Membrane transport system

Some alcohols, eg, propylene glycol, not only lower water activity but also have an additional preservative effect caused by the way they interfere with the ceU membrane transport system of the contaminating microorganisms. Surfactants (qv) may show a similar effect. 

Adenosine is produced by many tissues, mainly as a byproduct of ATP breakdown. It is released from neurons, glia and other cells, possibly through the operation of the membrane transport system. Its rate of production varies with the functional state of the tissue and it may play a role as an autocrine or paracrine mediator (e.g. controlling blood flow). The uptake of adenosine is blocked by dipyridamole, which has vasodilatory effects. The effects of adenosine are mediated by a group of G protein-coupled receptors (the Gi/o-coupled Ai- and A3 receptors, and the Gs-coupled A2a-/A2B receptors). Ai receptors can mediate vasoconstriction, block of cardiac atrioventricular conduction and reduction of force of contraction, bronchoconstriction, and inhibition of neurotransmitter release. A2 receptors mediate vasodilatation and are involved in the stimulation of nociceptive afferent neurons. A3 receptors mediate the release of mediators from mast cells. Methylxanthines (e.g. caffeine) function as antagonists of Ai and A2 receptors. Adenosine itself is used to terminate supraventricular tachycardia by intravenous bolus injection. 

When the new term permease was coined to designate bacterial membrane proteins specialized in the transport of specific metabolites [1,2], it covered a concept which was not quite new. The existence of membrane transport systems had been demonstrated in animal tissues by Cori as early as 1925 (see [3]). However, the discovery and characterization of permeases in bacteria revolutionized prospects for studying the properties of transport systems, opening the way to a new field and a very fruitful methodology. 

The first of the haem uptake systems to be characterized at molecular level was that of Yersinia enterolitica, which closely resembles a typical siderophore uptake system (Stojiljkovic and Hantke, 1992, 1994), including a TonB-dependent outer membrane receptor for haem, a periplasmic binding protein, and a cytoplasmic membrane transport system. There also seems to be a protein that degrades haem and liberates haem iron within the cell. TonB-dependent outer membrane receptor proteins for haem have been cloned and sequenced from Shigella dysenteriae and E. coli (Mills and Payne, 1995 Torres and Payne, 1997), while in Vibrio cholera two genes are required for haem utilization, one an outer membrane receptor a second which may have a TonB-like function (Henderson and Payne, 1994). 

Wieland, T., et al. Identity of hepatic membrane transport systems for bile salts, phalloidin, and antamanide by photoaffinity labeling. Proc. Natl. Acad. Sci. U. S. A. 1984, 81, 5232-5236. 

Mercury can influence ion, water, and nonelectrolyte transport in different cells [ 14, 77]. The cell membrane is believed to be the first point of attack by heavy metals however, intracellular enzymes and metabolic processes may also be inhibited [70, 78, 79]. The attachment of heavy metals to ligands in or on the plasma membrane may result in changes in passive permeability or selective blockage of specific transport processes. Many membrane transport systems are known to be sensitive to sulphydryl-group modification [ 14, 80, 81]. 

The oxaloacetate formed in the mitochondrial matrix is initially reduced to ma-late, which can leave the mitochondria via inner membrane transport systems (see p. 212). 

The adenylyl cyclases are large transmembrane proteins with a complex transmembrane topology. The assumed topology (Fig. 5.22) shows a short cytoplasmic N-termi-nal section followed by a transmembrane domain Ml with six transmembrane sections, and a large cytoplasmic domain Cl. The structural motif is repeated so that a second transmembrane domain M2 and a second cytoplasmic domain C2 can be differentiated. The complicated structure resembles the structure of some ATP-dependent membrane transport systems such as the P glycoprotein. A transport function has not yet been demonstrated for adenylyl cyclase. 

Inhibitors of HMG-CoA reductase activity (for example compac-tin240), or compounds that lower the levels of the enzyme (including a number of oxygenated cholesterol derivatives,241- 24 la such as 25-liy-droxycholesterol), not only decrease the formation of polyprenyl diphosphate, but also affect the formation of cholesterol and the polyprenyl side-chains of coenzyme Q. Consequently, prolonged treatment with such compounds may cause side effects, for example, changes in membrane fluidity (see also, Section III,5), decreased activity of membrane enzymes,1214,2,3 and inactivation of membrane transport systems,246 and, therefore, indirectly prevent glvcosvlation of proteins. 

If the (3-lyase enzyme, or the renal basolateral membrane transport system, or y-glutamyltransferase, or cysteinylglycinase is inhibited, the nephrotoxicity of DCVC can be reduced, indicating that each of these processes is involved. 

A second membrane transport system essential to oxidative phosphorylation is the phosphate translocase, which promotes symport of one H2PO4 and one H+ into the matrix. This transport process, too, is favored by the transmembrane proton gradient (Fig. 19-26). Notice that the process requires movement of one proton from the P to the N side of the inner membrane, consuming some of the energy of electron transfer. A complex of the ATP synthase and both translocases, the ATP synthasome, can be isolated from... 

It seems unlikely that the first living cellular systems had time to evolve highly specialized membrane transport systems, which brings up the ques-... 

Figure 9.29 Some mammalian (left) and microbial (right) membrane transport systems. (A) Primary electrogenic mechanisms (pumps) creating either a Na+ or a H+ gradient. (B) Secondary active transport systems of the symport type, in which the entry of a nutrient S into the cell is coupled with the entry of either the sodium ions or protons. (D) Various passive ion movements, possibly via channels or uniports. (Reproduced by permission from Serrano R. Plasma Membrane ATPase of Plants and Fungi. Boca Raton CRC Press, 1985, p. 59.)...

Table 10.4. Some facilitated membrane transport systems ...

Decreased uptake leads to lower intracellular drug concentrations. In many cisplatin-resistant cell lines, reduced accumulation was observed. The cisplatin membrane transport system is poorly understood, but studies on cisplatin-resistant cells with decreased drug accumulation have identified two membrane proteins that may be involved in uptake and efflux respectively a 48-kDa protein with decreased expression and a 200-kDa glycoprotein with increased expression. 

Stimulus-evoked, calcium-dependent release of acetylcholine (ACh) from the cholinergic synapse normally occurs through the formation of a fusion complex between ACh-containing vesicles and the intracellular leaflet of the nerve terminal membrane (Amon et al., 2001). This synaptic vesicle fusion complex consists of several proteins of the SNARE family, including a 25 kDa synaptosomal associated protein (SNAP-25), vesicle-associated membrane protein (VAMP, or synaptobrevin), and the synaptic membrane protein syntaxin. Other SNARE proteins have been identified as components of membrane transport systems in yeast and mammals but have not been implicated as targets for BoNTs. Meanwhile, type A and E neurotoxins cleave SNAP-25 while types B, D, F, and G act on VAMP and type C1 toxin cleaves both syntaxin and SNAP-25. Neurotoxin-mediated cleavage of any of these substrates disrupts the processes involved in the exocytotic release of ACh and leads to flaccid paralysis of the affected skeletal muscles. 

Fig. I. Schematic apparatus for experiment (a) adsorption(electtic cahn balance)mBasureinent system and (b) membrane transport system...

MTS = specific membrane transport system for ornithine ( urea starter )... 

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