메뉴 건너뛰기




Volumn 9, Issue 2, 2000, Pages 289-301

A novel human odorant-binding protein gene family resulting from genomic duplicons at 9q34: Differential expression in the oral and genital spheres

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LIPOCALIN; ODORANT BINDING PROTEIN; PHEROMONE; UNCLASSIFIED DRUG;

EID: 0033979907     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/9.2.289     Document Type: Article
Times cited : (65)

References (57)
  • 1
    • 0025825726 scopus 로고
    • A novel mulligene family may encode odorant receptors: A molecular basis for odor recognition
    • Buck, L. and Axel, R. (1991) A novel mulligene family may encode odorant receptors: a molecular basis for odor recognition. Cell, 65, 175-187.
    • (1991) Cell , vol.65 , pp. 175-187
    • Buck, L.1    Axel, R.2
  • 2
    • 0029921089 scopus 로고    scopus 로고
    • Perireceptor events in olfaction
    • Pelosi, P. (1996) Perireceptor events in olfaction. J. Neurobiol., 30, 3-19.
    • (1996) J. Neurobiol. , vol.30 , pp. 3-19
    • Pelosi, P.1
  • 3
    • 0023609533 scopus 로고
    • Homology and structure-function correlations between α 1-acid glycoprotein and serum retinol-binding protein and its relatives
    • Pervaiz, S. and Brew, K. (1987) Homology and structure-function correlations between α 1-acid glycoprotein and serum retinol-binding protein and its relatives. FASEB J., 1, 209-214.
    • (1987) FASEB J. , vol.1 , pp. 209-214
    • Pervaiz, S.1    Brew, K.2
  • 4
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D.R. (1996) The lipocalin protein family: structure and function. Biochem. J., 318, 1-14.
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 5
    • 0033525727 scopus 로고    scopus 로고
    • Combinatorial receptor codes for odors
    • Malnic, B., Hirono, J., Sato, T. and Buck, L.B. (1999) Combinatorial receptor codes for odors. Cell, 96, 713-723.
    • (1999) Cell , vol.96 , pp. 713-723
    • Malnic, B.1    Hirono, J.2    Sato, T.3    Buck, L.B.4
  • 6
    • 0040352690 scopus 로고
    • Odorant-binding protein: Localization to nasal glands and secretions
    • Pevsner, J., Sklar, P.B. and Snyder, S.H. (1986) Odorant-binding protein: localization to nasal glands and secretions. Proc. Natl Acad. Sci. USA, 83, 4942-4946.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4942-4946
    • Pevsner, J.1    Sklar, P.B.2    Snyder, S.H.3
  • 7
  • 8
    • 0027310749 scopus 로고
    • Multiple types and forms of odorant-binding proteins in the Old-World porcupine Hystrix cristata
    • Felicioli, A., Ganni, M., Garibotti, M. and Pelosi, P. (1993) Multiple types and forms of odorant-binding proteins in the Old-World porcupine Hystrix cristata. Comp. Biochem. Physiol. B, 105, 775-784.
    • (1993) Comp. Biochem. Physiol. B , vol.105 , pp. 775-784
    • Felicioli, A.1    Ganni, M.2    Garibotti, M.3    Pelosi, P.4
  • 9
    • 0026347802 scopus 로고
    • Molecular cloning of putative odorant-binding and odorant-metabolizing proteins
    • Dear, T.N., Campbell, K. and Rabbitts, T.H. (1991) Molecular cloning of putative odorant-binding and odorant-metabolizing proteins. Biochemistry, 30, 10376-10382.
    • (1991) Biochemistry , vol.30 , pp. 10376-10382
    • Dear, T.N.1    Campbell, K.2    Rabbitts, T.H.3
  • 10
    • 0032575116 scopus 로고    scopus 로고
    • Cloning and expression of odorant-binding proteins Ia and Ib from mouse nasal tissue
    • Pes, D., Mameli, M., Andreini, I., Krieger, J., Weber, M., Breer, H. and Pelosi, P. (1998) Cloning and expression of odorant-binding proteins Ia and Ib from mouse nasal tissue. Gene, 212, 49-55.
