Phylogenetic Analysis of Three Lipocalin-Like Proteins Present in the Milk of Trichosurus vulpecula (Phalangeridae, Marsupialia)

Piotte, Christine; Hunter, Airlie; Marshall, Craig J.; Grigor, Murray R.

doi:10.1007/pl00006313

Cited by 34 publications

(19 citation statements)

References 26 publications

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“…in cow's milk), and WAP (e.g. in rat milk), but additional whey proteins have been identified in marsupials, such as early lactation protein, late lactation protein, and trichosurin (Nicholas et al, 1987;Piotte and Grigor, 1996;Demmer et al, 1998;Piotte et al, 1998).…”

Section: Evolution Of Milk Secretionmentioning

confidence: 99%

“…A b-lactoglobulin pseudogene is also suspected in the human genome, but there may be confusion with the glycodelin gene (Kontopidis et al, 2004). Other lipocalins (trichosurin, late lactation protein) are expressed in marsupial milk (Demmer et al, 1998;Piotte et al, 1998); however, these are only distantly related to b-lactoglobulin and are apparently of more recent origin (Ganfornina et al, 2000).…”

Section: Evolution Of Milk Secretionmentioning

confidence: 99%

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The evolution of milk secretion and its ancient origins

Oftedal

2012

Animal

205

142

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Lactation represents an important element of the life history strategies of all mammals, whether monotreme, marsupial, or eutherian. Milk originated as a glandular skin secretion in synapsids (the lineage ancestral to mammals), perhaps as early as the Pennsylvanian period, that is, approximately 310 million years ago (mya). Early synapsids laid eggs with parchment-like shells intolerant of desiccation and apparently dependent on glandular skin secretions for moisture. Mammary glands probably evolved from apocrine-like glands that combined multiple modes of secretion and developed in association with hair follicles. Comparative analyses of the evolutionary origin of milk constituents support a scenario in which these secretions evolved into a nutrient-rich milk long before mammals arose. A variety of antimicrobial and secretory constituents were co-opted into novel roles related to nutrition of the young. Secretory calcium-binding phosphoproteins may originally have had a role in calcium delivery to eggs; however, by evolving into large, complex casein micelles, they took on an important role in transport of amino acids, calcium and phosphorus. Several proteins involved in immunity, including an ancestral butyrophilin and xanthine oxidoreductase, were incorporated into a novel membrane-bound lipid droplet (the milk fat globule) that became a primary mode of energy transfer. An ancestral c-lysozyme lost its lytic functions in favor of a role as a-lactalbumin, which modifies a galactosyltransferase to recognize glucose as an acceptor, leading to the synthesis of novel milk sugars, of which free oligosaccharides may have predated free lactose. An ancestral lipocalin and an ancestral whey acidic protein four-disulphide core protein apparently lost their original transport and antimicrobial functions when they became the whey proteins b-lactoglobulin and whey acidic protein, which with a-lactalbumin provide limiting sulfur amino acids to the young. By the late Triassic period (ca 210 mya), mammaliaforms (mammalian ancestors) were endothermic (requiring fluid to replace incubatory water losses of eggs), very small in size (making large eggs impossible), and had rapid growth and limited tooth replacement (indicating delayed onset of feeding and reliance on milk). Thus, milk had already supplanted egg yolk as the primary nutrient source, and by the Jurassic period (ca 170 mya) vitellogenin genes were being lost. All primary milk constituents evolved before the appearance of mammals, and some constituents may have origins that predate the split of the synapsids from sauropsids (the lineage leading to 'reptiles' and birds). Thus, the modern dairy industry is built upon a very old foundation, the cornerstones of which were laid even before dinosaurs ruled the earth in the Jurassic and Cretaceous periods.Keywords: evolution, lactation, milk composition, casein, milk fat globule ImplicationsLactation has an evolutionary origin and biological context within which its secretory processes and milk constituents evolved. This revi...

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Section: Evolution Of Milk Secretionmentioning

confidence: 99%

Section: Evolution Of Milk Secretionmentioning

confidence: 99%

The evolution of milk secretion and its ancient origins

Oftedal

2012

Animal

205

142

View full text Add to dashboard Cite

show abstract

“…Gel electrophoresis studies of possum milk proteins, carried out on a limited number of samples, showed that early lactation protein, late lactation protein and transferrin are differentially expressed between phase 2 and 3 of lactation (Grigor et al 1991, Piotte & Grigor 1996, Piotte et al 1997a. The aim of this study was to determine the developmental expression pattern of eight major milk protein genes throughout lactation in the possum using RNA slot blotting techniques.…”

Section: Introductionmentioning

confidence: 99%

“…In phase 3 of lactation, milk production is at a peak and growth of the pouch young is greatest. We have recently cloned cDNAs for eight different milk protein genes which are abundantly expressed in the possum mammary gland (Piotte & Grigor 1996, Piotte et al 1997a observations). Some of these genes are homologues of proteins found in the milk of eutherian mammals, e.g.…”

Section: Introductionmentioning

confidence: 99%

“…In addition to these, there are three novel possum milk protein genes: early lactation protein, trichosurin and late lactation protein. The early lactation protein has sequence homology with the Kunitz family of protease inhibitors (Piotte & Grigor 1996) whereas late lactation protein and trichosurin, along with -lactoglobulin, belong to the lipocalin family of secretory ligand-binding proteins (Piotte et al 1997a). The possum late lactation protein is a homologue of a tammar wallaby (Macropus eugenii) whey protein which is only expressed in phase 3 of lactation (Nicholas et al 1987, Collet et al 1989).…”

Section: Introductionmentioning

confidence: 99%

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Differential expression of milk protein genes during lactation in the common brushtail possum (Trichosurus vulpecula)

Demmer

Ik²,

Ginger³

et al. 1998

Journal of Molecular Endocrinology

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In the common brushtail possum (Trichosurus vulpecula) lactation lasts for 200 days and consists of two distinct phases. Milk composition changes dramatically between phase 2 and 3, which correspond to early and late lactation respectively (phase 1 corresponds to pregnancy). RNA expression patterns have been established for eight major milk protein genes throughout lactation in possum mammary glands. The levels of mRNA expressed from two genes, encoding the early and late lactation proteins, were differentially regulated during lactation, with peak RNA levels occurring in phase 2 and 3 of lactation respectively. Expression of these two RNA transcripts did not overlap, and neither gene was expressed at significant levels between days 116 to 125, suggesting that the transition from phase 2 to phase 3 of lactation occurs at this time. The level of lysozyme, -lactalbumin and trichosurin mRNA increased in phase 3 of lactation, whereas the levels of -lactoglobulin, -casein and -casein mRNA remained constant throughout lactation. In the non-suckled gland, expression of milk protein genes was greatly reduced by day 6 of lactation. In conclusion, the early and late lactation protein genes are good markers for phase 2 and 3 of lactation, with the transition between these phases occurring around day 120 of lactation in the possum.

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β-Lactoglobulin

Sawyer¹

2003

Advanced Dairy Chemistry—1 Proteins

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Phylogenetic Analysis of Three Lipocalin-Like Proteins Present in the Milk of Trichosurus vulpecula (Phalangeridae, Marsupialia)

Cited by 34 publications

References 26 publications

The evolution of milk secretion and its ancient origins

The evolution of milk secretion and its ancient origins

Differential expression of milk protein genes during lactation in the common brushtail possum (Trichosurus vulpecula)

β-Lactoglobulin

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