Possible mechanism of membrane fusion

The stalker mechanism of membrane fusion was considered. Initiation and evolution of monolayer and bilayer bridges-stalks between the membranes were studied. From the expression of elastic energy of the stalk the value of spontaneous curvature of its membrane Ks at which the bridge may appear, was found. It was shown that in terms of the stalker mechanism formation of the stalk of the final radius or complete fusion were possible Ks values for realizing this or that variant were found. The energetic barrier of hydrophobic interaction and the barrier of elastic energy which the membranes had to overcome for stalker formation were found. The experimental data on the fusion of small and large liposomes were analysed.     

Possible role of transient electric fields in freezing-induced membrane destabilization

Summary Evidence is presented to support the hypothesis that electrical potentials generated during the freezing of aqueous solutions (the Workman-Reynolds effect) may contribute to the destabilization of the plasma membrane and cryoinjury of isolated protoplasts. Specifically. (1) electric potential diffrences of sufficient magnitude to cause lysis of the plasma membrane occur during the rapid freezing of isolated protoplasts suspended in sorbitol: (2) survival of protoplasts is inversely correlated with the magnitude of the potential difference and (3) cold acclimation increases the stability of the plasma membrane to applied electric fields. A discussion is given of the different physical phenomena though to be involved in the Workman-Reynolds effect. The basis equations for these phenomena are outlined.     

Possible role of electrical bilayers in the reaction of biological objects to external factors

Coincidence in the effects of the sound and electromagnetic threshold flows on receptors or organism accordingly and double electrical layer (DEL) is shown. The existence of universal non-specific mechanism of action of external factors upon the living tissue based on the DEL-reaction is suggested.     

Possible role of membrane proteins in mercury resistance of Enterobacter aerogenes

Mercury resistance shown by a strain of Enterobacter aerogenes was found to be determined by a plasmid. The resistance appeared to be not due to enzymatic volatilization of mercury, but due to the alteration in cellular permeability to mercury.Comparison of the outer membrane proteins was made between the resistant cells and the sensitive counterparts obtained by the treatment with mitomycin C, showing that two proteins with molecular weight of 46,000 and 44,000 had disappeared from the outer membrane along with the plasmid by the curing. These results suggest that the two membrane proteins mediating the cellular permeability to mercury compound may be responsible for the mercury resistance of the strain.     

Possible role of deep tubular invaginations of the plasma membrane in MHC-I trafficking

Tubules and vesicles are membrane carriers involved in traffic along the endocytic and secretory routes. The small GTPase Arf6 regulates a recycling branch of short dynamic tubular intermediates used by major histocompatibility class I (MHC-I) molecules to traffic through vesicles between endosomes and the plasma membrane. We observed that Arf6 also affects a second network of very long and stable tubules containing MHC-I, many of which correspond to deep invaginations of the plasma membrane. Treatment with wortmannin, an inhibitor of phosphatidylinositol-3-phosphate kinase, prevents formation of the short dynamic tubules while increasing the number of the long and very stable ones. Expression of NefAAAA, a mutant form of HIV Nef, increases the number of cells containing the stable tubules, and is used here as a tool to facilitate their study. Photoactivation of NefAAAA-PA-GFP demonstrates that this molecule traffics from endosomes to the tubules. Finally, live-cell imaging also shows internalization of MHC-I molecules into these tubules, suggesting that this is an additional route for MHC-I traffic.     

Possible mechanism for the influence of weak magnetic fields on biological systems

A physical mechanism is suggested for a resonant interaction of weak magnetic fields with biological systems. An ion inside a Ca(2+)-binding protein is approximated by a charged oscillator. A shift in the probability of ion transition between different vibrational energy levels occurs when a combination of static and alternating magnetic fields is applied. This in turn affects the interaction of the ion with the surrounding ligands. The effect reaches its maximum when the frequency of the alternating field is equal to the cyclotron frequency of this ion or to some of its harmonics or sub-harmonics. A resonant response of the biosystem to the magnetic field results. The proposed theory permits a quantitative explanation for the main characteristics of experimentally observed effects.     

Possible role of helix-coil transitions in the microscopic mechanism of muscle contraction.

Local helix-coil transitions in the coiled coil portion of myosin have long been implicated as a possible origin of tension generation in muscle. From a statistical mechanical theory of conformational transitions in coiled coils, the free energy required to form a randomly coiled bubble in the hinge region of myosin of the type conjectured by Harrington (Harrington, W. F., 1979, Proc. Natl. Acad. Sci. USA, 76:5066-5070) is estimated to be approximately 25 kcal/mol. Unfortunately this is far more than the free energy available from ATP hydrolysis if the crossbridges operate independently. Thus, in solution such bubbles are predicted to be absent, and the theory requires that the rod portion of myosin be a hingeless, continuously deforming rod. While such bubble formation in vivo cannot be entirely ruled out, it appears to be unlikely. We further conjecture that in solution the swivel located between myosin subfragments 1 and 2 (S-2 and S-1) is due to a locally random conformation of the chains caused by the presence of a proline residue at the point that physically separates the coiled coil from the globular portion of myosin. On attachment of S-1 to actin in the strong binding state, the configurational entropy of the random coil in the swivel region is greatly reduced relative to the case where the ends are free. This produces a spontaneous coil-to-helix transition in the swivel region that causes rotation of S-1 and the translation of actin. Thus, the model predicts that the actin filaments are pushed rather than pulled past the thick filaments by the crossbridges. The specific mechanism of force generation is examined in detail, and a simple statistical mechanical realization of the model is proposed. We find that the model gives a substantial number of qualitative and at times quantitative predictions in accord with experiment, and is particularly appealing in that it provides a simple means of free energy transduction--the well known fact that topological constraints shift the equilibrium between helical and random coil states.     

Possible mechanism of the reorganization of the cardiomyocyte plasma membrane in the suslik in the hibernation-arousal-wakefulness cycle

Studies have been made on the ultrastructure of cardiomyocytes during hibernation and arousal of the ground squirrel C. undulatus. It was found that the number of elements of the rough endoplasmic reticulum, Golgi complex, vesicles and ribosomes increases in the perinuclear areas of cardiomyocytes during arousal of animals. These areas are saturated with lipid inclusions and mitochondria. Numerous vesicles and fringed bubbles were found near the plasma membrane which has many caveolae. These findings may indicate the intense metabolism of the membrane material between plasmalemma and cytoplasmic vesicles. Possible mode of rapid reorganization of the sarcolemma and changes in its functional properties during hibernation-arousal stages are suggested. It is concluded that apart from structural and functional properties which are acquired by cells during preparation of animals to hibernation and which exhibit only small changes during the whole period of hibernation, cyclic changes in plasmalemma structure and function occur during arousal of the ground squirrels.     

Possible palindromes in immunoglobulin heavy-chain genes: Their role in membrane attachment

An analysis of mRNA structures as deduced from the amino acid sequences of immunoglobulin heavy chains reveals possible base-paired regions within the sequences coding for the 20 C-terminal amino acids of the human and chains. The two regions are similar in structure and contain a palindrome which might serve as an enzyme recognition site. Although other base-paired regions can be predicted in the remainder of the constant regions of these heavy chains, they have no common features. These regions and the palindromes within them may be involved in the regulation of membrane and serum immunoglobulin synthesis. Two possible mechanisms for this are proposed.