    • (1998) Gene , vol.212 , pp. 49-55
    • Pes, D.1    Mameli, M.2    Andreini, I.3    Krieger, J.4    Weber, M.5    Breer, H.6    Pelosi, P.7
  • 11
    • 0032521669 scopus 로고    scopus 로고
    • Lipocalins of boar salivary glands binding odours and pheromones
    • Marchese, S., Pes, D., Scaloni, A., Carbone V. and Pelosi, P. (1998) Lipocalins of boar salivary glands binding odours and pheromones. Eur. J. Biochem., 252, 563-568.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 563-568
    • Marchese, S.1    Pes, D.2    Scaloni, A.3    Carbone, V.4    Pelosi, P.5
  • 12
    • 0026726499 scopus 로고
    • cDNa cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily
    • Redl, B., Holzfeind, P. and Lottspeich, F. (1992) cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily. J. Biol. Chem., 267, 20282-20287.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20282-20287
    • Redl, B.1    Holzfeind, P.2    Lottspeich, F.3
  • 13
    • 0027406716 scopus 로고
    • Molecular cloning of human von Ebner's gland protein, a member of the lipocalin superfamily highly expressed in lingual salivary glands
    • Blaker, M., Kock, K., Ahlers, C., Buck, F. and Schmale, H. (1993) Molecular cloning of human von Ebner's gland protein, a member of the lipocalin superfamily highly expressed in lingual salivary glands. Biochim. Biophys. Acta, 1172, 131-137.
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 131-137
    • Blaker, M.1    Kock, K.2    Ahlers, C.3    Buck, F.4    Schmale, H.5
  • 15
    • 0031704524 scopus 로고    scopus 로고
    • Identification of a lipocalin in mucosal glands of the human tracheobronchial tree and its enhanced secretion in cystic fibrosis
    • Redl, B., Wojnar, P., Ellemunter, H. and Feichtinger, H. (1998) Identification of a lipocalin in mucosal glands of the human tracheobronchial tree and its enhanced secretion in cystic fibrosis. Lab. Invest., 78, 1121-1129.
    • (1998) Lab. Invest. , vol.78 , pp. 1121-1129
    • Redl, B.1    Wojnar, P.2    Ellemunter, H.3    Feichtinger, H.4
  • 16
    • 0031593397 scopus 로고    scopus 로고
    • Immunohistochemical localisation of tear lipocalin in human nasal mucosa
    • Fattori, B., Castagna, M., Megna, G., Casani, A. and Pelosi, P. (1998) Immunohistochemical localisation of tear lipocalin in human nasal mucosa. Rhinology, 36, 101-103.
    • (1998) Rhinology , vol.36 , pp. 101-103
    • Fattori, B.1    Castagna, M.2    Megna, G.3    Casani, A.4    Pelosi, P.5
  • 17
    • 0028608047 scopus 로고
    • Possible pheromone-carrier function of two lipocalin proteins in the vomeronasal organ
    • Miyawaki, A., Matsushita, F., Ryo, Y. and Mikoshiba, K. (1994) Possible pheromone-carrier function of two lipocalin proteins in the vomeronasal organ. EMBO J., 13, 5835-5842.
    • (1994) EMBO J. , vol.13 , pp. 5835-5842
    • Miyawaki, A.1    Matsushita, F.2    Ryo, Y.3    Mikoshiba, K.4
  • 18
    • 0018822923 scopus 로고
    • In vitro synthesis and characterization of precursors to the mouse major urinary proteins
    • Szoka, P.R., Gallagher, J.F. and Held, W.A. (1980) In vitro synthesis and characterization of precursors to the mouse major urinary proteins. J. Biol. Chem., 255, 1367-1373.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1367-1373
    • Szoka, P.R.1    Gallagher, J.F.2    Held, W.A.3
  • 21
    • 0023552861 scopus 로고
    • Cloning and nucleotide sequence of the bovine β-lactoglobulin gene
    • Jamieson, A.C., Vandeyar, M.A., Kang, Y.C., Kinsella, J.E. and Batt, C.A. (1987) Cloning and nucleotide sequence of the bovine β-lactoglobulin gene. Gene, 61, 85-90.
