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Epel, D, Cole B, Hamdoun A, Thurber RV.  2006.  The sea urchin embryo as a model for studying efflux transporters: Roles and energy cost. Marine Environmental Research. 62:S1-S4.   10.1016/j.marenvres.2006.04.062   AbstractWebsite

We describe the use of the sea urchin as a model for studying efflux transporters and estimating energy cost for the cytotoxin protective system provided by these transporters. The unfertilized egg has low transport activity, which increases to a new steady state shortly after fertilization. Activity results from p-glycoprotein (p-gp) and MRP type transporters which protect the embryo from cytotoxic drugs that can disrupt cell division or induce apoptosis. The energy cost is estimated from a novel use of calcein-AM as a substrate; keeping 0.25 mu M substrate levels out of the cell utilizes only 0.023% of steady state respiration. (c) 2006 Elsevier Ltd. All rights reserved.

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Hamdoun, AM, Griffin FJ, Cherr GN.  2002.  Tolerance to biodegraded crude oil in marine invertebrate embryos and larvae is associated with expression of a multixenobiotic resistance transporter. Aquatic Toxicology. 61:127-140.   10.1016/s0166-445x(02)00050-4   AbstractWebsite

The toxicity of water-soluble fractions of biodegraded crude oil (BWSF) to embryos and larvae of two marine invertebrates, the white sea urchin (Lytechinus anamesus) and the fat innkeeper (Urechis caupo), was studied. Santa Barbara Channel crude oil was artificially weathered and subjected to biodegradation using a mixed microbe culture obtained from natural oil seep sites. The degradation culture inoculated with seep sediment microbes accumulated 43.7 mug/l water-soluble hydrocarbons. In contrast water-soluble fractions from the non-degraded cultures (NWSF) only accumulated 3.05 mug/l. BWSF proved deleterious to Lytechinus embryo development at low concentrations (EC50 = 0.33 mg/l) but was essentially non-toxic to Urechis embryos/larvae up to 3.0 mg/l. An established mechanism for handling of a wide array of xenobiotics in Urechis embryos is the multixenobiotoic resistance transporter multixenobiotic response (MXR, also known as multidrug resistance, MDR). This mechanism is primarily mediated by ATP-dependent, efflux pumps that extrude a wide array of xenobiotic compounds. In this study, we show that Lytechinus larvae do not appear to express MXR efflux. protein nor MXR mediated dye efflux capacity. In contrast, BWSF acts as a competitive inhibitor of MXR transport-mediated dye efflux in Urechis larvae. These results suggest that MXR may be an important mechanism for extrusion of the by-products of crude oil degradation by microbes, and that the level of its expression may determine the susceptibility of organisms to degraded oil hydrocarbons. (C) 2002 Elsevier Science B.V. All rights reserved.

Gokirmak, T, Shipp LE, Campanale JP, Nicklisch SCT, Hamdoun A.  2014.  Transport in technicolor: Mapping ATP-binding cassette transporters in sea urchin embryos. Molecular Reproduction and Development. 81:778-793.   10.1002/mrd.22357   AbstractWebsite

One quarter of eukaryotic genes encode membrane proteins. These include nearly 1,000 transporters that translocate nutrients, signaling molecules, and xenobiotics across membranes. While it is well appreciated that membrane transport is critical for development, the specific roles of many transporters have remained cryptic, in part because of their abundance and the diversity of their substrates. Multidrug resistance ATP-binding cassette (ABC) efflux transporters are one example of cryptic membrane proteins. Although most organisms utilize these ABC transporters during embryonic development, many of these transporters have broad substrate specificity, and their developmental functions remain incompletely understood. Here, we review advances in our understanding of ABC transporters in sea urchin embryos, and methods developed to spatially and temporally map these proteins. These studies reveal that multifunctional transporters are required for signaling, homeostasis, and protection of the embryo, and shed light on how they are integrated into ancestral developmental pathways recapitulated in disease. Mol. Reprod. Dev. 81: 778-793, 2014. (c) 2014 Wiley Periodicals, Inc.

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Barron, ME, Thies AB, Espinoza JA, Barott KL, Hamdoun A, Tresguerres M.  2018.  A vesicular Na+/Ca2+ exchanger in coral calcifying cells. PLOS ONE. 13: Public Library of Science   10.1371/journal.pone.0205367   Abstract

The calcium carbonate skeletons of corals provide the underlying structure of coral reefs; however, the cellular mechanisms responsible for coral calcification remain poorly understood. In osteoblasts from vertebrate animals, a Na+/Ca2+ exchanger (NCX) present in the plasma membrane transports Ca2+ to the site of bone formation. The aims of this study were to establish whether NCX exists in corals and its localization within coral cells, which are essential first steps to investigate its potential involvement in calcification. Data mining identified genes encoding for NCX proteins in multiple coral species, a subset of which were more closely related to NCXs from vertebrates (NCXA). We cloned NCXA from Acropora yongei (AyNCXA), which, unexpectedly, contained a peptide signal that targets proteins to vesicles from the secretory pathway. AyNCXA subcellular localization was confirmed by heterologous expression of fluorescently tagged AyNCXA protein in sea urchin embryos, which localized together with known markers of intracellular vesicles. Finally, immunolabeling of coral tissues with specific antibodies revealed AyNCXA was present throughout coral tissue. AyNCXA was especially abundant in calcifying cells, where it exhibited a subcellular localization pattern consistent with intracellular vesicles. Altogether, our results demonstrate AyNCXA is present in vesicles in coral calcifying cells, where potential functions include intracellular Ca2+ homeostasis and Ca2+ transport to the growing skeleton as part of an intracellular calcification mechanism.