Question about deep-sea ceph's

Rapid membrane repair in two transected giant axons
by Krause, Todd Lawrence, Ph.D., The University of Texas at Austin, 1993, 209 pages; AAT 9323456
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Advisor: Bittner, George D.
School: The University of Texas at Austin
School Location: United States -- Texas
Index terms(keywords): Loligo pealei, Sepioteuthis lessoniana, Lumbricus terrestris
Source: DAI-B 54/04, p. 1822, Oct 1993
Source type: DISSERTATION
Subjects: Neurology, Cellular biology, Anatomy & physiology, Animals
Publication Number: AAT 9323456
Document URL: Shibboleth Authentication Request
ProQuest document ID: 747462731

Abstract (Document Summary)

For a nerve cell to survive transection, toxic changes in intracellular concentrations of ions or macromolecules must be prevented by the formation of a barrier (seal) at the site of damage. Despite the importance of sealing to the survival of damaged neurons and other cell types, sealing has not been well characterized and its mechanism is unknown in any cell type.

Using several functional (membrane potential, input resistance, complex input-impedance, and injury current density) and morphological (phase contrast microscopy, video-enhanced differential interference contrast microscopy, light microscopy and electron microscopy) measures, I assessed sealing in two invertebrate giant axons--the giant axon of squid (Loligo pealei and Sepioteuthis lessoniana) and the medial giant axon of earthworm (Lumbricus terrestris). The functional and morphological data together strongly suggest that when transected in standard salines, the squid axon does not seal within 2.5 hr, whereas the earthworm axon seals within 1 hr. Neither axon seals within 2.5 hr when transected in divalent cation free saline. Further, my data do not support the conventional notion that sealing occurs by constriction and fusion of axolemmal membranes at the cut end. Rather, my data indicates that earthworm axon seals by forming a plug of large $(\ge$5 $\mu$m) injury-induced vesicles at the cut axonal end.

I also assessed the ability of naturally occurring mechanisms of seal formation to facilitate the reconnection of lesioned axons by artificial means (i.e. polyethylene glycol). When the natural ability of earthworm axon to seal-off its cut end was controlled by adjusting the ionic concentration of the bath saline, lesioned axons were efficiently reconnected using polyethylene glycol. The extent of axonal reconnection was extensively characterized using morphological (light microscopy, electron microscopy, passive diffusion of intraxonally injected dye across the reconnection site) and functional (membrane potential, action potential and electrotonic potential conduction through the reconnection site) measures.
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Functional characterization of Electrophorus electrocyte sodium channels
by Shenkel, Scott, Ph.D., Yale University, 1992, 147 pages; AAT 9235556
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Advisor: Sigworth, Frederick J.
School: Yale University
School Location: United States -- Connecticut
Index terms(keywords): Electrophorus electricus
Source: DAI-B 53/07, p. 3350, Jan 1993
Source type: DISSERTATION
Subjects: Anatomy & physiology, Animals, Neurology, Biophysics
Publication Number: AAT 9235556
Document URL: Shibboleth Authentication Request
ProQuest document ID: 744439081

Abstract (Document Summary)

The first voltage gated Na channel to be purified biochemically and to be cloned and sequenced is that present in the electrocytes of the electric organ of the electric eel Electrophorus electricus. To complement what is known about its structure my work has focused on the study of the functional properties of the electrocyte Na channel based on electrophysiological measurements of purified, modified reconstituted channels in planar lipid bilayers and unmodified channels in patches of intact electrocyte membrane.

Na channels modified by mild trypsin-treatment and then incorporated into planar lipid bilayers have properties of steady-state voltage-dependence of activation, single-channel conductance, and sensitivity to tetrodotoxin and saxitoxin similar to those of unmodified Na channels in nerve and muscle cell membranes. One exception is the unusually high P$\sb{\rm Na}$/P$\sb{\rm K}$ selectivity ratio of 41, which is two to four times the values previously reported for Na channels in nerve and muscle cells.

My patch-clamp experiments on intact electrocytes have shown that the high P$\sb{\rm Na}$/P$\sb{\rm K}$ observed in the trypsinized channels in bilayers is a real property of the channels in the intact cell membrane. In addition, the trypsinized channels in bilayers and native channels have similar properties of steady-state voltage-dependence of activation and single-channel conductance. Furthermore, the properties of activation, inactivation and single-channel conductance of the electrocyte Na channel are similar to those of Na channels in nerve and muscle cell membranes. A surprising finding is the large variation in P$\sb{\rm Na}$/P$\sb{\rm K}$ among patches from the electrocytes observed under identical recording conditions. My results support the conclusion that there is heterogeneity in the selectivty properties of the Na channels.