    • (1987) Gene , vol.61 , pp. 85-90
    • Jamieson, A.C.1    Vandeyar, M.A.2    Kang, Y.C.3    Kinsella, J.E.4    Batt, C.A.5
  • 22
    • 0031890016 scopus 로고    scopus 로고
    • Phylogenetic analysis of three lipocalin-like proteins present in the milk of Trichosurus vulpecula (Phalangeridae, Marsupialia)
    • Piotte, C.P., Hunter, A.K., Marshall, C.J. and Grigor, M.R. (1998) Phylogenetic analysis of three lipocalin-like proteins present in the milk of Trichosurus vulpecula (Phalangeridae, Marsupialia). J. Mol. Evol., 46, 361-369.
    • (1998) J. Mol. Evol. , vol.46 , pp. 361-369
    • Piotte, C.P.1    Hunter, A.K.2    Marshall, C.J.3    Grigor, M.R.4
  • 23
    • 0031789624 scopus 로고    scopus 로고
    • Molecular cloning and hormonal regulation of a murine epididymal retinoic acid-binding protein messenger ribonucleic acid
    • Lareyre, J.J., Zheng, W.L., Zhao, G.Q., Kasper, S., Newcomer, M.E., Matusik, R.J., Ong, D.E. and Orgebin-Crist, M.C. (1998) Molecular cloning and hormonal regulation of a murine epididymal retinoic acid-binding protein messenger ribonucleic acid. Endocrinology, 139, 2971-2981.
    • (1998) Endocrinology , vol.139 , pp. 2971-2981
    • Lareyre, J.J.1    Zheng, W.L.2    Zhao, G.Q.3    Kasper, S.4    Newcomer, M.E.5    Matusik, R.J.6    Ong, D.E.7    Orgebin-Crist, M.C.8
  • 24
    • 0026326319 scopus 로고
    • Molecular cloning and characterization of a cDNa encoding for the mature form of a specific androgen dependent epididymal protein
    • Morel, L., Depeiges, A. and Dufaure, J.P. (1991) Molecular cloning and characterization of a cDNA encoding for the mature form of a specific androgen dependent epididymal protein. Cell. Mol. Biol., 37, 757-764.
    • (1991) Cell. Mol. Biol. , vol.37 , pp. 757-764
    • Morel, L.1    Depeiges, A.2    Dufaure, J.P.3
  • 25
    • 0030946843 scopus 로고    scopus 로고
    • Multiple forms of messenger ribonucleic acid encoding glycodelin in male genital tract
    • Koistinen, H., Koistinen, R., Kamarainen, M., Salo, J. and Seppala, M. (1997) Multiple forms of messenger ribonucleic acid encoding glycodelin in male genital tract. Lab. Invest., 76, 683-690.
    • (1997) Lab. Invest. , vol.76 , pp. 683-690
    • Koistinen, H.1    Koistinen, R.2    Kamarainen, M.3    Salo, J.4    Seppala, M.5
  • 26
  • 27
    • 0026695798 scopus 로고
    • Structural organization of the gene for prostaglandin D synthase in the rat brain
    • Igarashi, M., Nagata, A., Toh, H., Urade, Y. and Hayaishi, O. (1992) Structural organization of the gene for prostaglandin D synthase in the rat brain. Proc. Natl Acad. Sci. USA, 89, 5376-5380.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5376-5380
    • Igarashi, M.1    Nagata, A.2    Toh, H.3    Urade, Y.4    Hayaishi, O.5
  • 28
    • 0028136235 scopus 로고
    • Comparative mapping of lipocalin genes in human and mouse: The four genes for complement C8 γ chain, prostaglandin-D-synthase, oncogene-24p3 and progestagen-associated endometrial protein map to HSA9 and MMU2
    • Chan, P., Simon-Chazottes, D., Mattei, M.G., Guenet, J.L. and Salier, J.P. (1994) Comparative mapping of lipocalin genes in human and mouse: the four genes for complement C8 γ chain, prostaglandin-D-synthase, oncogene-24p3 and progestagen-associated endometrial protein map to HSA9 and MMU2. Genomics, 23, 145-150.
