메뉴 건너뛰기




Volumn 82, Issue 2, 2003, Pages 242-250

Cloning and characterization of HEP21,1 a new member of the uPAR/Ly6 protein superfamily predominantly expressed in hen egg white

Author keywords

Amino acid sequence; cDNA; Chicken egg white; HEP21; uPAR Ly 6

Indexed keywords

GALLUS GALLUS; SERPENTES;

EID: 0037317857     PISSN: 00325791     EISSN: None     Source Type: Journal    
DOI: 10.1093/ps/82.2.242     Document Type: Article
Times cited : (24)

References (34)
  • 1
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion and metastasis
    • Andreasen, P. A., R. Egelund, and H. H. Petersen. 2000. The plasminogen activation system in tumor growth, invasion and metastasis. Cell Mol. Life Sci. 57:25-40.
    • (2000) Cell Mol. Life Sci. , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 2
    • 0026474486 scopus 로고
    • Relative roles of decay-accelerating factor, membrane cofactor protein, and CD59 in the protection of human endothelial cells against complement-mediated lysis
    • Brooimans, R. A., P. A. van Wieringen, L. A. van Es, and M. R. Daha. 1992. Relative roles of decay-accelerating factor, membrane cofactor protein, and CD59 in the protection of human endothelial cells against complement-mediated lysis. Eur. J. Immunol. 22:3135-3140.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 3135-3140
    • Brooimans, R.A.1    Van Wieringen, P.A.2    Van Es, L.A.3    Daha, M.R.4
  • 3
    • 0031433280 scopus 로고    scopus 로고
    • New microsatellite markers in chicken optimized for automated fluorescent genotyping
    • Crooijmans, R. P. M. A., R. J. M. Dijkhof, J. J. van der Poel, and M. A. M. Groenen. 1997. New microsatellite markers in chicken optimized for automated fluorescent genotyping. Anim. Genet. 28:427-437.
    • (1997) Anim. Genet. , vol.28 , pp. 427-437
    • Crooijmans, R.P.M.A.1    Dijkhof, R.J.M.2    Van Der Poel, J.J.3    Groenen, M.A.M.4
  • 6
    • 0028176724 scopus 로고
    • A phospholipase A2 inhibitor from the plasma of the South American rattlesnake (Crotalus durissus terrificus). Protein structure, genomic structure, and mechanism of action
    • Fortes-Dias, C. L., Y. Lin, J. Ewell, C. R. Diniz, and T. Y. Liu. 1994. A phospholipase A2 inhibitor from the plasma of the South American rattlesnake (Crotalus durissus terrificus). Protein structure, genomic structure, and mechanism of action. J. Biol. Chem. 269:15646-15651.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15646-15651
    • Fortes-Dias, C.L.1    Lin, Y.2    Ewell, J.3    Diniz, C.R.4    Liu, T.Y.5
  • 7
    • 84982341706 scopus 로고
    • Fractions of egg white which control growth of bacteria
    • Garibaldi, J. A. 1960. Fractions of egg white which control growth of bacteria. Food Res. 25:337-344.
    • (1960) Food Res. , vol.25 , pp. 337-344
    • Garibaldi, J.A.1
  • 9
    • 84988122211 scopus 로고
    • Elimination of point streaking on silver stained two-dimensional gels by addition of iodoacetamide to the equilibration buffer
    • Görg, A., W. Postel, J. Weser, S. Gunther, J. R. Strahler, S. M. Hanash, and L. Somerlot. 1987. Elimination of point streaking on silver stained two-dimensional gels by addition of iodoacetamide to the equilibration buffer. Electrophoresis 8:122-124.
    • (1987) Electrophoresis , vol.8 , pp. 122-124
    • Görg, A.1    Postel, W.2    Weser, J.3    Gunther, S.4    Strahler, J.R.5    Hanash, S.M.6    Somerlot, L.7
  • 10
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg, A., W. Postel, and S. Gunther. 1988. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9:531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Görg, A.1    Postel, W.2    Gunther, S.3
  • 11
    • 0029047942 scopus 로고
