Genetic polymorphism of cat (Felis catus) plasma orosomucoid

Biochemical Genetics

Volumn 35, Issue 9-10, 1997, Pages 303-314

  Yoshida, Haruhiro ^a   Arthur, Helen ^b   Bell, Kevin ^b  

^a SENSHU UNIVERSITY   (Japan)

^b UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Felis catus; Genetics; Orosomucoid; Polymorphism

Indexed keywords

OROSOMUCOID; RABBIT ANTISERUM; SIALIDASE;

ANIMAL TISSUE; ARTICLE; CAT; CONTROLLED STUDY; FEMALE; GENE FREQUENCY; GENETIC POLYMORPHISM; IMMUNOBLOTTING; INHERITANCE; ISOELECTRIC FOCUSING; MALE; MATING; NONHUMAN; PHENOTYPE; PLASMA; POPULATION RESEARCH;

ALLELES; ANIMALS; ANIMALS, DOMESTIC; AUSTRALIA; CATS; GENE FREQUENCY; IMMUNOBLOTTING; ISOELECTRIC FOCUSING; NEURAMINIDASE; NEW ZEALAND; OROSOMUCOID; PHENOTYPE; POLYMORPHISM, GENETIC;

ANIMALIA; CATUS; FELIS CATUS; MAMMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0031414953     PISSN: 00062928     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021817720819     Document Type: Article

References (76)

