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due to an open reading frame on the BAT-specific uncoupling protein 1 ( UCP1 ) gene in the porcine species meaning that UCP1 is not expressed ( Berg et al . 2006 ). However, it has more recently been suggested that BAT is present in young piglets
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cloning of porcine MC3R Sequence analysis performed with DNAman program (Lynnon Corp., Quebec, Canada) suggested that the putative coding region of the pMC3R gene consists of a single exon of 960 bp. Thus, the pMC3R coding region was amplified directly
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made up of 392, 394, and 395 amino acids, respectively; they exhibit approximately 40% homology with α1-antitrypsin and are related to the serine protease inhibitor family. Previous studies found vaspin in human, mice, bovine, and porcine tissues
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Not only has the primary structure of porcine (thyro)calcitonin (CT) been elucidated but also the synthesis of the hormone has been reported (Rittel, Brugger, Kamber, Riniker & Sieber, 1968). Radioimmunoassays have been described by Deftos, Lee & Potts (1968), Arnaud, Tsao & Kaplan (1968) and Tashjian & Melvin (1968). The purpose of this communication is to report on the application of a highly sensitive radioimmunoassay to the study of the site of immunological activity within the porcine CT molecule and the extent of cross-reactivity between human and porcine CT.
A partially purified CT preparation from porcine thyroid glands, which had a biological activity of 8 MRC units/mg., was used for immunization. Five rabbits received an i.m. injection of 0·2 mg. of this material at 4-week intervals. The hormone was adsorbed on to aluminium hydroxide gel (Superfos Exp. Co, Copenhagen) and 0·5 ml. of the mixture (containing about 8 mg. Al(OH)
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-responsive ( Kuhl et al. 1980 ). Islets from neonatal animals like pigs provide an interesting model to study the effects of high glucose exposure on β-cell function and survival as well as differentiation from precursors. Neonatal porcine islets contain
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of IGFBP-5 as well as putative IGFBP-5 receptors may be responsible for the IGF-independent actions of IGFBP-5 on cells. IGFBP-5 is produced by myogenic cell lines, porcine embryonic myogenic cells (PEMCs), and porcine muscle satellite cells
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cumulus-enclosed oocyte maturation. EGF, by the same receptor EGFR as that of EGF-like factors ( Harris et al . 2003 ), has also been shown to mimic FSH-induced porcine oocyte meiotic maturation and development competence of oocytes ( Singh et al . 1993
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SUMMARY
Porcine parathyroid hormone has been isolated and purified. Its size and charge properties are similar to those of bovine and human parathyroid hormones and in a bioassay system the response to porcine hormone is parallel to that of bovine parathyroid hormone. Porcine parathyroid hormone has been labelled with 125I. The immunological properties of the porcine hormone were compared with human and bovine parathyroid hormone in a radioimmunoassay system using antisera against bovine parathyroid hormone. When labelled bovine parathyroid hormone was used as a tracer in the radioimmunoassay, porcine parathyroid hormone could be shown to differ immunologically from the hormones of the other two species. When labelled porcine hormone was used as tracer, it was displaced equally well by hormone from all three species, so that in addition to regions of difference in the molecule there are probably regions of similarity.
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ABSTRACT
Differential binding of homologous and heterologous prolactin was investigated in porcine mammary tissue. Specific binding of ovine prolactin to porcine mammary membranes or tissue slices was significantly greater than specific binding of the homologous porcine prolactin. Ovine prolactin was also more potent than porcine prolactin in stimulating proliferation of Nb2 cells. In contrast, stimulation of glucose metabolism in porcine mammary explants by porcine prolactin was greater than that by ovine prolactin. Differences in specific binding were probably not due to damage during iodination, as low concentrations of iodinated prolactins were similar to unlabelled prolactins in their abilities to stimulate proliferation of Nb2 cells. Furthermore, electrophoretic analysis of medium from binding reactions suggested that differences in specific binding were not due to proteolytic cleavage of the homologous prolactin into large (> 10 kDa) fragments. These studies suggest that ovine prolactin either binds to sites in addition to the authentic lactogenic receptor in porcine mammary tissue or that a significantly higher affinity of ovine prolactin for the porcine lactogenic receptor has little effect on its biological activity.
Journal of Endocrinology (1991) 130, 43–51
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). Using normal porcine thyrocytes as a culture model, we aimed to detect conditions under which no dedifferentiating effects on normal thyrocytes were observed and to detect effects that may be initiated after short periods of incubation. We determined
