (1998) J. Mol. Evol , vol.47 , pp. 167-171
    • Gambacurta, A.1    Piro, M.C.2    Ascoli, F.3
  • 9
    • 0037040980 scopus 로고    scopus 로고
    • Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli.Evidence for a novel inducible anaerobic nitric oxide-scavenging activity
    • Gardner AM and Gardner PR (2002). Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity. J. Biol. Chem. 277: 8166-8171.
    • (2002) J. Biol. Chem , vol.277 , pp. 8166-8171
    • Gardner, A.M.1    Gardner, P.R.2
  • 10
    • 0019860994 scopus 로고
    • Correlation of DNA exonic regions with protein structural units in haemoglobin
    • Go M (1981). Correlation of DNA exonic regions with protein structural units in haemoglobin. Nature 291: 90-92.
    • (1981) Nature , vol.291 , pp. 90-92
    • Go, M.1
  • 11
    • 0022394801 scopus 로고
    • Delineation of coding areas in DNA sequences through assignment of codon probabilities
    • Hinds PW and Blake RD (1985). Delineation of coding areas in DNA sequences through assignment of codon probabilities. J. Biomol. Struct. Dyn. 3: 543-549.
    • (1985) J. Biomol. Struct. Dyn , vol.3 , pp. 543-549
    • Hinds, P.W.1    Blake, R.D.2
  • 12
    • 34548785607 scopus 로고    scopus 로고
    • Respiratory protein-generated reactive oxygen species as an antimicrobial strategy
    • Jiang N, Tan NS, Ho B and Ding JL (2007). Respiratory protein-generated reactive oxygen species as an antimicrobial strategy. Nat. Immunol. 8: 1114-1122.
    • (2007) Nat. Immunol , vol.8 , pp. 1114-1122
    • Jiang, N.1    Tan, N.S.2    Ho, B.3    Ding, J.L.4
  • 13
    • 35348842113 scopus 로고    scopus 로고
    • A novel anticoagulant protein with high affinity to blood coagulation factor Va from Tegillarca granosa
    • Jung WK, Jo HY, Qian ZJ, Jeong YJ, et al. (2007). A novel anticoagulant protein with high affinity to blood coagulation factor Va from Tegillarca granosa. J. Biochem. Mol. Biol. 40: 832-838.
    • (2007) J. Biochem. Mol. Biol , vol.40 , pp. 832-838
    • Jung, W.K.1    Jo, H.Y.2    Qian, Z.J.3    Jeong, Y.J.4
  • 14
    • 77956501969 scopus 로고    scopus 로고
    • Hemoglobin-induced oxidative stress contributes to matrix metalloproteinase activation and blood-brain barrier dysfunction in vivo
    • Katsu M, Niizuma K, Yoshioka H, Okami N, et al. (2010). Hemoglobin-induced oxidative stress contributes to matrix metalloproteinase activation and blood-brain barrier dysfunction in vivo. J. Cereb. Blood Flow Metab. 30: 1939-1950.
    • (2010) J. Cereb. Blood Flow Metab , vol.30 , pp. 1939-1950
    • Katsu, M.1    Niizuma, K.2    Yoshioka, H.3    Okami, N.4
  • 15
    • 0036615243 scopus 로고    scopus 로고
    • Monoamine-dependent production of reactive oxygen species catalyzed by pseudoperoxidase activity of human hemoglobin
    • Kawano T, Pinontoan R, Hosoya H and Muto S (2002). Monoamine-dependent production of reactive oxygen species catalyzed by pseudoperoxidase activity of human hemoglobin. Biosci. Biotechnol. Biochem. 66: 1224-1232.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 1224-1232
    • Kawano, T.1    Pinontoan, R.2    Hosoya, H.3    Muto, S.4
  • 16
    • 20444476656 scopus 로고    scopus 로고
    • Structural divergence and distant relationships in proteins: Evolution of the globins
    • Lecomte JT, Vuletich DA and Lesk AM (2005). Structural divergence and distant relationships in proteins: evolution of the globins. Curr. Opin. Struct. Biol. 15: 290-301.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 290-301
    • Lecomte, J.T.1    Vuletich, D.A.2    Lesk, A.M.3
  • 17
    • 43049181937 scopus 로고    scopus 로고
    • Bovine hemoglobin: An attractive source of antibacterial peptides
    • Nedjar-Arroume N, Dubois-Delval V, Adje EY, Traisnel J, et al. (2008). Bovine hemoglobin: an attractive source of antibacterial peptides. Peptides 29: 969-977.
    • (2008) Peptides , vol.29 , pp. 969-977
    • Nedjar-Arroume, N.1    Dubois-Delval, V.2    Adje, E.Y.3    Traisnel, J.4
  • 18
    • 0035083211 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of hemoglobin
    • Parish CA, Jiang H, Tokiwa Y, Berova N, et al. (2001). Broad-spectrum antimicrobial activity of hemoglobin. Bioorg. Med. Chem. 9: 377-382.
    • (2001) Bioorg. Med. Chem , vol.9 , pp. 377-382
    • Parish, C.A.1    Jiang, H.2    Tokiwa, Y.3    Berova, N.4
  • 19
    • 40849092532 scopus 로고    scopus 로고
    • Characterization of the full length mRNA coding for Lucina pectinata HbIII revealed an alternative polyadenylation site
    • Rivera L, Lopez-Garriga J and Cadilla CL (2008). Characterization of the full length mRNA coding for Lucina pectinata HbIII revealed an alternative polyadenylation site. Gene 410: 122-128.
