The cell types of the pars tuberalis (PT) are the follicular cells, the pars distalis cells and the so-called PT-specific cells. The latter are distinct endocrine cells displaying melatonin receptors. Although the nature of the secretory product(s) of the PT-specific cells has not yet been clarified, the function of these cells has started to be unfolded. For practical reasons, previous authors have designated the, as yet, unidentified PT hormone(s) as tuberalin(s). PT-specific cells synthesise the common alpha subunit of the pars distalis glycoprotein hormones, and it has been suggested that tuberalin would correspond to the beta chain of a specific glycoprotein secreted by these cells. The aims of the present investigation were to identify the compounds secreted by the specific cells of bovine PT, and to establish their cellular and subcellular distribution. For this purpose, proteins secreted into the culture medium of PT explants were separated by electrophoresis and used to raise antibodies. Two of these proteins, with an apparent molecular mass of 21 and 72, generated antibodies (Ab-21 and Ab-72) that differentially immunoreacted with PT-specific cells. These two antibodies were used for immunoblotting of conditioned medium and of PT explants, and for light and electron microscopy immunocytochemistry. In immunoblots, Ab-21 reacted with compounds of 21, 22, 47 and 52 kDa, whereas Ab-72 revealed a compound of 72 kDa only. Ab-72 immunoreactive material corresponded to a protein, here designated as tuberalin I, secreted by a small population of PT-specific cells (type 2 cells), and stored in 140 nm secretory granules. Immunoreactive tuberalin I was missing from bovine pars distalis and from rat PT. The predominant population of PT-specific cells (type 3 cells) secreted and stored, within 280 nm secretory granules, an Ab-21 immunoreactive protein, here designated as tuberalin II. All cells of rat PT immunoreacted with Ab-21. In the cells of bovine and rat PT, immunoreactive tuberalin II was mostly confined to a paranuclear spot; this spot also bound wheat germ agglutinin and reacted with an antibody against the alpha chain of glycoprotein pars distalis hormones. It is suggested that tuberalin II would correspond to the beta chain of a specific glycoprotein secreted by type 3 PT-specific cells. In bovine PT, the cells displaying immunoreactive tuberalins I and II did not react with any of the antibodies against pars distalis hormones.

The present study aimed to determine whether porcine genotype and/or postnatal age influenced mRNA abundance or protein expression of uncoupling protein (UCP)2 or 3 in subcutaneous adipose tissue (AT) and skeletal muscle (SM) and the extent to which these differences are associated with breed-specific discordance in endocrine and metabolic profiles. Piglets from commercial and Meishan litters were ranked according to birth weight. Tissue samples were obtained from the three median piglets from each litter on either day 0, 4, 7, 14 or 21 of neonatal life. UCP2 protein abundance in AT was similar between genotypes on the first day of life, but it was elevated at all subsequent postnatal ages (P<0.05) in AT of Meishan piglets. In contrast, UCP2 mRNA abundance was lower in Meishans up to 14 days of age. UCP2 mRNA expression was not correlated with protein abundance in either breed at any age. UCP3 mRNA in AT was similar between breeds up to day 7; thereafter, expression was higher (general linear model, P<0.05) in Meishan piglets. Conversely, UCP3 mRNA expression in SM was higher in commercial piglets after day 7. Colonic temperature remained lower in Meishan than commercial piglets throughout the study; this was most obvious in the immediate post-partum period when Meishan piglets had lower (P<0.05) plasma triiodothyronine. In conclusion, we have demonstrated that porcine genotype influences the expression and abundance of UCP2 and 3, an influence which may, in part, be due to the distinctive endocrine profiles associated with each genotype.

Many tissues undergo a rapid transition after birth, accompanied by dramatic changes in mitochondrial protein function. In particular, uncoupling protein (UCP) abundance increases at birth in the lung and adipose tissue, to then gradually decline, an adaptation that is important in enabling normal tissue function. Leptin potentially mediates some of these changes and is known to promote the loss of UCP1 from brown fat but its effects on UCP2 and related mitochondrial proteins (i.e. voltage-dependent anion channel (VDAC) and cytochrome c) in other tissues are unknown. We therefore determined the effects of once-daily jugular venous administration of ovine recombinant leptin on mitochondrial protein abundance as determined by immunoblotting in tissues that do (i.e. the brain and pancreas) and do not (i.e. liver and skeletal muscle) express UCP2. Eight pairs of 1-day-old lambs received either 100 μg leptin or vehicle daily for 6 days, before tissue sampling on day 7. Administration of leptin diminished UCP2 abundance in the pancreas, but not the brain. Leptin administration had no affect on the abundance of VDAC or cytochrome c in any tissue examined. In leptin-administered animals, but not controls, UCP2 abundance in the pancreas was positively correlated with VDAC and cytochrome c content, and UCP2 abundance in the brain with colonic temperature. In conclusion, leptin administration to neonatal lambs causes a tissue-specific loss of UCP2 from the pancreas. These effects may be important in the regulation of neonatal tissue development and potentially for optimising metabolic control mechanisms in later life.