Cloned transgenic cattle produce milk with higher levels of β-casein and κ-casein

Brophy, Brigid; Smolenski, Grant; Wheeler, Thomas T.; Wells, David N.; L'Huillier, P.J.; Laible, Götz

doi:10.1038/nbt783

Cited by 235 publications

(153 citation statements)

References 40 publications

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“…Mouse models have been developed for most of the above modifications indicating the feasibility of obtaining significant alterations in milk composition but at the same time showing that unwanted side effects cannot be ruled out [83,84]. Only one full-scale study in livestock has been reported as yet [85]. The recent report showed that the casein ratio can be altered by overexpression of b-and k-casein in cattle clearly underpinning the potential for improvements in the functional properties of bovine milk [85].…”

Section: Dietary Modifications Of Animal Productsmentioning

confidence: 99%

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The contribution of farm animals to human health

Kues¹

2004

Trends in Biotechnology

117

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Section: Dietary Modifications Of Animal Productsmentioning

confidence: 99%

“…Only one full-scale study in livestock has been reported as yet [85]. The recent report showed that the casein ratio can be altered by overexpression of b-and k-casein in cattle clearly underpinning the potential for improvements in the functional properties of bovine milk [85].…”

Section: Dietary Modifications Of Animal Productsmentioning

confidence: 99%

The contribution of farm animals to human health

Kues¹

2004

Trends in Biotechnology

117

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“…Genetic manipulation of cattle with an objective to alter the milk properties is being attempted successfully (33). Given the expenses and the time scale of such experiments in livestock species, it is desirable to model the intended genetic changes in the mouse first.…”

Section: Discussionmentioning

confidence: 99%

κ-Casein-deficient mice fail to lactate

Shekar

Goel

Rani

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Acquisition of milk production capabilities by an ancestor of mammals is at the root of mammalian evolution. Milk casein micelles are a primary source of amino acids and calcium phosphate to neonates. To understand the role of -casein in lactation, we have created and characterized a null mouse strain (Csnk ؊/؊ ) lacking this gene. The mutant -casein allele did not affect the expression of other milk proteins in Csnk ؊/؊ females. However, these females did not suckle their pups and failed to lactate because of destabilization of the micelles in the lumina of the mammary gland. Thus, -casein is essential for lactation and, consequently, for the successful completion of the process of reproduction in mammals. In view of the extreme structural conservation of the casein locus, as well as the phenotype of Csnk ؊/؊ females, we propose that the organization of a functional -casein gene would have been one of the critical events in the evolution of mammals. Further, -casein variants are known to affect the industrial properties of milk in dairy animals. Given the expenses and the time scale of such experiments in livestock species, it is desirable to model the intended genetic modifications in mice first. The mouse strain that we have created would be a useful model to study the effect of -casein variants on the properties of milk and͞or milk products.casein locus ͉ evolution ͉ lactation ͉ milk ͉ micelle M ilk production is an essential component of the reproductive strategy of mammals. The development of a zygote into an organism is accompanied by the preparation of milk synthesis potential by the mammary gland. Perinatal survival in mammals is solely dependent on the availability of milk from the mother. Caseins account for Ͼ80% of the total milk proteins (1). These proteins exist as micelles, consisting of three to four phosphoproteins (i.e., the calcium-sensitive caseins: ␣-, ␤-, ␥-, and ␦-casein in mice) and a calcium-insensitive phosphoglycoprotein, -casein (2). In addition to functioning as the primary source of amino acids, one of the key functions of micelles is to sequester large amounts of calcium phosphate from the maternal diet or bodily stores and make it readily available to the newborn. Calcium-sensitive casein genes seem to have evolved from a primitive casein gene through gene duplication and exon shuffling (3); however, it appears that -casein is not related structurally and evolutionarily to these genes. Instead, it appears to be related to ␥-fibrinogen (4, 5). Recently, it has also been speculated that both the calcium-sensitive and the calciuminsensitive casein gene belong to one gene family (6). The null mutation of the ␤-casein gene in mice (7) and that of ␣ S1 -casein in goats (8) do not show any significant effect on milk micelle formation and lactation. The lack of adverse effects on micelle formation in these mutants suggests functional redundancy amongst calcium-sensitive caseins. However, the absence of ␣ S1 -casein in goats does affect the rate of transport of caseins. The experimental ev...

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“…This is expected to stabilise micelles and to favour cheese preparation [18]. Unexpectedly, this milk is slightly yellow coloured and it contains lower amounts of β-casein [19].…”

Section: Improvement Of Milk Qualitymentioning

confidence: 99%

Preparation of recombinant proteins in milk to improve human and animal health

Soler¹,

Thépot²,

Rival‐Gervier³

et al. 2006

Reprod. Nutr. Dev.

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-Milk is a very abundant source of proteins for animal and human consumption. Milk composition can be modified using transgenesis, including exogenous gene addition and endogenous gene inactivation. The study of milk protein genes has provided researchers with regulatory regions capable of efficiently and specifically driving the expression of foreign genes in milk. The projects underway are aimed at modifying milk composition, improving its nutritional value, reducing mammary infections, providing consumers with antipathogen proteins and preparing purified recombinant proteins for pharmaceutical use. The present paper summarises the current progress in this field. milk / recombinant proteins / animal and human health

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Cloned transgenic cattle produce milk with higher levels of β-casein and κ-casein

Cited by 235 publications

References 40 publications

The contribution of farm animals to human health

The contribution of farm animals to human health

κ-Casein-deficient mice fail to lactate

Preparation of recombinant proteins in milk to improve human and animal health

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