The high Na channel density in the intact electrocyte has allowed the recording of gating currents in isolated membrane patches. The properties of these gating currents were found to be similar to those of the squid giant axon and other preparations.
 
FEEDING STUDIES OF THE MURICID GASTROPOD OCENEBRA ERINACEA (LINNAEUS, 1758), WITH ULTRASTRUCTURAL AND HISTOCHEMICAL INVESTIGATIONS OF THE ABO (ACCESSORY BORING ORGAN)
by HUMPHREY, ELAINE CHRISTINA, Ph.D., University of Southampton (United Kingdom), 1990, 185 pages; AAT DX94706
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School: University of Southampton (United Kingdom)
School Location: England
Source: DAI-B 52/10, p. 5121, Apr 1992
Source type: DISSERTATION
Subjects: Oceanography
Publication Number: AAT DX94706
Document URL: Shibboleth Authentication Request
ProQuest document ID: 745393841

Abstract (Document Summary)

Available from UMI in association with The British Library.

The response to prey and the general feeding behaviour of Ocenebra erinacea was observed together with feeding rates under specific laboratory conditions of different light, temperature and salinity regimes.

The ultrastructure of the accessory boring organ (ABO) was investigated by standard electron microscopical techniques and development of the ODO method gaining a spacial interpretation of this structurally complex organ. In the full description of the ABO, septate junctions in the apical region of the ABO, and "beaded" microvilli, were recorded.

A number of histochemical studies, mostly at the ultrastructural level, were undertaken including Ca-ATPase, Na-K-ATPase, acid phosphatase, adenylate cyclase, substance P, serotonin, a tracer study using horseradish peroxide and an etching study of the secretion of the ABO on the chitin/protein complex of squid pen, furthering information chronicled on the muricid ABO. The enzyme results indicated at least three domains in the plasmalemma of the epithelial cells: the apical membrane, the contralacunal membrane, and the intercolumnar membrane.

Whilst investigating the developing ABO in the larvae, a method for inducing egg capsule production in the laboratory was formulated.
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Canales ionicos de neuronas septales aisladas: Caracterizacion electrofisiologica y modulacion por TRH y LHRH
by Castellano Orozco, Antonio Gonzalo, xx, Universidad de Sevilla (Spain), 1989, 128 pages; AAT C145815
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Alternate Language Title: Ionic channels in septal neurons: Characterization and modulation by TRH and LHRH
Language: Spanish , ES
School: Universidad de Sevilla (Spain)
School Location: Spain
Source: DAI-C 51/04, p. 541, Winter 1990
Source type: DISSERTATION
Subjects: Anatomy & physiology, Animals
Publication Number: AAT C145815
ISBN: 8474054826
Document URL: Shibboleth Authentication Request
ProQuest document ID: 743969711

Abstract (Document Summary)

The ionic currents of dispersed septal neurons were studied using the "whole-cell" variant of the "patch-clamp" technique. On depolarization all septal neurons generate Na, Ca, and K currents. The Na current activates rapidly and deactivates in 3 to 4 ms. This current is completely blocked by TTX and has characteristics similar to the ones of the Na current described by Hodgkin and Huxley in the squid giant axon. The calcium current is due to the activity of two types of calcium channels with properties similar to the fast (FD) and slow (SD) deactivating channels of other cells. The potassium current is mediated by at least three different K channels. There is a fast transient current which is deactivated at potentials more positive than $-$50 mV. At +40 mV this current deactivates almost totally in 20 ms. In addition, there are two components of slowly activating outward current, one of them with a clear dependence on the intracellular Ca$\sp{2+}$ concentration. The density of Na channels and the contribution of the different Ca and K channels to the total current varied from cell to cell. This indicates that there are several neuronal types in the septal nucleus. In some cells exposure to external TRH (1 $\mu$M) produces a reversible increase in the amplitude of the slow activating potassium current. In other cells, exposure to 1-3 $\mu$M TRH$\sb{\rm a}$ (acid form) produces a reversible decrease of the Na current amplitude without affecting either the activation and deactivation time courses or the shape of the I-V curve. A second exposure to TRH$\sb{\rm a}$ produces a lower effect. These results suggest the existence of a TRH receptor in the membrane of some cells of the septal nucleus. In some of the cells in which TRH$\sb{\rm a}$ previously produced a decrease in Na current amplitude, the exposure to 2-3 $\mu$M LHRH produces the same effect as the second exposure to TRH$\sb{\rm a}$.
 
