@article{mccullen_mcquilling_grossfeld_lubischer_clarke_loboa_2010, title={Application of Low-Frequency Alternating Current Electric Fields Via Interdigitated Electrodes: Effects on Cellular Viability, Cytoplasmic Calcium, and Osteogenic Differentiation of Human Adipose-Derived Stem Cells}, volume={16}, ISSN={["1937-3392"]}, url={https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20367249/?tool=EBI}, DOI={10.1089/ten.tec.2009.0751}, abstractNote={Electric stimulation is known to initiate signaling pathways and provides a technique to enhance osteogenic differentiation of stem and/or progenitor cells. There are a variety of in vitro stimulation devices to apply electric fields to such cells. Herein, we describe and highlight the use of interdigitated electrodes to characterize signaling pathways and the effect of electric fields on the proliferation and osteogenic differentiation of human adipose-derived stem cells (hASCs). The advantage of the interdigitated electrode configuration is that cells can be easily imaged during short-term (acute) stimulation, and this identical configuration can be utilized for long-term (chronic) studies. Acute exposure of hASCs to alternating current (AC) sinusoidal electric fields of 1 Hz induced a dose-dependent increase in cytoplasmic calcium in response to electric field magnitude, as observed by fluorescence microscopy. hASCs that were chronically exposed to AC electric field treatment of 1 V/cm (4 h/day for 14 days, cultured in the osteogenic differentiation medium containing dexamethasone, ascorbic acid, and β-glycerol phosphate) displayed a significant increase in mineral deposition relative to unstimulated controls. This is the first study to evaluate the effects of sinusoidal AC electric fields on hASCs and to demonstrate that acute and chronic electric field exposure can significantly increase intracellular calcium signaling and the deposition of accreted calcium under osteogenic stimulation, respectively.}, number={6}, journal={TISSUE ENGINEERING PART C-METHODS}, author={McCullen, Seth D. and McQuilling, John P. and Grossfeld, Robert M. and Lubischer, Jane L. and Clarke, Laura I. and Loboa, Elizabeth G.}, year={2010}, month={Dec}, pages={1377–1386} }
 @article{malomouzh_nikolsky_lieberman_sherman_lubischer_grossfeld_urazaev_2005, title={Effect of N-acetylaspartylglutamate (NAAG) on non-quantal and spontaneous quantal release of acetylcholine at the neuromuscular synapse of rat}, volume={94}, ISSN={["1471-4159"]}, url={https://doi.org/10.1111/j.1471-4159.2005.03194.x}, DOI={10.1111/j.1471-4159.2005.03194.x}, abstractNote={Abstract}, number={1}, journal={JOURNAL OF NEUROCHEMISTRY}, author={Malomouzh, AI and Nikolsky, EE and Lieberman, EM and Sherman, JA and Lubischer, JL and Grossfeld, RM and Urazaev, AK}, year={2005}, month={Jul}, pages={257–267} }
 @article{urazaev_grossfeld_lieberman_2005, title={Regulation of glutamate carboxypeptidase II hydrolysis of N-acetylaspartylglutamate (NAAG) in crayfish nervous tissue is mediated by glial glutamate and acetylcholine receptors}, volume={93}, ISSN={["1471-4159"]}, DOI={10.1111/j.1471-4159.2005.03041.x}, abstractNote={Abstract}, number={3}, journal={JOURNAL OF NEUROCHEMISTRY}, author={Urazaev, AK and Grossfeld, RM and Lieberman, EM}, year={2005}, month={May}, pages={605–610} }
 @article{buttram_engler_grossfield_urazaev_lieberman_2002, title={Glutamine uptake and metabolism to N-acetylaspartylglutamate (NAAG) by crayfish axons and glia}, volume={133}, ISSN={["1096-4959"]}, DOI={10.1016/S1096-4959(02)00124-0}, abstractNote={We have proposed that N-acetylaspartylglutamate (NAAG) or its hydrolytic product glutamate, is a chemical signaling agent between axons and periaxonal glia at non-synaptic sites in crayfish nerves, and that glutamine is a probable precursor for replenishing the releasable pool of NAAG. We report here, that crayfish central nerve fibers synthesize NAAG from exogenous glutamine. Cellular accumulation of radiolabel during in vitro incubation of desheathed cephalothoracic nerve bundles with [3H]glutamine was 74% Na(+)-independent. The Na(+)-independent transport was temperature-sensitive, linear with time for at least 4 h, saturable between 2.5 and 10 mM L-glutamine, and blocked by neutral amino acids and analogs that inhibit mammalian glutamine transport. Radiolabeled glutamine was taken up and metabolized by both axons and glia to glutamate and NAAG, and a significant fraction of these products effluxed from the cells. Both the metabolism and release of radiolabeled glutamine was influenced by extracellular Na(+). The uptake and conversion of glutamine to glutamate and NAAG by axons provides a possible mechanism for recycling and formation of the axon-to-glia signaling agent(s).