    • Sequence and structure of the mouse ThB gene
    • Gumley, T. P., I. F. McKenzie, and M. S. Sandrin. 1995. Sequence and structure of the mouse ThB gene. Immunogenetics 42:221-224.
    • (1995) Immunogenetics , vol.42 , pp. 221-224
    • Gumley, T.P.1    McKenzie, I.F.2    Sandrin, M.S.3
  • 12
    • 0033822833 scopus 로고    scopus 로고
    • Identification and localization of lysozyme as a component of the eggshell membranes and shell matrix
    • Hincke, M. T., J. Gautron, M. Panheleux, J. M. Garcia-Ruiz, M. D. McKee, and Y. Nys. 2000. Identification and localization of lysozyme as a component of the eggshell membranes and shell matrix. Matrix Biol. 19:443-453.
    • (2000) Matrix Biol. , vol.19 , pp. 443-453
    • Hincke, M.T.1    Gautron, J.2    Panheleux, M.3    Garcia-Ruiz, J.M.4    McKee, M.D.5    Nys, Y.6
  • 13
    • 2442538206 scopus 로고    scopus 로고
    • Interactions of egg white proteins
    • A. Gaonkar, ed. Marcel Dekker Inc., New York
    • Kato, A. 1997. Interactions of egg white proteins. Pages 357-375 in Ingredient Interactions, Effects on Food Quality. A. Gaonkar, ed. Marcel Dekker Inc., New York.
    • (1997) Ingredient Interactions, Effects on Food Quality , pp. 357-375
    • Kato, A.1
  • 14
    • 0026338740 scopus 로고
    • Two alternatively spliced mouse urokinase receptor mRNAs with different histological localization in the gastrointestinal tract
    • Kristensen, P., J. Eriksen, F. Blasi, and K. Danoe. 1991. Two alternatively spliced mouse urokinase receptor mRNAs with different histological localization in the gastrointestinal tract. J. Cell Biol. 115:1763-1771.
    • (1991) J. Cell Biol. , vol.115 , pp. 1763-1771
    • Kristensen, P.1    Eriksen, J.2    Blasi, F.3    Danoe, K.4
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 22:680-685.
    • (1970) Nature , vol.22 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0002966136 scopus 로고    scopus 로고
    • Identification of Ch21, a developmentally regulated chicken embryo protein, in egg albumen
    • L. G. Cavalchini and D. Baroli, ed. Associazione Italiana di Avicoltura Scientifica, Milano, Italy
    • Larsen, L. B., M. Hammershoj, and J. T. Rasmussen. 1999. Identification of Ch21, a developmentally regulated chicken embryo protein, in egg albumen. Pages 61-67 in Proceedings of the VIII European Symposium on the Quality of Eggs and Egg Products. Vol. II. L. G. Cavalchini and D. Baroli, ed. Associazione Italiana di Avicoltura Scientifica, Milano, Italy.
    • (1999) Proceedings of the VIII European Symposium on the Quality of Eggs and Egg Products , vol.2 , pp. 61-67
    • Larsen, L.B.1    Hammershoj, M.2    Rasmussen, J.T.3
  • 17
    • 0000884136 scopus 로고
    • Biochemical basis for the properties of egg white
    • Li-Chan, E., and S. Nakai. 1989. Biochemical basis for the properties of egg white. Crit. Rev. Poult. Biol. 2:21-58.
    • (1989) Crit. Rev. Poult. Biol. , vol.2 , pp. 21-58
    • Li-Chan, E.1    Nakai, S.2
  • 18
    • 0034933664 scopus 로고    scopus 로고
    • The urokinase plasminogen activator receptor (uPAR) as a target for the diagnosis and therapy of cancer
    • Mazar, A. P. 2001. The urokinase plasminogen activator receptor (uPAR) as a target for the diagnosis and therapy of cancer. Anticancer Drugs 12:387-400.
    • (2001) Anticancer Drugs , vol.12 , pp. 387-400
    • Mazar, A.P.1
  • 19
    • 0028873168 scopus 로고
    • Recent advances in the understanding of egg white protein functionality
    • Mine, Y. 1995. Recent advances in the understanding of egg white protein functionality. Trends Food Sci. Technol. 6:225-232.
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 225-232
    • Mine, Y.1
  • 20
    • 0015595842 scopus 로고