STRUCTURE AND BIOCHEMISTRY OF SQUID PHOTORECEPTOR MICROVILLI
by LANGMACK, KEITH ANTONY, D.Phil., University of Oxford (United Kingdom), 1989, 170 pages; AAT D-91445
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School: University of Oxford (United Kingdom)
School Location: England
Source: DAI-B 51/10, p. 4737, Apr 1991
Source type: DISSERTATION
Subjects: Zoology, Oceanography, Anatomy & physiology, Animals, Biochemistry, Ophthalmology
Publication Number: AAT D-91445
Document URL: Shibboleth Authentication Request
ProQuest document ID: 745062521

Abstract (Document Summary)

Available from UMI in association with The British Library. Requires signed TDF.

This thesis reports results of studies on the proteins of squid photoreceptor microvilli. This serves as a model system both for signal transduction and for membrane-cytoskeletal interactions, which are crucial processes in the response of cells to external stimuli. The approach used here has been both biochemical and structural. First of all, the glycosylation of the microvillar proteins was investigated by lectin affinity blotting. This revealed that some of the cytoskeletal proteins were glycosylated. This gave a possible explanation for the cytoskeletal aggregating on isolation with non-ionic detergent. Some of the cytoskeletal proteins are transmembrane and the hydrophobic regions, exposed on addition of detergent, associate in a non-specific manner to produce the aggregation. The aggregates were reduced in size by the addition of high concentrations of salt. It was found that salt-solubilised proteins re-aggregated on the addition of micromolar quantities of Mg-ATP. This also results in the phosphorylation of two of the cytoskeletal proteins (molecular weights 110 and 130 kDa). A cytoskeletal protein of 110 kDa binds actin and cross-reacts with an antimyosin head monoclonal antibody. This protein was therefore thought to be a myosin I. Negative stain electron microscopy of the cytoskeleton has also shown the aggregation.

The structure of the microvillar membranes was studied by negative staining. This revealed projections from the surface that were associated with membrane-membrane interactions. By labelling the membranes with concanavalin A-gold, it was shown that these projections were most likely to be on the cytoplasmic surface of the membranes. Rhodopsin was purified by chromatography and reconstituted into lipid vesicles. These vesicles showed similar projections to the native membranes, indicating that the projections contain rhodopsin. Rhodopsin in native membranes was observed in partially ordered arrays.

The G$\sb{\beta}$ subunit (the $\beta$ subunit of a GTP-binding protein) was isolated by sucrose density gradient centrifugation. Vesicles containing this polypeptide had a morphology that was dependent on their lipid content rather than their protein content.
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INVESTIGATION OF THE MOLECULAR BASIS OF DIRECTED PARTICLE MOVEMENT IN THE SQUID GIANT AXON (VESICLES, CELL MOTILITY, FAST AXONAL TRANSPORT)
by GILBERT, SUSAN POND, Ph.D., Dartmouth College, 1986, 121 pages; AAT 8628285
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School: Dartmouth College
School Location: United States -- New Hampshire
Source: DAI-B 47/09, p. 3615, Mar 1987
Source type: DISSERTATION
Subjects: Biology
Publication Number: AAT 8628285
Document URL: Shibboleth Authentication Request
ProQuest document ID: 751453941

Abstract (Document Summary)

The research presented in this thesis was designed to provide new information about the motive force generating system responsible for the important neurological process, fast axonal transport. This process involves the rapid, bidirectional movement of membranous organelles along the length of the axon and is responsible for transfer of proteins and neurotransmitters or their precursors to the synapse. To learn more about this process, a model system was developed using isolated axoplasmic vesicles from the squid giant axon. The membranes of the vesicles were labeled fluorescently and were made to move either by injecting them into another axon or by allowing them to associate with an oriented microtubule substrate in the form of flagellar axonemal microtubules. In both model systems, the exogenous vesicles were observed to move bidirectionally and in an ATP dependent and trypsin sensitive manner. Furthermore, these vesicles were observed to translocate on isolated axonemal microtubules in the presence or absence of flagellar dynein. Because the vesicles were observed to move in either direction on a single axoneme, the inherent structural polarity of the microtubule did not specify the direction of vesicle movement. Moreover, the vesicle motility was ATP dependent and trypsin sensitive, yet flagellar dynein was not responsible for the vesicle translocations.

