Molecular Cloning and Characterization of P47, a Novel Boar Sperm-Associated Zona Pellucida-Binding Protein Homologous to a Family of Mammalian Secretory Proteins1

Ensslin, Michael A.; Vogel, Tanja; Calvete, Juan J.; Thole, Hubert; Schmidtke, Jörg; Matsuda, Tsukasa; Töpfer‐Petersen, Edda

doi:10.1095/biolreprod58.4.1057

Cited by 83 publications

(73 citation statements)

References 27 publications

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“…In summary, SED1 appears to facilitate a diverse range of cellular interactions as varied as sperm-egg binding (10,23), macrophage clearance of apoptotic lymphocytes (24,25) and mammary epithelial cells (8,9), and mammary gland branching morphogenesis (current study). That SED1 may represent one member of a family of similar bi-motif signaling proteins is illustrated by the homologous protein Del1, which participates in endothelial adhesion to basal lamina during vascularization (17).…”

Section: Discussionmentioning

confidence: 75%

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The EGF repeat and discoidin domain protein, SED1/MFG-E8, is required for mammary gland branching morphogenesis

Ensslin

Shur

2007

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

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SED1, also known as MFG-E8, is a secreted protein composed of two EGF repeats (the second of which contains an RGD motif) and two discoidin/Factor V/VIII C domains. SED1 is expressed by a wide range of cell types, where it participates in diverse cellular interactions, such as sperm binding to the egg coat and macrophage recognition of apoptotic lymphocytes. Although SED1 was originally identified as a milk protein, its function in the mammary gland remains unclear; suggested functions include inhibition of viral infection and clearance of apoptotic cells during mammary gland involution. We report here that SED1 has an unexpected obligatory role during mammary gland development. Unlike that seen in WT glands, SED1-null glands show severely reduced branching from epithelial ducts and from terminal end buds, which are thin and poorly developed. SED1 is expressed by both luminal and myoepithelial cells in the developing epithelial duct, and binds to ␣v integrin receptors on myoepithelial cells leading to MAPK activation and cell proliferation. The absence of SED1 leads to greatly reduced levels of activated MAPK and a concomitant reduction in cell proliferation and branching throughout the epithelial tree. These results suggest that SED1 contributes, at least partly, to the intercellular signaling between luminal and myoepithelial cells that is required for branching morphogenesis.cell adhesion ͉ epithelia ͉ integrins

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Section: Discussionmentioning

confidence: 75%

“…(Error bars, SD.) (10,23) and macrophage-lymphocyte interactions (24,25), plays an obligatory role in branching morphogenesis as well.…”

Section: Discussionmentioning

confidence: 99%

The EGF repeat and discoidin domain protein, SED1/MFG-E8, is required for mammary gland branching morphogenesis

Ensslin

Shur

2007

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

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“…Interestingly, a number of proteins that were detected as zona binding proteins from the APM were highly specific for the clustered DRM. These identified proteins were also described in the literature as zona binding proteins, including: AQN-3 (also known as spermadhesin; Calvete et al, 1996), P47 (the porcine homologue of SED1, Ensslin et al, 1998;Ensslin and Shur, 2007) and fertilin beta (Yamagata et al, 2002). Fertilin-beta is a transmembrane protein thought to function as an adhesion molecule for the zona pellucida; it was shown to have no function in sperm-egg membrane fusion as reported previously (Yamagata et al, 2002).…”

Section: Sperm Membrane Microdomains and The Zona Bindingmentioning

confidence: 81%

Sperm head membrane reorganisation during capacitation

Gadella¹,

Tsai²,

Boerke³

et al. 2008

Int. J. Dev. Biol.

173

150

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The sperm cell has a characteristic polarized morphology and its surface is also highly differentiated into different membrane domains. Junctional protein ring structures seal the surface of the mid-piece from the head and the tail respectively and probably prevent random diffusion of membrane molecules over the protein rings. Despite the absence of such lateral diffusion-preventing structures, the sperm head surface is also highly heterogeneous. Furthermore, lipid and membrane protein ordering is subjected to changes when sperm become capacitated. The forces that maintain the lateral polarity of membrane molecules over the sperm surface, as well as those that cause their dynamic redistribution, are only poorly understood. Nevertheless, it is known that each of the sperm head surface regions has specific roles to allow sperm to fertilize the oocyte: a specific region is devoted to zona pellucida binding, a larger area of the sperm head surface is involved in the acrosome reaction (intracellular fusion), while yet another region is involved in egg plasma membrane binding and fertilization fusion (intercellular membrane fusion). All three events occur in the area of the sperm head where the plasma membrane covers the acrosome. Recently, lipid ordered microdomains (lipid rafts) were discovered in membranes of many biological specimens including sperm. In this review, we cover the latest insights about sperm lipid raft research and discuss how sperm lipid raft dynamics may relate to sperm-zona binding and the zona-induced acrosome reaction.

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“…Another interesting case of a DS domain protein mediating cellular interactions is the apparent involvement of P47 (identical to milk fat globule) in fertilization. This protein was detected on the acrosomal cap of testicular sperm and on spermatozoa bound to zona pellucida (Ensslin et al, 1998) suggesting an active role in binding of the sperm to the zona pellucida. Finally, the Dl domain of GOase, which was shown to have weak galactosebinding activity, was proposed to function as an anchor fixing the enzyme to carbohydrates of the cell walls of a tree, the natural habitat of the fungus from which the protein was purified.…”

Section: Evolutionary Andfunctional Implicationsmentioning

confidence: 96%

The discoidin domain family revisited: New members from prokaryotes and a homology‐based fold prediction

Hofmann²,

et al. 1998

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Abstract:Members of the discoidin (DS) domain family, which includes the CI and C2 repeats of blood coagulation factors V and VIII, occur in a great variety of eukaryotic proteins, most of which have been implicated in cell-adhesion or developmental processes. So far, no three-dimensional structure of a known example of this extracellular module has been determined, limiting the usefulness of identifying a new sequence as member of this family. Here, we present results of a recent search of the protein sequence database for new DS domains using generalized profiles, a sensitive multiple alignment-based search technique. Several previously unrecognized DS domains could be identified by this method, including the first examples from prokaryotic species. More importantly, we present statistical, structural, and functional evidence that the Dl domain of galactose oxidase whose three-dimensional structure has been determined at 1.7 A resolution, is a distant member of this family. Taken together, these findings significantly expand the concept of the DS domain, by extending its taxonomic range and by implying a fold prediction for all its members. The proposed alignment with the galactose oxidase sequence makes it possible to construct homology-based three-dimensional models for the most interesting examples, as illustrated by an accompanying paper on the CI and C2 domains of factor V.

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Molecular Cloning and Characterization of P47, a Novel Boar Sperm-Associated Zona Pellucida-Binding Protein Homologous to a Family of Mammalian Secretory Proteins1

Cited by 83 publications

References 27 publications

The EGF repeat and discoidin domain protein, SED1/MFG-E8, is required for mammary gland branching morphogenesis

The EGF repeat and discoidin domain protein, SED1/MFG-E8, is required for mammary gland branching morphogenesis

Sperm head membrane reorganisation during capacitation

The discoidin domain family revisited: New members from prokaryotes and a homology‐based fold prediction

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