Allurin: Exploring the Activity of a Frog Sperm Chemoattractant in Mammals

Burnett, Lindsey A.; Sugiyama, Hitoshi; Washburn, Catherine; Bieber, Allan L.; Chandler, Douglas E.

doi:10.1007/978-4-431-54589-7_4

Cited by 2 publications

(1 citation statement)

References 62 publications

(91 reference statements)

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“…In addition, the sperm fused only after the acrosome reaction, when PA levels increase. The authors conclude that the sperm equatorial segment “is the primary domain of spermatozoa membranes that harbours the fusogenic capacity of sperm.” In Xenopus fertilization, sperm are attracted to the egg by release of allurin which binds at the equatorial segment of sperm (Burnett et al, 2014). …”

Section: Pld and Pa Are Associated With Membrane Fusionmentioning

confidence: 99%

Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development

Stith

2015

Developmental Biology

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This review emphasizes how lipids regulate membrane fusion and the proteins involved in three developmental stages: oocyte maturation to the fertilizable egg, fertilization and during first cleavage. Decades of work show that phosphatidic acid (PA) releases intracellular calcium, and recent work shows that the lipid can activate Src tyrosine kinase or phospholipase C during Xenopus fertilization. Numerous reports are summarized to show three levels of increase in lipid second messengers inositol 1,4,5-trisphosphate and sn 1,2-diacylglycerol (DAG) during the three different developmental stages. In addition, possible roles for PA, ceramide, lysophosphatidylcholine, plasmalogens, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 4,5-bisphosphate, membrane microdomains (rafts) and phosphatidylinositol 3,4,5-trisphosphate in regulation of membrane fusion (acrosome reaction, sperm-egg fusion, cortical granule exocytosis), inositol 1,4,5-trisphosphate receptors, and calcium release are discussed. The role of six lipases involved in generating putative lipid second messengers during fertilization is also discussed: phospholipase D, autotaxin, lipin1, sphingomyelinase, phospholipase C, and phospholipase A2. More specifically, proteins involved in developmental events and their regulation through lipid binding to SH3, SH4, PH, PX, or C2 protein domains is emphasized. New models are presented for PA activation of Src (through SH3, SH4 and a unique domain), that this may be why the SH2 domain of PLCγ is not required for Xenopus fertilization, PA activation of phospholipase C, a role for PA during the calcium wave after fertilization, and that calcium/calmodulin may be responsible for the loss of Src from rafts after fertilization. Also discussed is that the large DAG increase during fertilization derives from phospholipase D production of PA and lipin dephosphorylation to DAG.

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Section: Pld and Pa Are Associated With Membrane Fusionmentioning

confidence: 99%

Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development

Stith

2015

Developmental Biology

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Tracing the Evolutionary History of the CAP Superfamily of Proteins Using Amino Acid Sequence Homology and Conservation of Splice Sites

Abraham

Chandler

2017

J Mol Evol

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Proteins of the CAP superfamily play numerous roles in reproduction, innate immune responses, cancer biology, and venom toxicology. Here we document the breadth of the CAP (Cysteine-RIch Secretory Protein (CRISP), Antigen 5, and Pathogenesis-Related) protein superfamily and trace the major events in its evolution using amino acid sequence homology and the positions of exon/intron borders within their genes. Seldom acknowledged in the literature, we find that many of the CAP subfamilies present in mammals, where they were originally characterized, have distinct homologues in the invertebrate phyla. Early eukaryotic CAP genes contained only one exon inherited from prokaryotic predecessors and as evolution progressed an increasing number of introns were inserted, reaching 2-5 in the invertebrate world and 5-15 in the vertebrate world. Focusing on the CRISP subfamily, we propose that these proteins evolved in three major steps: (1) origination of the CAP/PR/SCP domain in bacteria, (2) addition of a small Hinge domain to produce the two-domain SCP-like proteins found in roundworms and anthropoids, and (3) addition of an Ion Channel Regulatory domain, borrowed from invertebrate peptide toxins, to produce full length, three-domain CRISP proteins, first seen in insects and later to diversify into multiple subtypes in the vertebrate world.

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Allurin: Exploring the Activity of a Frog Sperm Chemoattractant in Mammals

Cited by 2 publications

References 62 publications

Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development

Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development

Tracing the Evolutionary History of the CAP Superfamily of Proteins Using Amino Acid Sequence Homology and Conservation of Splice Sites

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