1. Allderdice, P. W., Kaita, H., Lewis, M., McAlpine, P. J., Wong, P., Anderson, J., and Giblett, E. R. (1986). Segregation of marker loci in families with an inherited paracentric insertion of chromosome 9. Am. J. Hum. Genet. 39:612.
2. Baumann, H., and Berger, F. G. (1985). Genetics and evolution of the acute phase proteins in mice. Mol. Gen. Genet. 201:505.
3. Bell, K., Patterson, S. D., and Pollitt, C. C. (1984). The plasma protease inhibitor system (Pi) of standardbred horses. Anim. Blood Grps. Biochem. Genet. 15:191.
4. Bennett, M., and Schmid, K. (1980). Immunosuppression by human plasma α1-acid glycoprotein: Importance of the carbohydrate moiety. Proc. Natl. Acad. Sci. USA 77:6109.
5. Board, P. G., Jones, I. M., and Bentley, A. K. (1986). Molecular cloning and nucleotide sequence of human α1 acid glycoprotein cDNA. Gene 44:127.
6. Brinkman-van der Linden, E. C. M., van Ommen, E. C. R., and van Dijk, W. (1996). Glycosylation of α1-acid glycoprotein in septic shock: Changes in degree of branching and in expression of sialyl Lewis-x groups. Glycoconjugate J. 13:27.
7. Cerri, N., and DeFerrari, F. (1992). Genetic polymorphism of orosomucoid (ORM1 and ORM2) in Lombardy (Italy). Int. J. Leg. Med. 104:325.
8. Charet, J.-C., Watine, J., Lepretre, A., Raimbault, C., and Charet, P. (1996). Orosomucoid:prealbumin ratio in the monitoring of lung cancer. Clin. Biochem. 29:287.
9. Coddeville, B., Stratil, A., Wieruszeski, J.-M., Strecker, G., Montreuil, J., and Spik, G. (1989). Primary structure of horse serotransferrin glycans. Demonstration that heterogeneity is related to the number of glycans and to the presence of N-acetylneuraminic acid and N-acetyl-4-O-acetylneuraminic acid. Eur. J. Biochem. 186:583.
10. Cooper, R., and Papaconstantinou, J. (1986). Evidence for the existence of multiple α1-acid glycoprotein genes in the mouse. J. Biol. Chem. 261:1849.
11. Couperwhite, S., Stone, R. T., and Archibald, A. L. (1994). A PstI RFLP at the porcine orosomucoid locus (ORM). Anim. Genet. 25:285.
12. Cox, D. W., and Francke, U. (1985). Direct assignment of orosomucoid to human chromosome 9 and α2HS-glycoprotein to chromosome 3 using fetal liver x rat hepatoma hybrids. Hum. Genet. 70:109.
13. Darlington, G. J., Wilson, D. R., and Lachman, L. B. (1986). Monocyte-conditioned medium, interleukin 1 and tumour necrosis factor stimulate the acute phase response in human hepatoma cells in vitro. J. Cell Biol. 103:787.
14. DeGraaf, T. W., Van der Stelt, M. E., Angergen, M. G., and van Dijk, W. (1993). Inflammation-induced expression of sialyl Lewis X-containing glycan structures on α1-acid glycoprotein (orosomucoid) in human sera. J. Exp. Med. 177:657.
15. Dello, C. P., Belpaire, F. M., Kint, J. A., and Fraeyman, N. H. (1987). Dog alpha-1-acid glycoprotein. J. Pharmacol. Meth. 18:335.
16. Dello, C. P., Belpaire, F. M., De Rick, A., and Fraeyman, N. H. (1988). Influence of inflammation on serum concentration, molecular heterogeneity and drug binding properties of canine alpha-1-acid glycoprotein. J. Vet. Pharmacol. Ther. 11:71.
17. Dente, L. (1989). Human α1-acid glycoprotein. Prog. Clin. Biol. Res. 300:85.
18. Dente, L., Ciliberto, G., and Cortese, R. (1985). Structure of the human α1-acid glycoprotein gene: Sequence homology with other human acute phase protein genes. Nucleic Acids Res. 13:3941.
19. Dente, L., Pizza, M. G., Metspalu, A., and Cortese, R. (1987). Structure and expression of the genes coding for human α1-acid glycoprotein. EMBO J. 6:2289.
20. Eap, C. B., Cuendet, C., and Baumann, P. (1988). Orosomucoid (alpha-1 acid glycoprotein) phenotyping by use of immobilized pH gradients with 8M urea and immunoblotting. Hum. Genet. 80:183.
