Lactose Synthesis

This chapter is related to lactose synthesis, its chemistry, regulation, and differences between species, especially in cattle. Lactose synthesis takes place in the Golgi apparatus of mammary epithelial cells (MEC) by the lactose synthase (LS) enzyme complex from two precursors, glucose and UDP-galactose. The enzyme complex is formed by galactosyltransferase, and it is associated with α-lactalbumin. Importantly, the lactose secreted determines the volume of milk produced, due to its osmotic properties. Milk contains 5% lactose and 80% water, percentages that remain constant during lactation in the different mammalian species. The low variation in milk lactose content indicates that lactose synthesis remains constant throughout the period of lactation and that is highly conserved in all mammals. Lactose synthesis is initiated during the first third of the pregnancy, increasing after birth and placenta removal. Different glucose transporters have been involved in mammary glucose uptake, mainly facilitative glucose transporters GLUT1, GLUT8, and GLUT12 and sodium-glucose transporter SGLT1, with more or less participation depending on mammal species.

Evolution of Pinnipedia lactation strategies: a potential role for α-lactalbumin?

Despite the considerable variation in milk composition found among mammals, a constituent common across all groups is lactose, the main sugar and osmole in most eutherians milk. Exceptions to this are the families Otariidae (fur seals and sea lions) and Odobenidae (walruses), where lactose has not been detected. We investigated the molecular basis for this by cloning α-lactalbumin, the modifier protein of the lactose synthase complex. A mutation was observed which, in addition to preventing lactose production, may enable otariids to maintain lactation despite the extremely long inter-suckling intervals during the mother's time at sea foraging (more than 23 days in some species).

A MvaI PCR-RFLP detecting a silent allele at the goat α-lactalbumin locus

Alpha-lactalbumin (α-la), a calcium metalloprotein, is one of the major serum-proteins in ruminant milk (Jenness, 1982) and induces lactose synthesis in the mammary gland by interacting with the enzyme UDP-galactosyltransferase, giving rise to the heterodimer enzyme lactose synthase (Ebner & Brodbeck, 1968; Kuhn, 1983). The goat α-la transcription unit (LALBA), located on chromosome 5 (Hayes et al. 1993), is organized in 4 exons varying in length from 75 nucleotides (3rd exon) to 329 nucleotides (4th exon) coding for a 123-amino acid polypeptide chain (Vilotte et al. 1991). According to the strong similarity between bovine α-la (Vilotte et al. 1987) and human lysozyme (similar molecular weight, the same number of S-S bonds, identical N and C terminal residues; Peters et al. 1989), it has been proposed that both genes arose from a common ancestor (Vilotte et al. 1991).