}, number={2}, journal={COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY}, author={Buttram, JG and Engler, JA and Grossfield, RM and Urazaev, AK and Lieberman, EM}, year={2002}, month={Oct}, pages={209–220} }
 @article{gafurov_urazaev_grossfeld_lieberman_2002, title={Mechanism of NMDA receptor contribution to axon-to-glia signaling in the crayfish medial giant nerve fiber}, volume={38}, ISSN={["0894-1491"]}, DOI={10.1002/glia.10042}, abstractNote={Abstract}, number={1}, journal={GLIA}, author={Gafurov, BS and Urazaev, AK and Grossfeld, RM and Lieberman, EM}, year={2002}, month={Apr}, pages={80–86} }
 @article{engler_gottesman_harkins_urazaev_lieberman_grossfeld_2002, title={Properties of glutaminase of crayfish CNS: Implications for axon-glia signaling}, volume={114}, ISSN={["0306-4522"]}, DOI={10.1016/S0306-4522(02)00357-3}, abstractNote={Glutaminase of crayfish axons is believed to participate in recycling of axon-glia signaling agent(s). We measured the activity and properties of glutaminase in crude homogenates of crayfish CNS, using ion exchange chromatography to separate radiolabeled product from substrate. Crayfish glutaminase activity is cytoplasmic and/or weakly bound to membranes and dependent on time, tissue protein, and glutamine concentration. It resembles the kidney-type phosphate-activated glutaminase of mammals in being stimulated by inorganic phosphate and alkaline pH and inhibited by the product glutamate and by the glutamine analog 6-diazo-5-oxo-L-norleucine. During incubation of crayfish CNS fibers in Na(+)-free saline containing radiolabeled glutamine, there is an increased formation of radiolabeled glutamate in axoplasm that is temporally associated with an increase in axonal pH from about 7.1 to about 8.0. Both the formation of glutamate and the change in pH are reduced by 6-diazo-5-oxo-L-norleucine. Our results suggest that crayfish glutaminase activity is regulated by cellular changes in pH and glutamate concentration. Such changes could impact availability of the axon-glia signaling agents glutamate and N-acetylaspartylglutamate.}, number={3}, journal={NEUROSCIENCE}, author={Engler, JA and Gottesman, JM and Harkins, JC and Urazaev, AK and Lieberman, EM and Grossfeld, RM}, year={2002}, pages={699–705} }
 @article{urazaev_buttram_deen_gafurov_slusher_grossfeld_lieberman_2001, title={Mechanisms for clearance of released N-acetylaspartylglutamate in crayfish nerve fibers: Implications for axon-glia signaling}, volume={107}, ISSN={["0306-4522"]}, DOI={10.1016/S0306-4522(01)00393-1}, abstractNote={Crayfish nerve fibers incubated with radiolabeled glutamate or glutamine accumulate these substrates and synthesize radioactive N-acetylaspartylglutamate (NAAG). Upon stimulation of the medial giant nerve fiber, NAAG is the primary radioactive metabolite released. Since NAAG activates a glial hyperpolarization comparable to that initiated by glutamate or axonal stimulation through the same receptor, we have proposed that it is the likely mediator of interactions between the medial giant axon and its periaxonal glia. This manuscript reports investigations of possible mechanisms for termination of NAAG-signaling activity. N-acetylaspartyl-[(3)H]glutamate was not accumulated from the bath saline by unstimulated crayfish giant axons or their associated glia during a 30-min incubation. Stimulation of the central nerve cord at 50 Hz during the last minute of the incubation dramatically increased the levels of radiolabeled glutamate, NAAG, and glutamine in the medial giant axon and its associated glia. These results indicate that stimulation-sensitive peptide hydrolysis and metabolic recycling of the radiolabeled glutamate occurred. There was a beta-NAAG-, quisqualate- and 2-(phosphonomethyl)-pentanedioic acid-inhibitable glutamate carboxypeptidase II activity in the membrane fraction of central nerve fibers, but not in axonal or glial cytoplasmic fractions. Inactivation of this enzyme by 2-(phosphonomethyl)-pentanedioic acid or inhibition of N-methyl-D-aspartate (NMDA) receptors by MK801 reduced the glial hyperpolarization activated by high-frequency stimulation. These results indicate that axon-to-glia signaling is terminated by NAAG hydrolysis and that the glutamate formed contributes to the glial electrical response in part via activation of NMDA receptors. Both NAAG release and an increase in glutamate carboxypeptidase II activity appear to be induced by nerve stimulation.