    • (1994) Genomics , vol.23 , pp. 145-150
    • Chan, P.1    Simon-Chazottes, D.2    Mattei, M.G.3    Guenet, J.L.4    Salier, J.P.5
  • 29
    • 0029788496 scopus 로고    scopus 로고
    • The human complement C8G gene, a member of the lipocalin gene family: Polymorphisms and mapping to chromosome 9q34.3
    • Dewald, G., Cichon, S., Bryant, S.P., Hemmer, S., Nothen, M.M. and Spurr, N.K. (1996) The human complement C8G gene, a member of the lipocalin gene family: polymorphisms and mapping to chromosome 9q34.3. Ann. Hum. Genet., 60, 281-291.
    • (1996) Ann. Hum. Genet. , vol.60 , pp. 281-291
    • Dewald, G.1    Cichon, S.2    Bryant, S.P.3    Hemmer, S.4    Nothen, M.M.5    Spurr, N.K.6
  • 30
    • 0028204454 scopus 로고
    • Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins
    • Kock, K., Ahlers, C. and Schmale, H. (1994) Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins. Eur. J. Biochem., 221, 905-916.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 905-916
    • Kock, K.1    Ahlers, C.2    Schmale, H.3
  • 31
    • 13144253092 scopus 로고    scopus 로고
    • Molecular evolution: Recent cases of spliceosomal intron gain?
    • Logsdon Jr, J.M., Stoltzfus, A. and Doolittle, W.F. (1998) Molecular evolution: recent cases of spliceosomal intron gain? Curr. Biol., 8, R560-R563.
    • (1998) Curr Biol. , vol.8 , pp. R560-R563
    • Logsdon J.M., Jr.1    Stoltzfus, A.2    Doolittle, W.F.3
  • 32
    • 0027262581 scopus 로고
    • Cloning of a human lacrimal lipocalin secreted in tears [letter]
    • Lassagne, H. and Gachon, A.M. (1993) Cloning of a human lacrimal lipocalin secreted in tears [letter]. Exp. Eye Res., 56, 605-609.
    • (1993) Exp. Eye Res. , vol.56 , pp. 605-609
    • Lassagne, H.1    Gachon, A.M.2
  • 33
    • 0027420733 scopus 로고
    • Assignment of the human tear lipocalin gene (LCNI) to 9q34 by in situ hybridization
    • Lassagne, H., Ressot, C., Mattei, M.G. and Gachon, A.M. (1993) Assignment of the human tear lipocalin gene (LCNI) to 9q34 by in situ hybridization. Genomics, 18, 160-161.
    • (1993) Genomics , vol.18 , pp. 160-161
    • Lassagne, H.1    Ressot, C.2    Mattei, M.G.3    Gachon, A.M.4
  • 36
    • 0028286959 scopus 로고
    • Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli
    • Holzfeind, P. and Redl, B. (1994) Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli. Gene, 139, 177-183.
    • (1994) Gene , vol.139 , pp. 177-183
    • Holzfeind, P.1    Redl, B.2
  • 40
    • 0023960321 scopus 로고
    • The structural motif of β-lactoglobulin and retinol-binding protein: A basic framework for binding and transport of small hydrophobic molecules? Trends Biochem
    • Godovac-Zimmermann, J. (1988) The structural motif of β-lactoglobulin and retinol-binding protein: a basic framework for binding and transport of small hydrophobic molecules? Trends Biochem. Sci., 13, 64-66.
    • (1988) Sci. , vol.13 , pp. 64-66
    • Godovac-Zimmermann, J.1
  • 42
    • 0027140130 scopus 로고
    • Origin of late lactation protein from β-lactoglobulin in the tammar wallaby
    • Woodlee, G.L., Gooley, A.A., Collet, C. and Cooper, D.W. (1993) Origin of late lactation protein from β-lactoglobulin in the tammar wallaby. J. Hered., 84, 460-465.
    • (1993) J. Hered. , vol.84 , pp. 460-465
    • Woodlee, G.L.1    Gooley, A.A.2    Collet, C.3    Cooper, D.W.4
  • 43
    • 0021488518 scopus 로고
    • A 45-kb DNA domain with two divergently orientated genes is the unit of organisation of the murine major urinary protein genes
    • Clark, A.J., Hickman, J. and Bishop, J. (1984) A 45-kb DNA domain with two divergently orientated genes is the unit of organisation of the murine major urinary protein genes. EMBO J., 3, 2055-2064.