Because isolated microtubules were shown to support vesicle motility, it was assumed that the ATP binding proteins essential for vesicle translocation were present in the vesicle preparation. To identify these molecules, the radioactive photoaffinity analog of ATP, (alpha)('32)P 8-azidoadenosine 5'-triphosphate, was used. The results identify and characterize a vesicle associated polypeptide that bound the analog. This polypeptide was isolated in association with vesicles or stabilized microtubules and migrated at an M(,r) of 292 kd. Furthermore, the 292 kd polypeptide crossreacted with antiserum to porcine brain microtubule associated protein 2 (MAP 2). Because the 292 kd polypeptide binds ATP, is associated with axoplasmic vesicles that translocate on MAP-free microtubules in an ATP dependent manner, and can be isolated in association with vesicles and microtubules, this MAP 2-like polypeptide is believed to be involved in vesicle-microtubule interactions that promote vesicle motility.
 
TRANSPORT OF SECRETORY VESICLES IN MURINE ANTERIOR PITUITARY TUMOR CELLS (FAST, REGULATED SECRETION, ATT-20 CELLS)
by SCHROER, TRINA ALEXIS, Ph.D., University of California, San Francisco, 1986, 157 pages; AAT 8613054
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School: University of California, San Francisco
School Location: United States -- California
Source: DAI-B 47/03, p. 1044, Sep 1986
Source type: DISSERTATION
Subjects: Biochemistry
Publication Number: AAT 8613054
Document URL: Shibboleth Authentication Request
ProQuest document ID: 753313461

Abstract (Document Summary)

Secretory and membrane proteins destined for export from the cell move to the cell surface in membrane vesicles. Two biochemically distinct classes of secretory vesicles exist in the murine anterior pituitary tumor cell line AtT-20. I have demonstrated using indirect immunofluorescence that proteins carried in the different vesicles have different intracellular destinations. ACTH is concentrated at the tips of cell processes and in the Golgi region. In contrast, the constitutively exported murine leukemia virus membrane glycoprotein is observed only in the cell body plasma membrane and not in processes. The influenza virus membrane glycoprotein, hemagglutinin, introduced into cells by transfection, is also constitutively exported and is found exclusively on the cell body surface. Constitutive secretory vesicles appear to release their contents only at the surface of the cell body and not in processes.

Secretion from the regulated and constitutive secretory pathways is inhibited to different degrees by reduced temperature. Constitutive secretion of ACTH precursor and the secreted form of vesicular stomatitis virus glycoprotein is inhibited approximately 7-fold at 20(DEGREES)C. In the regulated pathway, ACTH precursor is processed to mature ACTH and stored in dense core secretory granules at least as well at 20(DEGREES)C as at 37(DEGREES)C. Autoradiography of sulfate labeled cells indicated that secretory granules are transported normally to the ends of processes at 20(DEGREES)C. However, regulated secretion of mature ACTH is inhibited completely.

The movement of isolated secretory vesicles along axonal microtubules was examined in vitro. Purified synaptic vesicles from electric rays were fluorescently labeled and their movement in cytoplasm isolated from squid giant axons was examined by fluorescence microscopy. The synaptic vescles behaved like endogenous squid organelles, moving preferentially toward the synapse at a velocity of 2 microns per second and binding to microtubules when movement was inhibited by a non-hydrolyzable ATP analog. Vesicles that had been proteolytically digested with trypsin or pronase were observed to move in axoplasm and to bind to microtubules but the direction preference was abolished. Vesicles treated with elastase neither moved nor bound. Apparently, different synaptic vesicle membrane proteins are responsible for the property of microtubule binding and the preference for anterograde movement.
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STUDIES OF TWO NATURALLY OCCURRING COMPOUNDS WHICH EFFECT RELEASE OF ACETYLCHOLINE FROM SYNAPTOSOMES
by KOENIG, MICHAEL LEO, Ph.D., University of Southern California, 1985; AAT 0557728
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School: University of Southern California
School Location: United States -- California
Source: DAI-B 46/12, p. 4098, Jun 1986
Source type: DISSERTATION
Subjects: Biology
Publication Number: AAT 0557728
Document URL: Shibboleth Authentication Request
ProQuest document ID: 752246591

Abstract (Document Summary)

Two naturally occurring compounds which effect the release of neurotransmitter from synaptosomes have been purified to apparent homogeneity. Iotrochotin (IOT) isolated from wound exudate of the Caribbean purple bleeder sponge promotes release in a manner that is independent of the extracellular Ca('2+) ion concentration. Leptinotarsin (LPT-d), a protein taken from hemolymph of the Colorado potato beetle, Leptinotarsa decemlineata, stimulates Ca('2+)-dependent release.