}, number={4}, journal={NEUROSCIENCE}, author={Urazaev, AK and Buttram, JG and Deen, JP and Gafurov, BS and Slusher, BS and Grossfeld, RM and Lieberman, EM}, year={2001}, pages={697–703} }
 @article{gafurov_urazaev_grossfeld_lieberman_2001, title={N-acetylaspartylglutamate (NAAG) is the probable mediator of axon-to-glia signaling in the crayfish medial giant nerve fiber}, volume={106}, ISSN={["1873-7544"]}, DOI={10.1016/S0306-4522(01)00271-8}, abstractNote={Glial cell hyperpolarization previously has been reported to be induced by high frequency stimulation or glutamate. We now report that it also is produced by the glutamate-containing dipeptide N-acetylaspartylglutamate (NAAG), by its non-hydrolyzable analog β-NAAG, and by NAAG in the presence of 2-(phosphonomethyl)-pentanedioic acid (2-PMPA), a potent inhibitor of the NAAG degradative enzyme glutamate carboxypeptidase II. The results indicate that NAAG mimics the effect of nerve fiber stimulation on the glia. Although glutamate has a similar effect, the other presumed product of NAAG hydrolysis, N-acetylaspartate, is without effect on glial cell membrane potential, as is aspartylglutamate (in the presence of 2-PMPA). The hyperpolarization induced by stimulation, glutamate, NAAG, β-NAAG, or NAAG plus 2-PMPA is completely blocked by the Group II metabotropic glutamate receptor antagonist (S)-α-ethylglutamate but is not altered by antagonists of Group I or III metabotropic glutamate receptors. The N-methyl-D-aspartate receptor antagonist MK801 reduces but does not eliminate the hyperpolarization generated by glutamate, NAAG or stimulation. These results, in combination with those of the preceding paper, are consistent with the premise that NAAG could be the primary axon-to-glia signaling agent. When the unstimulated nerve fiber is treated with cysteate, a glutamate reuptake blocker, there is a small hyperpolarization of the glial cell that can be substantially reduced by pretreatment with 2-PMPA before addition of cysteate. A similar effect of cysteate is seen during a 50 Hz/5 s stimulation. From these results we suggest that glutamate derived from NAAG hydrolysis appears in the periaxonal space under the conditions of these experiments and may contribute to the glial hyperpolarization.}, number={1}, journal={NEUROSCIENCE}, author={Gafurov, B and Urazaev, AK and Grossfeld, RM and Lieberman, EM}, year={2001}, pages={227–235} }
 @article{urazaev_grossfeld_fletcher_speno_gafurov_buttram_lieberman_2001, title={Synthesis and release of N-acetylaspartylglutamate (NAAG) by crayfish nerve fibers: Implications for axon-glia signaling}, volume={106}, ISSN={["0306-4522"]}, DOI={10.1016/S0306-4522(01)00270-6}, abstractNote={Early physiological and pharmacological studies of crayfish and squid giant nerve fibers suggested that glutamate released from the axon during action potential generation initiates metabolic and electrical responses of periaxonal glia. However, more recent investigations in our laboratories suggest that N-acetylaspartylglutamate (NAAG) may be the released agent active at the glial cell membrane. The investigation described in this paper focused on NAAG metabolism and release, and its contribution to the appearance of glutamate extracellularly. Axoplasm and periaxonal glial cell cytoplasm collected from medial giant nerve fibers (MGNFs) incubated with radiolabeled L-glutamate contained radiolabeled glutamate, glutamine, NAAG, aspartate, and GABA. Total radiolabel release was not altered by electrical stimulation of nerve cord loaded with [(14)C]glutamate by bath application or loaded with [(14)C]glutamate, [(3)H]-D-aspartate or [(3)H]NAAG