The echinoderm lytic system

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  • This article was downloaded by: [Fondren Library, Rice University ]On: 17 November 2014, At: 08:15Publisher: Taylor & FrancisInforma Ltd Registered in England and Wales Registered Number: 1072954 Registered office: Mortimer House,37-41 Mortimer Street, London W1T 3JH, UK

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    The echinoderm lytic systemCalogero Canicatt aa Dipartimento di Biologia , Universit di Lecce , Via Prov.le LecceMonteroni, Lecce, I73100,ItalyPublished online: 28 Jan 2009.

    To cite this article: Calogero Canicatt (1992) The echinoderm lytic system, Bolletino di zoologia, 59:2, 159-166, DOI:10.1080/11250009209386664

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  • Boll. Zool. 59: 159-166(1992)

    The echinoderm lytic system

    CALOGERO CANICATTDipartimento di Biologia, Universit di Lecce,Via Prov.le Lecce-Monteroni, 1-73100 Lecce (Italy)

    INTRODUCTION

    Lysins are biologically active substances characterizedby their lytic properties against foreign targets. In inver-tebrates, these molecules are important factors involvedin the humoral defence mechanisms (Canicatt, 1990a).

    Lytic activity has been evidenced in several groupsboth of acoelomate (Bretting & Renwrantz, 1973; Kamiyaet al., 1985; Norton et al., 1989) and coelomate(Weinheimer et al., 1969, 1970; Day et al., 1972; Bretting& Renwrantz, 1973; Parrinello et al., 1979; Anderson,1980; Parrinello & Rindone, 1981; Cenini, 1983; Tuan &Yoshino, 1984; Tuckova et al., 1986; Canicatt, 1987a;Leippe & Renwrantz, 1988) invertebrates. It depends onmolecules of proteic nature which show a remarkabledegree of resemblance to cytolytic peptides (Bernheimer& Rudy, 1986; Bernheimer, 1990). Generally, the lytic ac-tivity of the invertebrate body fluids is evidenced byusing vertebrate erythrocytes as experimental target. Theresulting lytic effect is therefore referred to as hemolytic.However, other kinds of cells, such as fibroblasts andblood platelets, are lysed by lysins. Bacteria are alsouseful targets to demonstrate killing properties of thelytic system (Roch, 1979; Hltmark et al., 1980; Roch etal., 1981; Anderson & Chain, 1982; Valembois et al.,1986).

    The biological properties of invertebrate lyticmolecules appear to depend upon the formation of trans-membrane channels that are formed by aggregation ofmolecules in the membrane bilayer (Bernheimer & Rudy,1986; Roch et al., 1989; Canicatt, 1990a). These obser-vations suggest a resemblance with vertebrate pore-forming proteins (Canicatt, 1990a).

    Much attention has been paid to echinodermhemolysins, especially because of their phylogeneticposition. The aim of the present review is to summarizecurrent knowledge on the lytic system of this highlydiversified group.

    NATURALLY OCCURRING HEMOLYSIN

    ABSTRACT

    Echinoderms possess factors responsible for lysis of target cells.Information on their nature, occurrence, physical and chemicalproperties and biological role are summarized. Further results onbinding properties to surface components are discussed, including ahypothetical explanation both for hemolysin-target interaction andregulation.

    KEY WORDS: Echinoderms - Hemolysin - Opsonin.

    ACKNOWLEDGEMENTS

    I am grateful to a number of former and present colleagues whocollaborated in the study of the echinoderm lytic system. They in-clude: V. Arizza, D. Ciulla, E. L. Cooper, G. D'Ancona, E. Farina-Lipari, A. Miglietta, N. Parrinello, D. Rindone, J. Tschopp.

    In echinoderms, the coelomic fluid contained in thewide coelomic cavity possesses naturally occurring lyticproperties (Ryoyama, 1973; Parrinello et al., 1979; Ber-theussen, 1983; Canicatt, 1987a, 1989; Leonard et al.,1990) against suitable target cells. The activity dependson molecules of proteinaceous nature unrelated tosaponins (Fig. 1), biologically active, water-soluble mix-ture of at least six glycosides (Nigrelli et al., 1967).