21. Eiberg, H., Mohr, J., and Nielsen, L. S. (1982). Linkage of orosomucoid (ORM) to ABO and AK1. Cytogenet. Cell Genet. 32:272.
22. Eiberg, H., Mohr, J., and Nielsen, L. S. (1983). Delta-aminolevulinate dehydrase: Synteny with ABO-AK1-ORM (and assignment of chromosome 9). Clin. Genet. 23:150.
23. Escallon, M. H., Ferrell, R. E., and Kamboh, M. I. (1987). Genetic studies of low-abundance human plasma proteins. V. Evidence for a second orosomucoid structural locus (ORM2) expressed in plasma. Am. J. Hum. Genet. 41:418.
24. Fan, C., and Liden, S. (1994). Association between orosomucoid (ORM) types and psoriasis. Hum. Hered. 44:72.
25. Fan, C., Sikstrom, C., Beckman, G., and Beckman, L. (1993). Orosomucoid polymorphism in Finns, Swedes and Swedish Saamis. Hum. Hered. 43:272.
26. Fan, C., Nylander, P.-O., Sikstrom, C., and Thunell, M. (1995a). Orosomucoid and haptoglobin types in patients with sarcoidosis. Exp. Clin. Immunogenet. 12:31.
27. Fan, C., Nylander, P.-O., Stendahl, U., Thunell, M., and Beckman, L. (1995b). Synergistic interaction between ORM1 and C3 types in disease associations. Exp. Clin. Immunogenet. 12:92.
28. Fontanesi, L., Davoli, R., Zambonelli, P., and Russo, V. (1994). HincII and PstI reveal polymorphisms at the porcine orosomucoid (ORM) locus. Anim. Genet. 25:369. Erratum: Anim. Genet. 26:214 (1995).
29. Fukuma, Y., Kashimura, S., Umetsu, K., Yuasa, I., Nakano, B., and Nakasomo, I. (1990). Two new orosomucoid (ORM2) variants in Japanese. Hum. Hered. 40:302.
30. Furukawa, T., and Sugiyama, F. (1986). Analysis of feline plasma proteins by immunoelectrophoresis and polyacrylamide gel electrophoresis. Jpn. J. Vet. Sci. 48:643.
31. Gouffaux, M., Pastoret, P. P., Henroteaux, M., and Massip, A. (1975). Feline infectious peritonitis: Proteins of plasma and ascitic fluid. Vet. Pathol. 12:335.
32. Herve, F., Duche, J. C., Dathis, P., Marche, C., Barre, J., and Tillement, J. P. (1996). Binding of disopryamide, methadone, dipyridamole, chlorpromazine, lignocaine and progesterone to the two main genetic variants of human alpha1-acid glycoprotein - evidence for drug-binding difference between the variants and for the presence of two separate drug-binding sites on the alpha(1)-acid glycoprotein. Pharmacogenetics 6:403.
33. Imamura, H., Maruyama, T., Okabe, H., Shimada, H., and Otagiri, M. (1994). A simple and rapid fluorometric determination method of α1-acid glycoprotein in serum using quinaldine red. Pharm. Res. 11:566.
34. Itoh, H., Tamura, K., Izumi, M., Motoi, Y., Kidoguchi, K., and Funayama, Y. (1993). The influence of age and health status on serum alpha1-acid glycoprotein level of conventional and specific pathogen-free pigs. Can. J. Vet. Res. 57:74.
35. Juneja, R. K., Niini, T., Larssen, H. E. B., and Sandberg, K. (1991). Genetic polymorphism of six plasma proteins in the domestic cat. J. Hered. 82:178.
36. Kremmer, T., Boldizsar, M., Kovacs, J., Paulik, E., Bencsik, K., and Szajani, B. (1995). Determination and analysis of human serum alpha-1-acid glycoprotein by liquid Chromatographic methods. J. Liquid Chromatogr. 18:1207.
37. Kuschner, I. (1982). The phenomenon of the acute phase response. Ann. N.Y. Acad. Sci. 389:39.
38. Kuschner, I., and Mackiewicz, A. (1987). Acute phase proteins as disease markers. Dis. Markers 5:1.
39. Lee, S.-C., Chang, C.-J., Lee, Y-M., Lei, H.-Y., Laei, M.-Y., and Chen, D.-S. (1989). Molecular cloning of cDNAs corresponding to two genes of α1-acid glycoprotein and characterization of two alleles of AGP-1 in the mouse. DNA 8:245.
40. Mackiewicz, A., and Mackiewicz, K. (1995). Glycoforms of serum α1-acid glycoprotein as markers of inflammation and cancer. Glycoconjugate J. 12:241.
