Retinol in avian oogenesis: molecular properties of the carrier protein

Normal embryo development in oviparous (egg-laying) species requires the coordinated targeting to growing oocytes of nutrients and regulatory molecules such as retinol, the precursor of active retinoids. Serum retinol-binding protein (RBP) is the major carrier protein for retinol in the circulatory system of vertebrates. In oviparous animals, RBP is thought to function in the delivery of retinol to yolk, in analogy to other important nutrients and vitamins known to accumulate within the oocyte. Here, immunoelectron microscopy revealed that RBP indeed accumulates in yolk, in particular in the electron-lucent phase of yolk organelles known to harbor other serum-derived yolk proteins and their receptors. To gain understanding of the RBP-mediated serum-to-yolk transport of retinol, we have characterized the chicken carrier protein at the molecular level. The essential function of RBPs is emphasized by the first known avian RBP structure, which confirms that these vitamin carriers are among the most highly conserved serum proteins known. Interestingly, by analysis of RBP hepatic RNA and serum protein levels, we identified a unique property of chicken RBP relative to other known RBPs and yolk precursors, i.e., the absence of estrogen induction. One cause of the observed reduction in RBP RNA is an estrogen-dependent decrease of RBP gene transcription. Furthermore, Northern blot analysis of tissues of the hen demonstrated a lack of RBP synthesis by the oocyte or other ovarian cells, confirming the exogenous (hepatic) origin of yolk RBP. These results provide strong evidence that chicken RBP is an essential serum-to-yolk vitamin carrier with certain properties different from those of other such transporters.