    • Factors affecting the growth of Pseudomonas fluorescens in liquid egg white
    • Nath, K. R., and C. Baker. 1973. Factors affecting the growth of Pseudomonas fluorescens in liquid egg white. Appl. Microbiol. 25:442-446.
    • (1973) Appl. Microbiol. , vol.25 , pp. 442-446
    • Nath, K.R.1    Baker, C.2
  • 21
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 23
    • 0016711037 scopus 로고
    • High-resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. 1975. High-resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 24
    • 0028350083 scopus 로고
    • Isolation and characterization of a phospholipase A2 inhibitor from the blood plasma of the Thailand cobra Naja naja kaouthia
    • Ohkura, N., S. Inoue, K. Ikeda, and K. Hayashi. 1994. Isolation and characterization of a phospholipase A2 inhibitor from the blood plasma of the Thailand cobra Naja naja kaouthia. Biochem. Biophys. Res. Commun. 200:784-788.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 784-788
    • Ohkura, N.1    Inoue, S.2    Ikeda, K.3    Hayashi, K.4
  • 25
    • 0023883889 scopus 로고
    • N-terminal and cDNA characterization of murine lymphocyte antigen Ly-6C.2
    • Palfree, R. G. E., S. Sirlin, F. J. Dumont, and U. Haemmerling. 1988. N-terminal and cDNA characterization of murine lymphocyte antigen Ly-6C.2. J. Immunol. 140:305@nd310.
    • (1988) J. Immunol. , vol.140 , pp. 305
    • Palfree, R.G.E.1    Sirlin, S.2    Dumont, F.J.3    Haemmerling, U.4
  • 26
    • 0027217194 scopus 로고
    • Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator
    • Ploug, M., M. Kjalke, E. Ronne, U. Weidle, G. Hoyer-Hansen, G. and K. Dano. 1993. Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator. J. Biol. Chem. 268:17539-17546.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17539-17546
    • Ploug, M.1    Kjalke, M.2    Ronne, E.3    Weidle, U.4    Hoyer-Hansen, G.5    Dano, K.6
  • 27
    • 0028064814 scopus 로고
    • Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom α-neurotoxins
    • Ploug, M., and V. Ellis. 1994. Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom α-neurotoxins. FEBS Lett. 349:163-168.
    • (1994) FEBS Lett. , vol.349 , pp. 163-168
    • Ploug, M.1    Ellis, V.2
  • 28
    • 0019487684 scopus 로고
    • Glycoprotein molecular-weight estimation using sodium dodecyl sulfate-pore gradient electrophoresis: Comparison of tris-glycine and tris-borate-EDTA buffer systems
    • Poduslo, J. F. 1981. Glycoprotein molecular-weight estimation using sodium dodecyl sulfate-pore gradient electrophoresis: comparison of tris-glycine and tris-borate-EDTA buffer systems. Anal. Biochem. 114:131-139.
    • (1981) Anal. Biochem. , vol.114 , pp. 131-139
    • Poduslo, J.F.1
  • 29
    • 0028010999 scopus 로고
    • Isolation and characterization of multiple isoforms of the rat urokinase receptor in osteoblasts
    • Rabbani, S. A., N. Rajwans, A. Achbarou, K. K. Murthy, and D. Goltzman. 1994. Isolation and characterization of multiple isoforms of the rat urokinase receptor in osteoblasts. FEBS Lett. 338:69-74.
    • (1994) FEBS Lett. , vol.338 , pp. 69-74
    • Rabbani, S.A.1    Rajwans, N.2    Achbarou, A.3    Murthy, K.K.4    Goltzman, D.5
  • 30
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud, T. 1998. Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 19:758-760.
    • (1998) Electrophoresis , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 33
    • 0029715684 scopus 로고    scopus 로고
    • Egg proteins: What are their functions?
    • Stevens, L. 1996. Egg proteins: what are their functions? Sci. Progr. 79:65-87.
    • (1996) Sci. Progr. , vol.79 , pp. 65-87
    • Stevens, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.