41. Merritt, C. M., and Board, P. G. (1988). Structure and characterization of a duplicated human α1-acid glycoprotein gene. Gene 66:97.
42. Merritt, C. M., Easteal, S., and Board, P. G. (1990). Evolution of human α1-acid glycoprotein genes and surrounding Alu repeats. Genomics 6:659.
43. Miller, I., and Gemeiner, M. (1992). Two-dimensional electrophoresis of cat sera: Protein identification by cross reacting antibodies against human serum proteins. Electrophoresis 13:450.
44. Murakami, Y., Itoh, T., Ohata, K., and Yasue, H. (1995). Assignment of α1-acid glycoprotein gene (ORM1) to swine chromosome region 1q210-q212 by fluorescence in situ hybridization. Cytogenet. Cell Genet. 70:186.
45. Nicollet, I., Lebreton, J.-P., Fontaine, M., and Hiron, M. (1981). Evidence for alpha-1-acid glycoprotein populations of different pi values after concanavalin A affinity chromatography: Study of their evolution during inflammation in man. Biochim. Biophys. Acta 668:235.
46. Ohno, K., Yuasa, I., Akaboshi, S., Itoh, M., Yoshida, K., Ehara, H., Ochiai, Y., and Takeshita, K. (1992). The carbohydrate deficient glycoprotein syndrome in three Japanese children. Brain Dev. 14:30.
47. Picornell, A., Casto, J. A., and Ramon, M. M. (1994). Serum protein polymorphism in Chuetas (Majorcan Jews) - GC, A2HS, ORM, ITI and HP. Gene Geog. 8:137.
48. Pilz, A., Moseley, H., Peters, J., and Abbott, C. (1992). Comparative mapping of mouse chromosome 4 and human chromosome 9: Lv, Orm, and Hxb are closely linked on mouse chromosome 4. Mammal. Genome 3:247.
49. Pollitt, C. C., and Bell, K. (1980). Protease inhibitor system in horses: Classification and detection of a new allele. Anim. Blood Grps. Biochem. Genet. 11:235.
50. Pollitt, C. C., and Bell, K. (1983). Characterization of the α-protease inhibitor system in Thoroughbred horse plasma by horizontal two-dimensional (ISO-DALT) electrophoresis. 1. Protein staining. Anim. Blood Grps. Biochem. Genet. 14:83.
51. Reinke, R., and Feigelson, P. (1985). Rat α1-acid glycoprotein: Gene sequence and regulation by glucocorticoids in transfected L-cells. J. Biol. Chem. 260:4397.
52. Saha, N., Undevia, J. V., Juneja, R. K., Gahne, B., and Tay, J. S. H. (1992). Polymorphism of alpha-a-acid (orosomucoid), alpha-2-HS-glycoproteins and alpha-1-B among the Parsis of India. Hum. Hered. 42:367.
53. Salzano, F. M., Umetsu, K., Yuasa, I., Black, F. L., and Suzuki, T. (1990). Isoelectric focusing studies in Brazilian Indians - uncovering variation of ORM, AHSG and IF. Jpn. J. Hum. Genet. 35:283.
54. Samak, R., Edelstein, R., and Israel, L. (1982). Immunosuppressive effect of acute-phase reactant proteins in vitro and its relevance to cancer. Cancer Immunol. Immunother. 13:38.
55. Sandiumenge, T., Vives, S., and Moral, P. (1993). Orosomucoid and haptoglobin polymorphisms in two Spanish Pyrenean populations. Gene Geog. 7:243.
56. Schmid, K. (1975). α1-Acid glycoprotein. In Putman, F. W. (ed.), The Plasma Proteins, Vol. 1, Academic Press, New York, London, p. 183.
57. Schmid, K., Kaufmann, H., Isemura, S., Bauer, F., Emura, J., Motoyama, T., Ishigoro, M., and Nanno, S. (1973). Structure of α1-acid glycoprotein. The complete amino acid sequence, multiple amino acid substitutions and homology with the immunoglobulins. Biochemistry 12:2711.
58. Taira, T., Fujinaga, T., Tamura, K., Izumi, M., Itoh, H., Tsunoda, N., Yamashita, K., Okumura, M., and Mizuno, S. (1992). Isolation and characterization of alpha-1-acid glycoprotein from horses, and its evaluation as an acute-phase reactive protein in horses. Am. J. Vet. Res. 53:961.
59. Thymann, M., and Weidinger, S. (1988). Subtyping of orosomucoid 1 (ORM1) by isoelectric focusing in agarose and polyacrylamide gels. Electrophoresis 9:380.
