Pietrain swine homozygous for the hal gene (n) associated with porcine stress syndrome (PSS) and a Pietrain-derivative breed, Near Pietrain (NP), with a frequency of .31 for n, were mated to produce reciprocal F1, F2, and purebred NP litters. The halothane challenge test was performed on all 40 parents and 240 progeny to predict their hal genotype and PSS susceptibility. The DNA-based assay for a C to T mutation at base pair 1,843 of the skeletal muscle ryanodine receptor (ryr1) cDNA, which is very highly correlated with PSS, was also determined for these animals. The predicted hal genotypes observed in the progeny differed significantly from the expected Mendelian ratios, and the halothane challenge test consistently overestimated the n/n hal genotype. However, the ryr1 genotypes observed in the progeny did not differ significantly from the expected Mendelian ratios, and this DNA-based assay apparently misidentified only one of the 40 parents. The results of this study indicate that the assay for the ryr1 mutation more accurately predicts both the homozygous and heterozygous forms of the PSS gene than does the halothane challenge test.
One hundred thirty-one pigs representing seven different breed groups (Minnesota No. 1 [M], Pietrain [P], Yorkshire [Y], and crosses PY, P[PY], P[NP], and P[YP]P) and three halothane gene genotypes (NN, Nn, and nn) were tested for breed, sex, and halothane gene (HAL) effects on growth and carcass performance. Breed effects were significant for all traits measured. Sex effect was significant for most traits except for meat scores. The HAL-locus linkage group explained 20 to 30% of the total variation for meat quality scores and 1 to 10% for meat quantity and growth traits. Pietrain x Yorkshire was the fastest growing breed group and had relatively good carcass quality. Pietrain and its related crosses had the most lean muscle but the lowest meat quality. The HN (HAL negative, genotype Nn) individuals within the PPY and PNP groups grew more quickly and had higher meat quality scores and less muscling than HP (HAL positive, genotype nn) individuals. A second experiment with 40 pigs showed significant differences in fat concentration in the loin muscle between breeds (M, Y, and P) and between genotypes within the NP population (NP[HP] and NP[HN]). The phenotypic correlation between fat percentage and marbling was .59 (P less than .01). The NP(HP) had higher water percentage in lean than the NP(HN). The water percentage was negatively correlated with meat quality scores of color, firmness, and marbling with phenotypic correlations of -.10, -.23, and -.57 (P less than .01), respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
Pigs heterozygous for the halothane-sensitivity gene exhibit a distinct phenotype with regard to both in vivo and in vitro muscle responses to halothane (E. M. Gallant, J. R. Mickelson, B. D. Roggow, S. K. Donaldson, C. F. Louis, and W. E. Rempel. Am. J. Physiol. 257 (Cell Physiol. 26): C781-C786, 1989). In this paper heavy sarcoplasmic reticulum (SR) preparations were isolated from the muscles of pigs of all three genotypes. The rate of calcium release from SR of pigs homozygous for the halothane-sensitivity gene was approximately twice that of SR from pigs homozygous for the normal allele. Furthermore, in the presence of 6 microM Ca2+, the binding of [3H]ryanodine to SR isolated from the homozygous halothane-sensitive pigs was of a higher affinity than was the binding to SR isolated from the homozygous normal pigs (Kd = 70-90 vs. 265 nM, respectively). The SR from pigs heterozygous for the halothane-sensitivity gene, however, demonstrated intermediate values for the rate of calcium release and the affinity for [3H]ryanodine (Kd = 192 nM). Thus the alterations in heavy SR calcium release and [3H]ryanodine binding in the pigs containing one copy of the halothane-sensitivity gene demonstrate a distinct heterozygote phenotype. These data also suggest that the protein product of this gene is closely associated with, and perhaps identical to, the SR calcium release channel-ryanodine receptor protein.
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