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Secretory characteristics of the ghrelin profile for the pig are still unknown. Our objective was to clarify the mechanisms that influence ghrelin secretion during differing feeding patterns. Pigs were initially fed a commercial pelleted diet offered ad libitum and blood samples collected for 24 h at intervals of 1 h. The pigs were then entrained for 17 days to a twice daily interval feeding regimen (0900-1000 and 1600-1700 h) and blood samples were collected for 12 h (0800-2000 h). This was followed by a similar interval feeding and blood sampling regimen with the 0900-1000 h feeding period being replaced by a sham feed where pigs were shown their usual feed but none offered. During the ad libitum feeding regimen, there was no preprandial rise or postprandial fall in circulating plasma total ghrelin concentration, which remained constant throughout the sampling period. In addition, no preprandial rise or postprandial fall in ghrelin concentrations was observed when pigs were fed either twice or once daily; however, plasma ghrelin concentration rose gradually over the 12-h sampling period during the twice daily feeding regimen and increased further when pigs were fed once per day. This increase in ghrelin levels coincided with an increase in plasma GH and non-esterified fatty acid concentrations and was not associated with either plasma glucose or insulin concentrations. These results suggest that circulating total plasma ghrelin concentrations in the pig appear to be influenced by chronic changes in energy balance rather than the feeding pattern per se.

The effect of daily administration of ovine GH for a period of 4 weeks on somatomedin-C biological activity in plasma was investigated in mature Merino sheep fed a maintenance energy intake (low plane; LP) or 1.6 times this amount (high plane; HP). The GH treatment resulted in a significant (P less than 0.05) increase in plasma GH levels in blood samples collected 23.5 h after each daily injection in both LP and HP groups. Plasma concentrations of somatomedin-C activity and insulin were significantly stimulated to a maximum level by the third GH injection and remained at this level for 7 days. Subsequently, circulating levels of both hormones fell to 40-50% of the peak response to GH and returned to basal levels within 48 h of the cessation of GH injections. In the HP group the response of plasma insulin and somatomedin-C activity to GH injection was greater than in the LP group.

Specific receptor sites for murine epidermal growth factor (EGF) have been characterized and their distribution determined in ovine skin. Binding of 125I-labelled EGF to skin membrane particles was temperature- and time-dependent, with equilibrium being reached within 1 h at 23 degrees C. Analysis of skin biopsies collected from ten castrated Merino sheep demonstrated the presence of a single class of saturable, high-affinity binding sites with a dissociation constant of 64 +/- 4 (S.E.M.) pmol/l and a binding capacity of 33.8 +/- 4.5 fmol/mg protein. Skin particle binding of 125I-labelled EGF was inhibited equipotently by mouse salivary gland EGF, EGF produced by recombinant DNA procedures and urogastrone. The EGF peptides 1-48, 6-53 and 7-53, derived from the native molecule by enzymatic cleavage, were much less potent. The relative binding potency of these molecules was correlated with their ability to induce precocious eyelid opening in mice and to inhibit wool follicle activity. Synthetic fragments representing the major structural domains of the EGF molecule (EGF(29-44), EGF(33-42) and EGF(3-31] were inactive in both the receptor and bioassays. Autoradiography of skin sections incubated with 125I-labelled EGF in vitro or of sections from skin which was perfused with 125I-labelled EGF in vivo demonstrated that EGF receptors were localized in undifferentiated cells of the epidermis and sebaceous glands, the inner and outer root sheath and bulb of wool follicles and in dermal arterioles. Differences in receptor concentration were observed between follicles following in-vivo perfusion of 125I-labelled EGF but not when the in-vitro labelling technique was used. The presence of receptors in these regions is consistent with the morphological changes in sheep skin in response to EGF administration which have been reported previously.