60. Umetsu, K., Yuasa, I., Chen, E.-R., Kudo, T., and Suzuki, T. (1988a). Orosomucoid 1 and orosomucoid 2 types in the Taiwanese and Japanese: Evidence for five new orosomucoid variants. Electrophoresis 9:224.
61. Umetsu, K., Yuasa, I., Nishimura, H., Sasaki, H., and Suzuki, T. (1988b). Genetic polymorphisms of orosomucoid and alpha-2-HS-glycoprotein in a Philippine population. Hum. Hered. 38:287.
62. Umetsu, K., Yuasa, I., Nishi, K., Brinkmann, B., and Suzuki, T. (1989a). Orosomucoid (ORM) typing by isoelectric focusing: Description of two new alleles in a German population and thermostability in bloodstains. Z. Rechstmed. 102:171.
63. Umetsu, K., Yuasa, I., Yamashita, T., Saito, S., Yamaguchi, T., Ellepola, S. B., Ishida, T., and Suzuki, T. (1989b). Genetic polymorphisms of orosomucoid and alpha-2-HS-glycoprotein in Thai, Sri Lankan and Paraguayan populations. Jpn. J. Hum. Genet. 34:195.
64. van Dijk, A., Havenaar, E. C., and Brinkman-van der Linden, B. C. M. (1995). α1-acid glycoprotein (orosomucoid): Pathophysiological changes in glycosylation in relation to its function. Glycoconjugate J. 12:227.
65. Villalobos, A. P., Ivancic, J. S., and Halsall, H. B. (1994). The lipocalin model for human orosomucoid: Support from the chromatography of orosomucoid-monoclonal antibody complexes. Chromatographia 39:475.
66. Webb, G. C., Earle, M. E., Merritt, C., and Board, P. G. (1988). Localization of human α1 acid glycoprotein gene to 9q31-q34.1. Cytogenet. Cell Genet. 47:18.
67. Yiping, H., Qing, G., and Meiyun, W. (1992). Genetic polymorphisms of alpha-2-HS-glycoprotein, group-specific component and orosomucoid in the Han population, Chengdu, China. Hum. Hered. 42:380.
68. Yuasa, I., Umetsu, K., Suenaga, K., and Robinet-Levy, M. (1986). Orosomucoid (ORM) typing by isoelectric focusing: Evidence for two structural loci ORM1 and ORM2. Hum. Genet. 74:160.
69. Yuasa, I., Suenaga, K., Umetsu, K., Ito, K., and Robinet-Levy, M. (1987). Orosomucoid (ORM) typing by isoelectric focusing: Evidence for gene duplication of ORM1 and genetic polymorphism of ORM2. Hum. Genet. 77:255.
70. Yuasa, I., Umetsu, K., and Suenaga, K. (1988). Orosomucoid (ORM) typing by isoelectric focusing: Evidence for an additional duplicated ORM1 locus haplotype and close linkage of two ORM loci. Am. J. Hum. Genet. 43:165.
71. Yuasa, I., Umetsu, K., Shotake, T., Ishida, T., Takenaka, O., Terao, K., and Kawamoto, Y. (1990a). Orosomucoid typing by isoelectric focusing: Genetic variation of Orosomucoid in Asian macaques (genus Macaca). Electrophoresis 11:840.
72. Yuasa, I., Umetsu, K., Suenaga, K., Iha, M., Hirata, H., and Ikebuchi, J. (1990b). Orosomucoid (ORM) typing by isoelectric focusing: An analysis of ORM haplotypes. Hum. Hered. 40:267.
73. Yuasa, I., Umetsu, K., Suenaga, K., Ikebuchi, J., and Suzuki, T. (1990c). Orosomucoid (ORM) typing by isoelectric focusing: Evidence for several new variants including ORM1 and ORM2 silent alleles. Vox Sang. 58:129.
74. Yuasa, I., Umetsu, K., Udono, T., Sasaoka, S., Suzuki, R., Shotake, T., Kawamoto, Y., Takenaka, O., and Nozawa, K. (1991). Orosomucoid typing of apes (Family Pongidae) by isoelectric focusing: Among primates do only humans have two functional Orosomucoid loci? Biochem. Genet. 29:525.
75. Yuasa, I., Weidinger, S., Umetsu, K., Suenaga, K., Ishimoto, G., Eap, B. C., Duche, J.-C., and Baumann, P. (1993). Orosomucoid system: 17 additional Orosomucoid variants and proposal for a new nomenclature. Vox Sang. 64:47.
76. Yuasa, I., Ohno, K., Hashimoto, K., lijima, K., Yamashita, K., and Takeshita, K. (1995). Carbohydrate-deficient glycoprotein syndrome: Electrophoretic study of multiple serum glycoproteins. Brain Dev. 17:13.