β-1,4-Galactosyltransferase Expression during Spermatogenesis: Stage-Specific Regulation by t Alleles and Uniform Distribution in +-Spermatids and t-Spermatids

Pratt, Sana Abuhamad; Shur, Barry D.

doi:10.1006/dbio.1993.1060

Cited by 15 publications

(13 citation statements)

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“…During spermatogenesis, GalT-I is synthesized by spermatogonia, primary and secondary spermatocytes, and round spermatids (Pratt and Shur, 1993;Charron et al, 1999). Interestingly, a unique transcript is synthesized in spermatocytes and round spermatids that, when translated, yields only the long form of the protein (Charron et al, 1999).…”

Section: ␤14galactosyltransferase As An Adhesion Receptormentioning

confidence: 99%

“…Interestingly, a unique transcript is synthesized in spermatocytes and round spermatids that, when translated, yields only the long form of the protein (Charron et al, 1999). As the round spermatids change their shape to that of mature sperm, GalT-I moves to the developing sperm head and becomes localized to the plasma membrane in the acrosomal region of sperm (Scully et al, 1987;Pratt and Shur, 1993). GalT-I from sperm behaves as a typical integral membrane protein with a molecular weight of 60 kDa (Shur and Neely, 1988).…”

Section: ␤14galactosyltransferase As An Adhesion Receptormentioning

confidence: 99%

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Molecular Basis of Mammalian Gamete Binding

Miller

Shi

Burkin

2002

Recent Progress in Hormone Research

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Despite the importance of fertilization for controlling human reproduction, regulating animal production, and promoting preservation of endangered species, the molecular basis underlying gamete binding and fertilization has been perplexing. More progress has been made in the mouse than in other mammals and, recently, targeted deletion of specific genes in the mouse has yielded intriguing results. This review will emphasize research performed by our laboratory and others done primarily with mouse gametes but will include some interesting observations from other mammals. Studies of murine fertilization indicate that oligosaccharides on the egg coat glycoprotein ZP3 bind sperm. The precise oligosaccharides that bind sperm are the subject of considerable debate. ZP3 also induces exocytosis of the sperm acrosome, allowing sperm to penetrate through the egg coat (zona pellucida). A number of candidate ZP3 receptors have been proposed and studies of ␤1,4galacto-syltransferase-I (GalT-I) are reviewed here in the most detail. Sperm from mice with a targeted deletion of GalT-I still are able to bind the zona pellucida but are unable to acrosome react and penetrate through the zona. Therefore, the unique role of GalT-I appears to be in signal transduction. GalT-I forms a complex with heterotrimeric G proteins and activates signaling, leading to exocytosis in sperm and in heterologous cells expressing GalT-I. Other signaling steps triggered by GalT-I are under active investigation; this receptor forms a complex with a protein kinase anchoring protein.After exocytosis of the acrosome, sperm penetrate the zona pellucida and fuse with the oocyte plasma membrane using ADAM family members on sperm and integrins on oocytes. These proteins, along with the tetraspanins on oocytes, may form a complex web at gamete fusion. Targeted deletion of specific genes in this putative complex has provided important information about their redundancy. After the oocyte is fertilized, the binding site for GalT-I is lost from ZP3, preventing additional sperm from binding to the zona pellucida. New technical advances and creative ideas offer the opportunity to make important advances and to solve the conundrum of fertilization.

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Section: ␤14galactosyltransferase As An Adhesion Receptormentioning

confidence: 99%

Section: ␤14galactosyltransferase As An Adhesion Receptormentioning

confidence: 99%

Molecular Basis of Mammalian Gamete Binding

Miller

Shi

Burkin

2002

Recent Progress in Hormone Research

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“…The most thoroughly characterized sperm surface proteins known to have specific zona pellucida-and carbohydrate-binding sites are: the mouse proteins ~l,4-galactosyltransferase (GalTase) (Miller et al, 1992) and sp56 (Bookbinder et al, 1995); the rabbit protein Sp17 (Richardson et al, 1994;Yamasaki et al, 1995); a human mannose-binding protein (Benoff, 1993); and the members of the porcine spermadhesin protein family known as AQN-1, AQN-3, and AWN Topfer-Petersen et al, 1995). Mouse GalTase, rabbit Sp17, and human mannose-binding protein are sperm type-I integral membrane proteins (Miller et al, 1992;Benoff, 1993), whereas mouse sp56 and the porcine spermadhesins are peripherally associated proteins (Cheng et al, 1994;DostAlovh et al, 1994).…”

Section: Sperm-associated Zona Pellucida-and Carbohydratebinding Protmentioning

confidence: 99%

“…l), these residues are replaced by D and Q, respectively, in mannose-like-binding CRDs (Drickamer, 1992). From these considerations, it has been proposed that rabbit Sp17, whose amino acid sequence contains some of the invariant amino acids of a C-type CRD, may belong to the subfamily of proteins with affinity for galactose (Richardson et al , 1994). On the other hand, the sequence of a complete cDNA of the human sperm mannose-binding lectin encodes a protein with seven putative mannose-like-binding CRDs (Benoff et al, 1993).…”

Section: Sperm Membrane C-type Lectinsmentioning

confidence: 99%

“…The GalTase has been found on all mammalian sperm 602 I Glycobiology of Fertilization tested so far and appears to be confined to the plasma membrane in those species whose sperm has been analyzed by subcellular fractionation (Miller et al, 1992). The GalTase gene is expressed in murine testicular germ cells and the enzyme is localized on the surface of spermatogonia, spermatocytes, and spermatids (Pratt and Shur, 1993). In spermatids, GalTase is localized in the sperm membrane overlying the acrosome.…”

Section: Mouse Sperm G14-galactosyltransferasementioning

confidence: 99%

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Glycobiology of Fertilization

Sinowatz¹,

Tpfer-Petersen²,

Calvete³

1996

Glycosciences

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Biological consequences of targeting β1,4‐galactosyltransferase to two different subcellular compartments

1995

Self Cite

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beta 1,4-galactosyltransferase is unusual among the glycosyltransferases in that it is found in two subcellular compartments where it performs two distinct functions. In the trans-Golgi complex, galactosyltransferase participates in oligosaccharide biosynthesis, as do the other glycosyltransferases. On the cell surface, however, galactosyltransferase associates with the cytoskeleton and functions as a receptor for extracellular oligosaccharide ligands. Although we now know much regarding galactosyltransferase function in these two compartments, little is known about how it is targeted to these different sites. By cloning the galactosyltransferase gene products, certain features of the protein have been identified that may be critical for its expression on the cell surface or retention within the Golgi complex. This article discusses recent studies which suggest that a cytoplasmic sequence unique to one galactosyltransferase isoform is required for targeting a portion of this protein to the plasma membrane, enabling it to function as a cell adhesion molecule. These findings allow one to manipulate surface galactosyltransferase expression, either positively or negatively, and perturb galactosyltransferase-dependent cellular interactions during fertilization and development.

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β-1,4-Galactosyltransferase Expression during Spermatogenesis: Stage-Specific Regulation by t Alleles and Uniform Distribution in +-Spermatids and t-Spermatids

Cited by 15 publications

References 0 publications

Molecular Basis of Mammalian Gamete Binding

Molecular Basis of Mammalian Gamete Binding

Glycobiology of Fertilization

Biological consequences of targeting β1,4‐galactosyltransferase to two different subcellular compartments

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