Invertebrates storage

Cyprid major protein is a larval storage protein necessary for successful metamorphosis. " Production of cyprid major protein was increased in the barnacle Balanus amphitrite following exposure to both nonylphenol and estradiol, suggesting that it may be a potential biomarker of estrogen exposure in invertebrates such as barnacles. " "... 

Burges, H.D. and Hurst, J.A. 1977. Ecology of Bacillus thuringiensis in storage moths. J. Invertebr. Pathol. 30, 131-139. 

Octopamine (4.41), which carries a p-hydroxyl group, is taken up even more readily into storage vesicles and is, in turn, released when the neuron fires. As an adrenergic agonist, octopamine is, however, only about one-tenth as active as NE therefore, it acts as a very weak neurotransmitter. Compounds such as this behave like neurotransmitters of low potency, and are called false transmitters. On the other hand, octopamine may be a true transmitter in some invertebrates, with receptors that cannot be occupied either by other catecholamines or by serotonin. 

Copper Essential to all organisms constituent of redox enzymes and hemocyanin." Very toxic to most plants highly toxic to Invertebrates, moderately so to mammals. Pollution from industrial smoke and possibly from agricultural use. Wilson s disease, genetic recessive, results in toxic increase in copper storage. 

Respiratory pigments similar to the vertebrate haemoglobins have also been identified in many invertebrates. These vary from small proteins with two Fe-porphyrin units to large molecules containing up to 190 Fe-porphyrin units. Myoglobin, the 02 storage protein in muscle tissue, is also a small iron-protoporphyrin protein. The crystal structures of this and a number of other porphyrin proteins are now known (Chapter 20.2, Table 11). 

This iron storage protein is widely distributed in many mammalian cells, and also in invertebrates, plants, fungi and a number of bacteria, where it is associated with a fe-type cytochrome. There have been considerable advances recently in the understanding of its structure and physiological function.1093 1098... 

The action of tyramine on nerve receptors is mainly indirect by release of norepinephrine and dopamine from neuronal storage sites (363, 384). Tyramine and its /3-oxidized counterpart octopamine have been referred to as false neurotransmitters because these compounds can be taken up, stored, and released from nerve endings in a way similar to those of the principal neurotransmitters norepinephrine and dopamine (385). Octopamine was first discovered in salivary glands of octopods (386). The compound is widely distributed in the animal kingdom and is present in high amounts in the nervous system of several species of invertebrates such as molluscs and arthropods, where it acts as a specific transmitter substance (387). Octopamine may also play a role in the regulation of adrenergic neurotransmission in mammals (387). Administration of octopamine to intact animals produces a transient rise in blood pressure (388). 

In museum collections, most invertebrates will be encountered as natural history specimens, which are divided into dry and wet-preserved. Those animals having a shell or tough exoskeleton, like starfish, shelled mollusks, and lobsters, may be dried after death. The tissue may be removed, but it is often left inside the shell or carapace to shrivel and dry. Wet-preserved specimens are usually fixed in a solution of formalin or some other preservative to prevent the tissues from deteriorating quickly after death. After a brief period, the specimen is usually removed from the toxic fixing solution, rinsed, and placed in a storage solution of 70% ethanol (alcohol) mixed with water. 

In order to ovecome these defects, much research has been done in an attempt to clarify the mechanisms and causes of these changes during frozen storage of meats. Such studies have included a wide variety of animals including beef animals, hogs, poultry, fish, shellfish and other invertebrate aquatic animals. The number of papers published in this area amounts to several hundred. 

Hemerythrin (Hr) is an 02-carrying protein found in a few phyla of marine invertebrates where it is thought to function as an O2 storage reservoir. The diiron active site reversibly binds the O2. Several reviews that discuss various aspects of Hr structure and function are available.Hr most often occurs as an octamer of essentially identical 02-binding subunits, although tetrameric, trimeric, and dimeric Hrs are also known. A monomeric counterpart, myoHr, is confined to muscle tissues of the same marine invertebrates. The structure of the myoHr subunit and active site are both very similar to those of Hr. The following discussion, therefore, applies, with very few exceptions, equally well to both Hr and myoHr. 

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