    Vertebrate erythrocytes were the main targets usedand, as demonstrated in different species, the specificityof the lytic action was wide, being directed againstalmost all the erythrocyte types tested including mam-malians, reptiles, amphibians and fishes (Ryoyama, 1973;Parrinello et al., 1979; Canicatti, 1987a, 1989). However,in Strongylocentrotus droebachiensis a restrictedspecificity was observed. In this echinoid, in fact, of all

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  • 160 C. CANICATT

    CH.

    Fig. 1 - Chemical structure of the echinoderm saponins. A: 22-25epoxyholothurinogenine; B: holothurogenine; C: 12-methoxy-7-8-diidro-22-25-epoxyholothurogenine; D: hoioxine.

    the erythrocyte types assayed (human, mouse, rabbit andsheep), only rabbit red cells were lysed. Generally thehemolytic titers consistently vary from one erythrocytetype to another. As shown in Figure 2, this different reac:

    tivity seems not to depend on the systematic position ofthe different red cells, nor on the structural differencesbetween erythrocytes (presence or absence of nucleus).Rabbit and human cells were the most sensitive targets,whereas sheep erythrocytes were the least reactive. In-dividual variations of the hemolytic activity could bemeasured in echinoid, asteroid and holothuroidcoelomic fluids. As demonstrated by Canicatt (1989),when a total number of 78 Marthasterias glacialis(Asteroidea) coelomic fluids were tested individually,only 38 were reactive towards rabbit erythrocytes. Thereactivity does not depend on sex, nor on age, nor'on theprotein content of the coelomic fluid. It could dependon seasonal parameters (i.e., temperature, photoperiodetc.) or on the biology of the reproductive cycle. At leastfor M. glacialis, the decrease of the number of reactantanimals seems to correspond with the reproductiveperiod: late spring to summer (Tortonese, 1965)-.Biological variability in hemolytic response of thecoelomic fluid was also monitored in another asteroidAsterias forbesi (Leonard et al., 1990). The authorsbelieve that it is a consequence of maintaining theanimals in an artificial environment. This is not true forM. glacialis, nor for P. lividus, since the coelomic fluids;assayed immediately after collection, presented similardegrees of individual variations to those of the specieskept in acquaria.

    In addition to hemolytic activity, the echinodermcoelomic fluid exerts also lytic activity against mam-

    Hemolytlc titer

    frog naJe chtok*n rat mou* g. pVg rabbit ah*p pig hors* human

    t = l A. cralplnaEE3 P. a*pxum EHUD P. Hvldu KS3 M. putch*rrlmu5H3 8. dro*tMK>hl*fZD M. glaolall ESS H. polll

    Fig. 2 - Sensitivity of different erythrocytc species to lysis by echinoderm coelomic fluids.

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  • ECHINODERM HEMOLYSIN 161

    malian malignant cells. As demonstrated in Holothuriapolii (Canicatti, unpublished data), the degree of lysiswas influenced by coelomic fluid dilution. Mousemastocytome P815 was the most sensitive target (degreeof lysis of 100+0.2 %). As sensitive as normal rabbiterythrocytes (87.11.2%) was human leukemia K562 cellline. The least sensitive target was mouse flbrosarcomaWEHJ 164/14 (65.0*1.0%).

    Auto- and allogeneic cells are neither lysed nordamaged. In P. lividus, the incubation of coelomic fluidwith auto- and allogeneic dechorionat'ed eggs did notproduce cytolysis, nor reduction in the ability of the eggsto be fertilized (Canicatti, 1991). These results indicatethat the membrane of self cells probably lackshemolysin binding components. On the other hand, it isalso probable that autologous membranes possessprotective components which do not allow any interac-tion between lysins and membrane.

    RELATIONSHIP BETWEEN PROTEASE ACTIVITYAND HEMOYLTIC ACTIVITY

    Echinoderm coelomic fluid possesses protease activity(Canicatti, 1990b). It depends on thermolabile enzymesinfluenced by

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