by axonal injection. However, when radiolabeled glutamate was used for bath loading, radiolabel distribution among glutamate and its metabolic products in the superfusate was changed by stimulation. NAAG was the largest fraction, accounting for approximately 50% of the total recovered radiolabel in control conditions. The stimulated increase in radioactive NAAG in the superfusate coincided with its virtual clearance from the medial giant axon (MGA). A small, stimulation-induced increase in radiolabeled glutamate in the superfusate was detected only when a glutamate uptake inhibitor was present. The increase in [(3)H]glutamate in the superfusion solution of nerve incubated with [(3)H]NAAG was reduced when beta-NAAG, a competitive glutamate carboxypeptidase II (GCP II) inhibitor, was present.Overall, these results suggest that glutamate is metabolized to NAAG in the giant axon and its periaxonal glia and that, upon stimulation, NAAG is released from the axon and converted in part to glutamate by GCP II. A quisqualate- and beta-NAAG-sensitive GCP II activity was detected in nerve cord homogenates. These results, together with those in the accompanying paper demonstrating that NAAG can activate a glial electrophysiological response comparable to that initiated by glutamate, implicate NAAG as a probable mediator of interactions between the MGA and its periaxonal glia.}, number={1}, journal={NEUROSCIENCE}, author={Urazaev, AK and Grossfeld, RM and Fletcher, PL and Speno, H and Gafurov, BS and Buttram, JG and Lieberman, EM}, year={2001}, pages={237–247} }
 @article{rathinam_chen_grossfeld_2000, title={Cloning and sequence analysis of a cDNA for an inducible 70 kDa heat shock protein (Hsp70) of the American oyster (Crassostrea virginica)}, volume={11}, DOI={10.3109/10425170009033240}, abstractNote={We have been investigating 70 kDa heat shock proteins (Hsp70s) as potential molecular markers for improved breeding and stress management to revitalize stocks of the American oyster, C. virginica. From a C. virginica visceral mass library, a 2.2 kb full-length cDNA was isolated that included a 634 amino acid open reading frame possessing approximately 80% sequence identity with inducible and constitutive Hsp70s of a broad array of animal species. Northern blotting indicated that the cloned cDNA preferentially recognized an mRNA of about 2 kb that was virtually absent from visceral mass under basal conditions but greatly increased after in vivo heat shock of American and Pacific oysters, suggesting that the cDNA codes for an inducible Hsp70.}, number={3-4}, journal={DNA Sequence}, author={Rathinam, A. V. and Chen, T. T. and Grossfeld, R. M.}, year={2000}, pages={261–264} }
 @article{kane_buttram_urazaev_lieberman_grossfeld_2000, title={Uptake and metabolism of glutamate at non-synaptic regions of crayfish central nerve fibers: Implications for axon-glia signaling}, volume={97}, ISSN={["0306-4522"]}, DOI={10.1016/S0306-4522(00)00054-3}, abstractNote={In crayfish and squid giant nerve fibers, glutamate appears to be an axon-glia signaling agent. We have investigated glutamate transport and metabolism by crayfish central nerve fibers in order to identify possible mechanisms by which glutamate could subserve this non-synaptic signaling function. Accumulation of radiolabeled L-glutamate by desheathed cephalothoracic nerve bundles was temperature and Na(+) dependent, linear with time for at least 8h and saturable at about 0.5-1mM L-glutamate. Most accumulated radiotracer was associated with the periaxonal glial sheath and remained as glutamate. Compounds known to block glutamate transport in invertebrate peripheral nerves or mammalian brain slices or cell cultures were also effective on crayfish central nerve fibers. Tissue radiotracer levels were only 3% of control levels when 1mM p-chloromercuriphenylsulfonate was present, and 13%, 20%, 26%, 38% and 42% of control levels, respectively, when L-cysteate, L-cysteine sulfinate, L-aspartate, D-aspartate or DL-threo-beta-hydroxyaspartate was present. L-Glutamine, GABA, N-methyl-DL-aspartate, alpha-aminoadipate and D-glutamate were without inhibitory effect on tissue tracer accumulation. Radiolabeled D-aspartate was an equivalent non-metabolized substitute for radiolabeled L-glutamate. D-Aspartate, p-chloromercuriphenylsulfonate and GABA had comparable effects on isolated medial giant nerve fibers.These studies indicate that L-glutamate is taken up primarily by the periaxonal glia of crayfish central nerve fibers by a low-affinity, saturable, Na(+)-dependent transport system and is retained by the fibers primarily in that form. Our results suggest that the glia are not only the target of the glutamate signal released from non-synaptic regions of the crayfish medial giant axon during high-frequency stimulation, but that they are also the primary site of its inactivation.