    • (1984) EMBO J. , vol.3 , pp. 2055-2064
    • Clark, A.J.1    Hickman, J.2    Bishop, J.3
  • 44
    • 0023390753 scopus 로고
    • Structure and expression of the genes coding for human α 1-acid glycoprotein
    • Dente, L., Pizza, M.G., Metspalu, A. and Cortese, R. (1987) Structure and expression of the genes coding for human α 1-acid glycoprotein. EMBO J., 6, 2289-2296.
    • (1987) EMBO J. , vol.6 , pp. 2289-2296
    • Dente, L.1    Pizza, M.G.2    Metspalu, A.3    Cortese, R.4
  • 45
    • 0023282332 scopus 로고
    • A novel whey protein synthesized only in late lactation by the mammary gland from the lammar (Macropus eugenii)
    • Nicholas, K.R., Messer, M., Elliott, C., Maher, F. and Shaw, D.C. (1987) A novel whey protein synthesized only in late lactation by the mammary gland from the lammar (Macropus eugenii). Biochem. J., 241, 899-904.
    • (1987) Biochem. J. , vol.241 , pp. 899-904
    • Nicholas, K.R.1    Messer, M.2    Elliott, C.3    Maher, F.4    Shaw, D.C.5
  • 46
    • 0032103101 scopus 로고    scopus 로고
    • Subtypes of odorant-binding proteins - Heterologous expression and ligand binding
    • Lobel, D., Marchese, S., Krieger, J., Pelosi, P. and Breer, H. (1998) Subtypes of odorant-binding proteins - heterologous expression and ligand binding. Eur. J. Biochem., 254, 318-324.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 318-324
    • Lobel, D.1    Marchese, S.2    Krieger, J.3    Pelosi, P.4    Breer, H.5
  • 49
    • 0030666566 scopus 로고    scopus 로고
    • Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug
    • Fuentes-Prior, P., Noeske-Jungblut, C., Donner, P., Schleuning, W.D., Huber, R. and Bode, W. (1997) Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc. Natl Acad. Sci. USA, 94, 11845-11850.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11845-11850
    • Fuentes-Prior, P.1    Noeske-Jungblut, C.2    Donner, P.3    Schleuning, W.D.4    Huber, R.5    Bode, W.6
  • 51
    • 0023038668 scopus 로고
    • Molecular cloning of the cDNA for two major androgen-dependent secretory proteins of 18.5 kilodaltons synthesized by the rat epididymis
    • Brooks, D.E., Means, A.R., Wright, E.J., Singh, S.P. and Tiver, K.K. (1986) Molecular cloning of the cDNA for two major androgen-dependent secretory proteins of 18.5 kilodaltons synthesized by the rat epididymis. J. Biol. Chem., 261, 4956-4961.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4956-4961
    • Brooks, D.E.1    Means, A.R.2    Wright, E.J.3    Singh, S.P.4    Tiver, K.K.5
  • 54
    • 0031081677 scopus 로고    scopus 로고
    • Specific repertoire of olfactory receptor genes in the male germ cells of several mammalian species
    • Vanderhaeghen, P., Schurmans, S., Vassart, G. and Parmentier, M. (1997) Specific repertoire of olfactory receptor genes in the male germ cells of several mammalian species. Genomics, 39, 239-246.
    • (1997) Genomics , vol.39 , pp. 239-246
    • Vanderhaeghen, P.1    Schurmans, S.2    Vassart, G.3    Parmentier, M.4
  • 55
    • 0029112604 scopus 로고
    • Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins
    • Bishop, R.E., Penfold, S.S., Frost, L.S, Holtje, J.V. and Weiner, J.H. (1995) Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins. J. Biol. Chem., 270, 23097-23103.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23097-23103
    • Bishop, R.E.1    Penfold, S.S.2    Frost, L.S.3    Holtje, J.V.4    Weiner, J.H.5
  • 57
    • 0032474475 scopus 로고    scopus 로고
    • The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism
    • Spinelli, S., Ramoni, R., Grolli, S., Bonicel, J., Cambillau, C. and Tegoni, M. (1998) The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry, 37, 7913-7918.
    • (1998) Biochemistry , vol.37 , pp. 7913-7918
    • Spinelli, S.1    Ramoni, R.2    Grolli, S.3    Bonicel, J.4    Cambillau, C.5    Tegoni, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.