• Asian-Australasian Journal of Animal Sciences
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• v.30 no.5
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• pp.638-642
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• 2017

Objective: This study aimed to validate the statistical evidence from the genome-wide association study (GWAS) as true-positive and to better understand the effects of the glycophorin C (GYPC) gene on serum hemoglobin traits. Methods: Our initial GWAS revealed the presence of two single nucleotide polymorphisms (SNPs) (ASGA0069038 and ALGA0084612) for the hemoglobin concentration trait (HGB) in the 2.48 Mb region of SSC15. From this target region, GYPC was selected as a promising gene that associated with serum HGB traits in pigs. SNPs within the GYPC gene were detected by sequencing. Thereafter, we performed association analysis of the variant with the serum hemoglobin level in three pig populations. Results: We identified one SNP (g.29625094 T>C) in exon 3 of the GYPC gene. Statistical analysis showed a significant association of the SNP with the serum hemoglobin level on day 20 (p<0.05). By quantitative real-time polymerase chain reaction, the GYPC gene was expressed in eight different tissues. Conclusion: These results might improve our understanding of GYPC function and provide evidence for its association with serum hemoglobin traits in the pig. These results also indicate that the GYPC gene might serve as a useful marker in pig breeding programs.

• Korean Journal of Veterinary Research
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• v.29 no.1
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• pp.13-20
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• 1989

The proteins of the bovine erythrocyte membrane were analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, and their relations to the slow sedimentation rate of bovine erythrocytes were investigated by treating the erythrocytes with trypsin. The erythrocyte sedimentation rates of bovine erythrocytes from Holstein and Korean native cattle were very slow compared with the human one (1/7 as slow as the human one) as reported previously. However, when human and Holstein erythrocytes were treated with trypsin (0.2 and 0.5 mg/ml) for 1 hour at ${37^{\circ}C}$, their sedimentation rates were markedly accelerated while the sedimentation rate of Korean native cattle's erythrocytes were not affected. Although the general protein profiles of the bovine erythrocyte membranes were almost similar to that of human, bovine erythrocyte membranes showed one additional protein band, called band Q in this study, which migrated electrophoretically to the mid-position between band 2 and band 3 in human erythrocyte membranes. Treatment of Holstein and human erythrocytes with trypsin caused a decrease or disapperance of the band Q from the erythrocyte membrane. Although the band Q in Korean native cattle's erythroyte membrane was decreased by trypsin treatment of the erythrocytes, the magnitude of the decrement was not so pronounced as in the case of human and Holstein erythrocytes. The glycoprotein profiles of the bovine erythrocyte membranes revealed by periodic acid-Schiff stain showed a marked difference from that of human. The PAS-1 (glycophorin) and PAS-2 (sialoglycoprotein) present in human erythrocyte membrane were almost absent from the bovine erythrocyte membranes. Instead, the bovine erythrocyte membranes showed a strong PAS-positive band near the origin of the electrophorograms, which is named as PAS-B in this study. The PAS-B band was disappered completely by the trypsin treatment of Holstein erythrocytes whereas the PAS-B band in Korean native cattle's erythrocyte membrane still remained after the trypsin treatment. The trypsin treatment of Korean native cattle's erythrocytes, however, led to the appearance of small molecular weight peptides, indicating that the high molecular weight glycoproteins were degraded by trypsin as in human and Holstein ones. These results suggest that the slow sedimentation rate of bovine erythrocytes is due in part to the presence of band Q protein fraction and PAS-B glycoprotein in the bovine erythrocytes.