}, number={3}, journal={NEUROSCIENCE}, author={Kane, LS and Buttram, JG and Urazaev, AK and Lieberman, EM and Grossfeld, RM}, year={2000}, pages={601–609} }
 @article{sheller_smyers_grossfeld_ballinger_bittner_1998, title={Heat-shock proteins in axoplasm: High constitutive levels and transfer of inducible isoforms from glia}, volume={396}, ISSN={["1096-9861"]}, DOI={10.1002/(SICI)1096-9861(19980622)396:1<1::AID-CNE1>3.0.CO;2-4}, abstractNote={To characterize heat‐shock proteins (HSPs) of the 70‐kDa family in the crayfish medial giant axon (MGA), we analyzed axoplasmic proteins separately from proteins of the glial sheath. Several different molecular weight isoforms of constitutive HSP 70s that were detected on immunoblots were approximately 1–3% of the total protein in the axoplasm of MGAs. To investigate inducible HSPs, MGAs were heat shocked in vitro or in vivo, then the axon was bathed in radiolabeled amino acid for 4 hours. After either heat‐shock treatment, protein synthesis in the glial sheath was decreased compared with that of control axons, and newly synthesized proteins of 72 kDa, 84 kDa, and 87 kDa appeared in both the axoplasm and the sheath. Because these radiolabeled proteins were present in MGAs only after heat‐shock treatments, we interpreted the newly synthesized proteins of 72 kDa, 84 kDa, and 87 kDa to be inducible HSPs. Furthermore, the 72‐kDa radiolabeled band in heat‐shocked axoplasm and glial sheath samples comigrated with a band possessing HSP 70 immunoreactivity. The amount of heat‐induced proteins in axoplasm samples was greater after a 2‐hour heat shock than after a 1‐hour heat shock. These data indicate that MGA axoplasm contains relatively high levels of constitutive HSP 70s and that, after heat shock, MGA axoplasm obtains inducible HSPs of 72 kDa, 84 kDa, and 87 kDa from the glial sheath. These constitutive and inducible HSPs may help MGAs maintain essential structures and functions following acute heat shock. J. Comp. Neurol. 396:1–11, 1998. © 1998 Wiley‐Liss, Inc.}, number={1}, journal={JOURNAL OF COMPARATIVE NEUROLOGY}, author={Sheller, RA and Smyers, ME and Grossfeld, RM and Ballinger, ML and Bittner, GD}, year={1998}, month={Jun}, pages={1–11} }
 @article{tirard_grossfeld_levine_kennedy-stoskopf_1997, title={Effect of Osmotic Shock on Protein Synthesis of Oyster Hemocytes In Vitro}, volume={116}, ISSN={0300-9629}, url={http://dx.doi.org/10.1016/S0300-9629(96)00115-6}, DOI={10.1016/s0300-9629(96)00115-6}, abstractNote={Because marine bivalves are osmoconformers, their cells may be exposed to widely fluctuating osmolality in some habitats. In vitro studies were conducted to evaluate the effect of changes in salinity on protein synthesis of oyster hemocytes. Increasing salinity from a control value of 20–25 ppt to 32–98 ppt decreased the rate of incorporation of amino acid into protein, but did not qualitatively alter the pattern of protein synthesis. On the other hand, decreasing salinity to 3.5–4 ppt not only decreased the rate of protein synthesis, but also altered the types of protein produced. At least a third of the cells remained viable at low salinity and resumed the control pattern of protein synthesis within hours after return to the normal medium. The response to hypoosmotic shock was different from the response to a hyperthermic shock, each stressor inducing expression of a characteristic set of proteins. Preferential synthesis of these proteins may represent an adaptation to preserve or restore oyster cell functions under adverse conditions.}, number={1}, journal={Comparative Biochemistry and Physiology Part A: Physiology}, publisher={Elsevier BV}, author={Tirard, C.T and Grossfeld, R.M and Levine, J.F and Kennedy-Stoskopf, S}, year={1997}, month={Jan}, pages={43–49} }
