2005
DOI: 10.1590/s0100-879x2005000800007
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Abstract: Many cellular proteins are bound to the surfaces of membranes and participate in various cell signaling responses. Interactions between this group of proteins are in part controlled by the membrane surface to which the proteins are bound. This review focuses on the effects of pressure on membrane-associated proteins. Initially, the effect of pressure on membrane surfaces and how pressure may perturb the membrane binding of proteins is discussed. Next, the effect of pressure on the activity and lateral associat… Show more

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Cited by 21 publications
(15 citation statements)
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References 17 publications
(12 reference statements)
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“…Membrane-bound, G-protein-regulated phospholipase C-ß (PLC-ß) metabolizes PIP-4,5-bisphosphate and modulates intracellular calcium concentrations and protein kinase C activities, and its activity is increased by pressure, as observed with previously studied PLC-∆. Dr. Scarlata's group showed that, as is the case for other interfacial enzymes, membrane binding was pressure-independent, that high hydrostatic pressure activated PLC-ß by hydration/conformation changes at the catalytic core, and moreover that, in the presence of the membrane, association with the regulatory G-protein was favored and that pressure up to 2 kbar did not increase hydration of the membrane interface (12). This was interpreted to indicate that the presence of membranes stabilized the protein complex due to the protein confinement on its surface, therefore pointing to a role of a reduced volume in the lateral association between membrane proteins.…”
Section: The Conference On High Pressure Bioscience and Biotechnologysupporting
confidence: 66%
See 1 more Smart Citation
“…Membrane-bound, G-protein-regulated phospholipase C-ß (PLC-ß) metabolizes PIP-4,5-bisphosphate and modulates intracellular calcium concentrations and protein kinase C activities, and its activity is increased by pressure, as observed with previously studied PLC-∆. Dr. Scarlata's group showed that, as is the case for other interfacial enzymes, membrane binding was pressure-independent, that high hydrostatic pressure activated PLC-ß by hydration/conformation changes at the catalytic core, and moreover that, in the presence of the membrane, association with the regulatory G-protein was favored and that pressure up to 2 kbar did not increase hydration of the membrane interface (12). This was interpreted to indicate that the presence of membranes stabilized the protein complex due to the protein confinement on its surface, therefore pointing to a role of a reduced volume in the lateral association between membrane proteins.…”
Section: The Conference On High Pressure Bioscience and Biotechnologysupporting
confidence: 66%
“…Suzanne F. Scarlata (State University of New York, Stony Brook, USA) reported on The Effects of Pressure on the Activated State of Phospholipase C-ß and its Interaction with G Protein Subunits (12). Membrane-bound, G-protein-regulated phospholipase C-ß (PLC-ß) metabolizes PIP-4,5-bisphosphate and modulates intracellular calcium concentrations and protein kinase C activities, and its activity is increased by pressure, as observed with previously studied PLC-∆.…”
Section: The Conference On High Pressure Bioscience and Biotechnologymentioning
confidence: 99%
“…The pressure and the shearing forces exerted on the sperm cells by the flushing method should be taken into account. Negative effect of pressure have been described in previous report on different types of cell (Bouaziz et al 1998;Fioravanti et al 2005;Santiago-Moreno et al 2007), perhaps caused by changes in ion fluxes through membranes (Podolsky 1956) and the perturbation of membrane-bound proteins (Scarlata 2005). However, no such differences were seen between samples after cooling at 5°C for 24 or 48 h, suggesting that any harmful effects are transitory and are more probably due to the activation of the less mature spermatozoa.…”
Section: Discussionmentioning
confidence: 59%
“…; Santiago‐Moreno et al. ), perhaps caused by changes in ion fluxes through membranes (Podolsky ) and the perturbation of membrane‐bound proteins (Scarlata ). However, no such differences were seen between samples after cooling at 5°C for 24 or 48 h, suggesting that any harmful effects are transitory and are more probably due to the activation of the less mature spermatozoa.…”
Section: Discussionmentioning
confidence: 99%
“…However, this method reduced sperm viability by about 7%, suggesting it may subject sperm cells to considerable mechanical stress. Many studies report the negative effects of high pressures on different cell types [Bouaziz et al 1998;Fioravanti et al 2005], perhaps caused by changes in ion fluxes through membranes [Podolsky 1956] and the perturbation of membrane-bound proteins [Scarlata 2005]. Early studies showed that the application of controlled pressure to bovine sperm cells resulted in a reduction in their motility, an increase in the number of spermatozoa with acrosome abnormalities, and an increase in the release of glutamic oxalacetic transaminase and hyaluronidase [Carter et al 1973].…”
Section: Discussionmentioning
confidence: 99%