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Gene/Protein
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Target Concepts:
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Query: UMLS:C0276640 (
TEM
)
20,729
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
It is well known that arginine vasopressin (AVP) produces up to a 40-fold increase (0.1 to 4.0 microL/min.cm2) in net water flux across the amphibian urinary bladder under an osmotic gradient (mucosal side 10% hypotonic). No AVP effect is observed when the gradient is in the opposite direction (serosal hypotonic). Similar asymmetrical behavior to osmotic gradients occurs in the frog corneal epithelium. This rectification phenomenon has not been satisfactorily explained. We measured net water fluxes in bladder sacs and confirmed that AVP has no effect when the serosal bath is hypotonic. We reasoned that the 'abnormal' serosal osmolarity was inducing changes in membrane water permeability, the very parameter being measured. Thus, we studied the effect of solution osmolarity on diffusional water flow (Jdw) across the frog bladder using 3H2O. As expected, AVP doubled Jdw (in either direction from 12 to 21 microL/min.cm2) when the serosal solution was iso-osmolar regardless of mucosal osmolarity. However, in the AVP-stimulated bladders, hypo-osmolarity of the serosal solution reduced Jdw by 42%, an effect that was reversible when normal osmolarity was re-established. Amphotericin B (instead of AVP) was used to irreversibly increase the permeability to water of the apical membrane. Under these conditions, basolateral hypotonicity also reversibly decreased Jdw by 32%, suggesting the basolateral membrane as the site where permeability is reduced. SEM and
TEM
of the tissue shows extreme swelling when it was exposed to serosal hypotonicity with or without AVP and typical surface morphology changes following hormone stimulation. We conclude that this swelling may initiate a signaling mechanism that reduces basolateral water permeability. These findings constitute evidence of basolateral
water channel
permeability regulation, which can also contribute to cell volume regulation.
...
PMID:Evidence of basolateral water permeability regulation in amphibian urinary bladder. 946 4
The Omega-loop of
TEM
beta-lactamase is involved in substrate recognition and catalysis. Its dynamical properties and interaction with water molecules were investigated by performing multiple molecular dynamics simulations of up to 50 ns. Protein flexibility was assessed by calculating the root mean-square fluctuations and the generalized order parameter, S(2). The residues in secondary structure elements are highly ordered, whereas loop regions are more flexible, which is in agreement with previous experimental observations. Interestingly, the Omega-loop (residues 161-179) is rigid with order parameters similar to secondary structure elements, with the exception of the tip of the loop (residues 173-177) that has a considerably higher flexibility and performs an opening and closing motion on the 50-ns timescale. The rigidity of the main part of the Omega-loop is mediated by stabilizing and highly conserved water bridges inside a cavity lined by the Omega-loop and residues 65-69 of the protein core. In contrast, the flexible tip of the Omega-loop lacks these interactions. Hydration of the cavity and exchange of the water molecules with the bulk solvent occurs via two pathways: the flexible tip that serves as a door to the cavity, and a temporary
water channel
involving the side chain of Arg(164).
...
PMID:Multiple molecular dynamics simulations of TEM beta-lactamase: dynamics and water binding of the omega-loop. 1988 98