 @article{siesko_fleming_grossfeld_1997, title={Stress protein synthesis and peroxidase activity in a submersed aquatic macrophyte exposed to cadmium}, volume={16}, ISSN={["1552-8618"]}, DOI={10.1897/1551-5028(1997)016<1755:SPSAPA>2.3.CO;2}, abstractNote={Sago pondweed (Potamogeton pectinatus L.) was exposed to CdCl, to evaluate peroxidase (POD) activity and stress protein (SP) synthesis as potential biomarkers of contaminant stress in an aquatic plant. Peroxidase activity did not increase in sago pondweed incubated for 24 h in a liquid culture medium containing 0.5, 0.75, or 1 mM CdCl,. By contrast, at each of these CdCl, concentrations, SPs of 162, 142, 122, 82, and 61 kDa were preferentially synthesized, and synthesis of a 66-kDa protein was reduced relative to controls. Peroxidase activity also did not change in sago pondweed rooted for 21 d in agar containing 1 mM CdCl2, despite the lower growth rate, lower protein content, and brown discoloration of the plants. Only when the plants were grown 7 or 21 d on agar containing 10 mM CdCl, were the growth retardation and phenotypic deterioration accompanied by significantly increased POD activity. In contrast, plants rooted for 7 d in agar containing 1 mM CdCl, were not significantly discolored or retarded in growth, yet they preferentially synthesized SPs of 122, 82, and 50 kDa and synthesized proteins of 59 and 52 kDa at reduced rates relative to controls. Similar changes in protein synthesis were accompanied by signs of depressed growth after 21 d of incubation with 1 mM CdCl, and with 7 or 21 d of exposure to 10 mM CdCl,. These data indicate that changes in SP synthesis may precede detectable alterations in growth of aquatic plants and, therefore, may be a potentially useful early biomarker of contaminant stress. However, further studies will be required to determine whether the SP response is measurable during exposure to environmentally relevant contaminant levels.}, number={8}, journal={ENVIRONMENTAL TOXICOLOGY AND CHEMISTRY}, author={Siesko, MM and Fleming, WJ and Grossfeld, RM}, year={1997}, month={Aug}, pages={1755–1760} }
 @article{tirard_grossfeld_levine_kennedy-stoskopf_1995, title={Effect of hyperthermia in vitro on stress protein synthesisand accumulation in oyster haemocytes}, volume={5}, ISSN={1050-4648}, url={http://dx.doi.org/10.1016/S1050-4648(05)80003-8}, DOI={10.1016/S1050-4648(05)80003-8}, abstractNote={Haemocytes comprise a major component of the non-specific defence mechanismsin marine bivalves. Induction of stress protein (SP) synthesis and accumulation of SPs was studied in vitro to define the metabolic response of oyster (C. virginica) haemocytes to acute temperature changes. An acute cold shock to near freezing had no significant effect on protein synthesis. However, a comparable heat shock of 20–28° C above the acclimation temperature of 20° C provoked a robust increase in synthesis of several SPs, especially those of about 70 (SP70), 37, 34 and 32 kDa. This response persisted for at least 24 h, during which time both isoforms of SP70-like immunoreactivity accumulated. Concomitantly, there was a decrease in the synthesis, but not in the level, of an actin-like protein of about 45 kDa. The extent of SP synthesis induction also was directly dependent on the duration of the preceding hyperthermia. Extending the duration of heat shock necessitated a longer recovery period, during which time amino acid incorporation returned towards or beyond the initial control values and cell viability was retained. After a severe heat shock at 46° C for 1 h, the predominant protein made for several days was SP70, which is known to be essential for stress tolerance in other biological systems. The results suggest that oyster haemocytes are remarkably resilient, and that SPs may contribute to their ability to resist or repair heat-evoked damage. This molecular adaptability could permit them to maintain immune surveillance during or immediately following serious threats to survival of these sessile ectotherms.}, number={1}, journal={Fish & Shellfish Immunology}, publisher={Elsevier BV}, author={Tirard, C.T. and Grossfeld, R.M. and Levine, J.F. and Kennedy-Stoskopf, S.}, year={1995}, month={Jan}, pages={9–25} }