IOT, purified by conventional chromatographic techniques, migrates as a single band on sodium dodecylsufate polyacrylamide gel electrophoresis (SDS-PAGE) slab gels. The protein is slightly acidic and has a molecular weight of approximately 18 kD. ('3)H Acetylcholine which has been introduced into synaptosomes as ('3)H choline can be released by IOT. The toxin releasable pool of labelled neurotransmitter is not depleted by depolarization of the synaptosomes with high potassium, and therefore seems to be primarily extravesicular. That IOT has membrane permeabilizing properties is suggested by the finding that small cytoplasmic molecules can be co-released with neurotransmitter. Adenosine triphosphate and exogenously added 2- ('3)H deoxy-D-glucose are readily released by the toxin, whereas larger cytoplasmic marker enzymes are not.

LPT-d is a larger protein (molecular weight = 45 kD) than IOT, and seems to effect primarily vesicular release by opening at least one type of presynaptic Ca('2+) channel. The facilitatory effects of the toxin on synaptosomal release can be inhibited by inorganic Ca('2+) channel antagonists, but are not generally affected by organic antagonists thought to be most effective as inhibitors of slow Ca('2+) channels. There is some evidence that the organic antagonist nifedipine, if added after LPT-d, can close the toxin-activated channels in cultured rat diencephalon cells. If so, the channels affected may be homologous with those found in smooth muscle and heart. Studies of the effects of LPT-d on Ca('2+) channels from a variety of tissues including Paramecium, squid optic lobe, smooth and skeletal muscle, and neuronal clonal cell lines, have shown the toxin to be an activator specifically of a type of channel found only in the mammalian central nervous system.

(Copies available exclusively from Micrographics Department, Doheny Library, USC, Los Angeles, CA 90089-0182.)
 
DIELECTRIC PROPERTIES OF THE SQUID GIANT AXON MEMBRANE
by FERNANDEZ, JULIO MARIANO, Ph.D., University of California, Los Angeles, 1982, 81 pages; AAT 8219681
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School: University of California, Los Angeles
School Location: United States -- California
Source: DAI-B 43/04, p. 962, Oct 1982
Source type: DISSERTATION
Subjects: Biophysics
Publication Number: AAT 8219681
Document URL: Shibboleth Authentication Request
ProQuest document ID: 753149681

Abstract (Document Summary)

Dielectric polarization of the cell membrane resulting from distortion and alignment of molecules under the influence of the applied electric field has been demonstrated in the squid giant axon membrane.

A method of measuring membrane dielectric polarization is developed in this dissertation. The method consists of measuring the complex admittance of the squid giant axon membrane under voltage clamp in the absence of ionic conductances for different membrane potentials. This is accomplished by adding a small Pseudo Random Binary Sequence (PRBS) to the membrane potential and the admittance is obtained from the applied membrane potential and its current response using Fourier techniques. Detailed design specifications are given for the implementation of the PRBS noise generator.

The results show that the membrane admittance is voltage dependent in the range between -120 mV and 50 mV and it is independent of the membrane potential outside this range. The voltage dependent part of the admittance can be related to the movement of charges responsible for the opening and closing of the sodium channel demonstrated previously by other techniques (Armstrong and Bezanilla, 1973).

The voltage independent admittance shows characteristics of dielectric loss which can be related to the movement of charges or dipoles which are likely to be associated to those intrinsic proteins of the membrane whose function is other than the gating of voltage dependent ionic channels.

