Asia contributes more than 90% to the world's aquaculture production. Like other farming systems, aquaculture is plagued with disease problems resulting from its intensification and commercialization. This paper describes the various factors, providing specific examples, which have contributed to the current disease problems faced by what is now the fastest growing food-producing sector globally. These include increased globalization of trade and markets; the intensification of fish-farming practices through the movement of broodstock, postlarvae, fry and fingerlings; the introduction of new species for aquaculture development; the expansion of the ornamental fish trade; the enhancement of marine and coastal areas through the stocking of aquatic animals raised in hatcheries; the unanticipated interactions between cultured and wild populations of aquatic animals; poor or lack of effective biosecurity measures; slow awareness on emerging diseases; the misunderstanding and misuse of specific pathogen free (SPF) stocks; climate change; other human-mediated movements of aquaculture commodities. Data on the socio-economic impacts of aquatic animal diseases are also presented, including estimates of losses in production, direct and indirect income and employment, market access or share of investment, and consumer confidence; food availability; industry failures. Examples of costs of investment in aquatic animal health-related activities, including national strategies, research, surveillance, control and other health management programmes are also provided. Finally, the strategies currently being implemented in the Asian region to deal with transboundary diseases affecting the aquaculture sector are highlighted. These include compliance with international codes, and development and implementation of regional guidelines and national aquatic animal health strategies; new diagnostic and therapeutic techniques and new information technology; new biosecurity measures including risk analysis, epidemiology, surveillance, reporting and planning for emergency response to epizootics; targeted research; institutional strengthening and manpower development (education, training and extension research and diagnostic services).

Abstract. Activation of various receptors by extracellular ligands induces an influx of Ca 2 § through the plasma membrane, but its molecular mechanism remains elusive and seems variable in different cell types. In the present study, we utilized mAbs generated against the cerebellar type I inositol 1,4,5-trisphosphate (InsP3) receptor and performed immunocytochemical and immunochemical experiments to examine its localization in several non-neuronal cells. By immunogold electron microscopy of ultrathin frozen sections as well as permeabilized tissue specimens, we found that a mAb to the type I InsP3 receptor (mAb 4Cll) labels the plasma membrane of the endothelium, smooth muscle cell and keratinocyte in vivo. Interestingly, the labeling with the antibody was confined to caveolae, smooth vesicular inpocketings of the plasma membrane. The reactive protein, with an Mr of 240,000 by SDS-PAGE, could be biotinylated with a membraneimpermeable reagent, sulfo-NHS-biotin, in intact cultured endothelial cells, and recovered by streptavidinagarose beads, which result further confirmed its presence on the cell surface. The present findings indicate that a protein structurally homologous to the type I InsP3 receptor is localized in the caveolar structure of the plasma membrane and might be involved in the Ca 2+ influx.

Rabbit antiserum prepared against an ATPase-containing tryptic fragment of dynein by ) specifically inhibited the ATPase activity of dynein 1 and not that of dynein 2. Varying amounts of this antidynein 1 serum were added to demembranated sperm while they were swimming in reactivating solution containing 1 mM ATP. The sperm continued to form regularly propagated flagellar bending waves, but the beat frequency decreased gradually with time, the greater part of the change occurring in the first 15 min. The beat frequency after 1 h was a function of the amount of antiserum used, and could be as low as 1 Hz. The waveforms of the treated sperm resembled those of normal reactivated sperm except that the bend angles of both the principal and reverse bends were larger in the proximal portion of the flagellum. The ATPase activity and corresponding beat frequency of sperm which had been pretreated with varying amounts of antidynein 1 serum for 15 min at 0~ and then diluted were both decreased as a function of the amount of antiserum added, the ATPase activity decreasing more steeply than the frequency. The ATPase activity of homogenized, nonmotile sperm also decreased upon pretreatment with antiserum, but the percentage decrease was less than for motile sperm. For moderate to low concentrations of antiserum, the rates of reaction with motile and with rigor sperm were almost identical. The overall results suggest that antidynein 1 inhibits the functioning of the dynein arms, probably by blocking the ATPase sites of the dynein 1.The general basis of the mechanism of flagellar motility is now well established (3,10,(18)(19)(20). Active sliding movements between doublet tubules of the axoneme are produced by the interaction of the dynein arms with ATP and the neighboring B-tubule, perhaps in a cyclical manner involving a making and breaking of cross-bridges in a manner analogous to that thought to occur in muscle (13). The ATPase protein, dynein, thus plays a key role in movement by mediating the conversion of the chemical energy provided by ATP dephosphorylation into mechanical work.However, the details of the energy transduction process are not yet understood, nor is it known by what mechanism the sliding movements of the tubules are regulated so as to produce the propagated bending waves characteristic of flagella.In an attempt to learn more about the involvement of dynein in the mechanism of movement, we have investigated the effects of an antiserum which is known to inhibit dynein ATPase activity in vitro on the motility, waveform, beat frequency, and ATPase activity of demembranated sea urchin sperm. The antiserum was prepared by

The 'motor' proteins of eukaryotic cells contain specialized domains that hydrolyse ATP to produce force and movement along a cytoskeletal polymer (actin in the case of the myosin family; microtubules in the case of the kinesin family and dyneins). There are motor-protein superfamilies in which each member has a conserved force-generating domain joined to a different 'tail' which conveys specific attachment properties. The minus-end-directed microtubule motors, the dyneins, may also constitute a superfamily of force-generating proteins with distinct attachment domains. Axonemal outer-arm dynein from sea urchin spermatozoa is a multimeric protein consisting of two heavy chains (alpha and beta) with ATPase activity, three intermediate chains and several light chains. Here I report the sequence of cloned complementary DNA encoding the beta heavy chain of a dynein motor molecule. The predicted amino-acid sequence reveals four ATP-binding consensus sequences in the central domain. The dynein beta heavy chain is thought to associate transiently with a microtubule during ATP hydrolysis, but the ATP-dependent microtubule-binding sequence common to the kinesin superfamily is not found in the dynein beta heavy chain. These unique features distinguish the dynein beta heavy chain from other motor protein superfamilies and may be characteristic of the dynein superfamily.

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Abstract. Males of the nematode Philometra lateolabracis (Yamaguti, 1935), the type species of the genus Philometra Costa, 1845, were discovered for the first time in gonads of its type host, the Japanese seaperch, Lateolabrax japonicus (Cuvier). Morphological comparisons carried out between the collected male and female P. lateolabracis with the male and female philometrid nematodes previously reported as P. lateolabracis infecting chicken grunt, Parapristipoma trilineatum (Thunberg), and red sea bream, Pagrus major (Temminck et Schlegel), revealed that the latter represent two new species, Philometra isaki sp. n. and Philometra madai sp. n., respectively. Molecular comparison of ITS2 rDNA between P. lateolabracis and P. madai supported the morphological conclusion that the two nematodes obtained from different fish species should be assigned to different species.

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