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Phenotypes of TGFß Knockout Mice

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Cytokine Knockouts

Part of the book series: Contemporary Immunology ((CONTIM))

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Abstract

The transforming growth factor-ß (TGFß) family consists of structurally related polypeptides that mediate important physiological processes. Significant advances have been made recently in understanding the functions of these molecules in vivo by the targeted ablation of various members of the super gene family. The family members include the TGF(is, activins, inhibins, bone morphogenetic proteins, Müllerian-inhibiting substance, nodal, dorsalin,and the products of the Drosophila decapentaplegic, and Xenopus Vg-1 genes (for review see refs. 1–4). Recently, the growth differentiation factor (GDF) family of proteins, a new member of the TGFβ family, has been described (5–7). TGFβl was first isolated from human platelets (8) and the cDNA sequence was later determined (9). TGFß 1 is a disulfide-linked homo-dimer of two 112 amino acid chains. Each chain is synthesized as the C-terminal domain of a 390 amino acid precursor. It has the characteristics of a secretory polypeptide, contains a hydrophobic signal sequence for translocation across the endoplasmic reticulum, and is glycosylated. The precursor cleavage site is a sequence of four basic amino acids immediately preceding the bioactive domain (9).

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Kallapur, S., Shull, M., Doetschman, T. (1998). Phenotypes of TGFß Knockout Mice. In: Durum, S.K., Muegge, K. (eds) Cytokine Knockouts. Contemporary Immunology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4757-2753-1_19

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