The admittance results support the view that the membrane is a mosaic of regions with different dielectric properties. This hypothesis is supported by experiments showing that the movement of charges responsible for sodium channel gating respond differently than lipophilic ions to perturbations of the lipid matrix. This suggests that the gating charge movement occurs in a region order than the bulk lipid matrix.
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CALCIUM HOMEOSTASIS AND THE EFFECT OF ANTICHOLINERGIC COMPOUNDS IN RAT BRAIN
by MELAMED, BRIAN RICHARD, Ph.D., Temple University, 1980, 112 pages; AAT 8025145
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School: Temple University
School Location: United States -- Pennsylvania
Source: DAI-B 41/05, p. 1736, Nov 1980
Source type: DISSERTATION
Subjects: Pharmacology
Publication Number: AAT 8025145
Document URL: Shibboleth Authentication Request
ProQuest document ID: 753778231

Abstract (Document Summary)

The influence of QNB (3-quinuclidinyl benzilate), benactyzine, atropine, scopolamine, dexetimide (d-benzetimide), and levetimide (l-benzetimide) on the calcium content of rat brain cortex slices was investigated. Slices were incubated either in "normal" (5 mMCl) glucose-bicarbonate medium at 37(DEGREES) for 60 min. or were depolarized by incubation in a medium containing 100 mM KCl. It was found that all of the compounds tested exerted effects only on depolarized slices. QNB at 0.1 and 1.0 mM inhibited the increase in calcium content of the depolarized slices. Studies of calcium efflux from ('45)Ca preloaded slices indicated that low concentrations of QNB (0.1, 0.01 mM) inhibited calcium extrusion while at high concentration (1.0 mM) QNB produced a slight enhancement of the rate of calcium efflux. Similar effects on calcium content were noted for benactyzine which was equipotent to QNB except at the 10 (mu)M concentration where no effect was observed. The stereoisomers, d- and l-benzetimide were approximately equipotent in their effects on calcium although the d-isomer has been shown to have 2000 times greater affinity for the muscarinic receptor. This would indicate that the calcium antagonistic effect is not mediated via an action on the muscarinic receptor. The belladonna alkaloids, atropine and scopolamine were considerably less potent than QNB. When the "lanthanum technique" was employed to displace extracellularly bound Ca('++) and to measure intracellular Ca('++) levels, it was found that 1, 10, and 100 (mu)M QNB all produced approximately the same degree of inhibition of K('+) - stimulated calcium accumulation. The effect of QNB on subcellular calcium storage sites showed that concentrations above 0.1 mM were required to inhibit energy-dependent calcium accumulation by rat brain mitochondrial and microsomal fractions. The effects were achieved in a calmodulin-independent manner, indicating therefore, that calmodulin was probably not a primary site of action. Studies in slices with vanadate ion, a specific inhibitor of ATP-dependent sodium independent, calcium pumping mechanisms in squid axons, produced an increase in calcium content that produced by omission of Na('+) ions. This observation provides further evidence for the existence of a dual mechanism for the extrusion of calcium from mammalian nervous tissue. Under conditions in which both efflux mechanisms were inhibited, QNB decreased the calcium content relative to the inhibited slices. The level of calcium achieved was still greater than that of the control slices. This indicated that blockade of calcium channels by QNB was at best incomplete and inadequate to explain the large decrease in calcium content observed. It was concluded that QNB displaced calcium from binding sites within the cell. The site of intracellular calcium storage affected was most likely the inner aspect of the plasma membrane. Some blockade of calcium channels must also occur in light of the observation that QNB decreased calcium content while inhibiting efflux. Results are discussed with regard to the overall nature and mechanisms of calcium storage in brain tissue. In addition, a suggestion is made relating the increased ability of QNB to alter calcium metabolism and the greater psychotomimetic potency of some of the glycolate esters as compared to other classes of anticholinergic compounds.
 
Those are a selection of theses available online.

DO NOT ASK ME TO TRANSLATE ANY OF IT!!! SOMEONE ASKED A QUESTION - I THROUGH A LITTLE RESEARCH BACK.

It's not English to me either!
 
Nice selection, Steve. It is interesting what a search will show.

Oh, as far as Characterization of squid KV1 voltage-gated potassium channels by expression in Xenopus oocytes? Xenopus is the genus of the African clawed frogs. Just a little offbeat trivia there.

D'oh! I misread the original question entirely... Forgot it was about cell membranes and temperature. Thought it was about the webbing tissue.

John
 
I had a read through most of that stuff, not too much on membranes - the Na gate thing is about electrical signals such as those in nerve fibres being inhibited by various chemicals. Most of the results turned up because they happened to use the words squid or membrane, although a few were focused on squids - the mRNA of giant squid nerve fibres was one.

I had a look through some I the stuff I did for a project, concerning tissues
- "Lipinsky M , the ammonium content in the tissues of selected squid species."
I know tissues arent membranes, but it might be on the right track. -
If you can find it, it may have info and some good references on the topic.
 

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