    • (2008) Gene , vol.410 , pp. 122-128
    • Rivera, L.1    Lopez-Garriga, J.2    Cadilla, C.L.3
  • 20
    • 0028035164 scopus 로고
    • Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata.Crystallographic analysis at 1.5 Å resolution
    • Rizzi M, Wittenberg JB, Coda A, Fasano M, et al. (1994). Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata.Crystallographic analysis at 1.5 Å resolution. J. Mol. Biol. 244: 86-99.
    • (1994) J. Mol. Biol , vol.244 , pp. 86-99
    • Rizzi, M.1    Wittenberg, J.B.2    Coda, A.3    Fasano, M.4
  • 21
    • 0021839995 scopus 로고
    • Cooperative dimeric and tetrameric clam haemoglobins are novel assemblages of myoglobin folds
    • Royer WE, Jr., Love WE and Fenderson FF (1985). Cooperative dimeric and tetrameric clam haemoglobins are novel assemblages of myoglobin folds. Nature 316: 277-280.
    • (1985) Nature , vol.316 , pp. 277-280
    • Royer Jr., W.E.1    Love, W.E.2    Fenderson, F.F.3
  • 22
    • 0034673683 scopus 로고    scopus 로고
    • Isolation and cDNA-derived amino acid sequences of hemoglobin and myoglobin from the deep-sea clam Calyptogena kaikoi
    • Suzuki T, Kawamichi H, Ohtsuki R, Iwai M, et al. (2000). Isolation and cDNA-derived amino acid sequences of hemoglobin and myoglobin from the deep-sea clam Calyptogena kaikoi. Biochim. Biophys. Acta 1478: 152-158.
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 152-158
    • Suzuki, T.1    Kawamichi, H.2    Ohtsuki, R.3    Iwai, M.4
  • 23
    • 0032053156 scopus 로고    scopus 로고
    • Functional adaptations of oxygen-transport proteins
    • Terwilliger NB (1998). Functional adaptations of oxygen-transport proteins. J. Exp. Biol. 201: 1085-1098.
    • (1998) J. Exp. Biol , vol.201 , pp. 1085-1098
    • Terwilliger, N.B.1
  • 24
    • 0347992855 scopus 로고    scopus 로고
    • The cDNA-derived amino acid sequence of hemoglobin II from Lucina pectinata
    • Torres-Mercado E, Renta JY, Rodriguez Y, Lopez-Garriga J, et al. (2003). The cDNA-derived amino acid sequence of hemoglobin II from Lucina pectinata. J. Protein Chem. 22: 683-690.
    • (2003) J. Protein Chem , vol.22 , pp. 683-690
    • Torres-Mercado, E.1    Renta, J.Y.2    Rodriguez, Y.3    Lopez-Garriga, J.4
  • 25
    • 33751230816 scopus 로고    scopus 로고
    • Distribution of virulent and pandemic strains of Vibrio parahaemolyticus in three molluscan shellfish species (Meretrix meretrix, Perna viridis, and Anadara granosa) and their association with foodborne disease in southern Thailand
    • Vuddhakul V, Soboon S, Sunghiran W, Kaewpiboon S, et al. (2006). Distribution of virulent and pandemic strains of Vibrio parahaemolyticus in three molluscan shellfish species (Meretrix meretrix, Perna viridis, and Anadara granosa) and their association with foodborne disease in southern Thailand. J. Food Prot. 69: 2615-2620.
    • (2006) J. Food Prot , vol.69 , pp. 2615-2620
    • Vuddhakul, V.1    Soboon, S.2    Sunghiran, W.3    Kaewpiboon, S.4
  • 26
    • 0036915028 scopus 로고    scopus 로고
    • Hemoglobin, from microorganisms to man: A single structural motif, multiple functions
    • Wajcman H and Kiger L (2002). Hemoglobin, from microorganisms to man: a single structural motif, multiple functions. C R. Biol. 325: 1159-1174.
    • (2002) C R. Biol , vol.325 , pp. 1159-1174
    • Wajcman, H.1    Kiger, L.2
  • 27
    • 61549133928 scopus 로고    scopus 로고
    • Structure and function evolution in the superfamily of globins
    • Wajcman H, Kiger L and Marden MC (2009). Structure and function evolution in the superfamily of globins. C R. Biol. 332: 273-282.
    • (2009) C R. Biol , vol.332 , pp. 273-282
    • Wajcman, H.1    Kiger, L.2    Marden, M.C.3
  • 28
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber RE and Vinogradov SN (2001). Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol. Rev. 81: 569-628.
    • (2001) Physiol. Rev , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 29
    • 0029240298 scopus 로고
    • Hemoglobin in the symbiont-harboring gill of the marine gastropod Alviniconcha hessleri
    • Wittenberg JB and Stein JL (1995). Hemoglobin in the symbiont-harboring gill of the marine gastropod Alviniconcha hessleri. Biol. Bull. 188: 5-7.
    • (1995) Biol. Bull , vol.188 , pp. 5-7
    • Wittenberg, J.B.1    Stein, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.