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At least 631 records · Page 35Linked to original sources
PubMed1988

[Mechanism of cell damage by hematoporphyrin derivative (HPD) plus light. II. Effect of HPD plus light on respiration and oxidative phosphorylation in hepatoma cells and normal liver mitochondria].

The effects of HPD plus light on energy metabolism and membrane structure of hepatoma cell and normal liver mitochondria were investigated. HPD was bound to mitochondria either in vitro or in vivo. Mitochondria bound HPD plus light increased MDA level, decreased respiratory intensity and respiratory control, dissociated phosphorylation from oxidation and enhanced mitochondria swelling on age. These effects were related to HPD concentration and exposure time but it was unchanged in the control. These results showed that the loss of function of oxidation phosphorylation was due to the mitochondrial membrane system damage under the action of singlet oxygen produced by HPD bound mitochondria following light activation.

Animals↗
PubMed1988

[Dependence of the degree of synergism in the simultaneous action of UV light and hyperthermia on yeast cells on the intensity of the UV light].

In experiments with wild-type diploid yeast cells of Saccharomyces cerevisiae it was shown that the definite temperature interval revealed the synergistic effect under simultaneous action of UV radiation and hyperthermia. The correlation between the degree of synergistic interaction and UV light intensity and irradiation temperature was estimated: the temperature interval synergistically enhancing the UV light effect was shifted towards higher temperatures as the UV light intensity was increasing, the optimal temperature to achieve the most synergistic effect existing for every intensity examined.

Diploidy↗
PubMed1988

Structure of human clathrin light chains. Conservation of light chain polymorphism in three mammalian species.

Complementary DNAs (cDNA) encoding the brain and non-brain forms of the human clathrin light chains LCa and LCb have been isolated, sequenced, and compared with their homologues in cow and rat. The significant differences that distinguish LCa from LCb and the brain from non-brain forms show remarkable preservation in all three species. These features include the position and sequence of the brain-specific inserts, a totally conserved region of 22 residues near the amino terminus, the LCb-specific phosphorylation site, the heavy chain binding site, and a distinctive pattern of cysteine residues near the carboxyl terminus. Unorthodox sequences for translation initiation and polyadenylation are found for LCb contrasting with LCa which exhibits orthodox regulatory sequences. Small insertions in human LCa revealed a duplicated sequence of 13 residues that flank the 22-residue conserved region. Only the carboxyl-terminal copy of this sequence is present in LCb. All sequences are consistent with the heavy chain binding site comprising an alpha-helical central region of the light chains. The hydrophobic face of this helix, which is presumed to interact with the heavy chain, is highly conserved between LCa and LCb, whereas the hydrophilic face shows considerable divergence. To help define the carboxyl-terminal limit of the heavy chain binding region, the epitope recognized by the CVC.6 monoclonal antibody was localized to residues 192-208 of LCa with glutamic acid 198 being of most importance. The faithful preservation of clathrin light chain polymorphism in three mammalian species provides evidence supporting a functional diversification of the brain and non-brain forms of LCa and LCb.

Amino Acid Sequence↗
PubMed1980

A method for the measurement of light transmission using a photometer provided with a measuring and a reference photocell along with a bifurcated fiber optic light guide.

A method for the measurement of light transmission is described. It makes use of an illuminator, a photometer to which a measuring and a reference photocell are connected, a bifurcated light guide and four special holders, two for the photocells and two for the branches of the light guide. The reference photocell gives the values of the first intensity while the measuring photocell, covered by the sample to be examined, gives the values of the second intensity. By just switching from one photocell to the other, without moving the sample it is possible to verify the values of both the first and the second intensity and consequently insure more precise measurements.

Fiber Optic Technology↗
PubMed1978

[Pupil and light sense perimetry with light and dark adaptation (author's transl)].

In comparison to light sense perimetry the use of pupillomotoric thresholds determination in the central region of the retina at various visual field illumination (10 asb, 0,1 asb, 0,001 asb, 45 degrees Meridian, 27' testpoint) has yielded the following results: 1. The maximum of the pupillomotoric sensitivity profile lies independant of the state of adaptation in the fovea. 2. Irrespective of adaptation state the course of the pupillographic profile curves are congruent. 3. Sensoric determinations show a slow flattening of the curves to the periphery whereas comparatively pupillographic determination yields a steep course (difference in areal summation). 4. In total the pupillomotoric sensitivity increases only about 10 db during the change of adaptation from light to dark. --As the phasic pupillo-light-reflex is elicited by rods and cones the differences between the sensoric and pupillomotoric threshold determinations must arise from intraretinal neuronal processes and not from the receptor reactions.

Adult↗
PubMed2000

Regulation of LPA-promoted myofibroblast contraction: role of Rho, myosin light chain kinase, and myosin light chain phosphatase.

Myofibroblasts generate the contractile force responsible for wound healing and pathological tissue contracture. In this paper the stress-relaxed collagen lattice model was used to study lysophosphatidic acid (LPA)-promoted myofibroblast contraction and the role of the small GTPase Rho and its downstream targets Rho kinase and myosin light chain phosphatase (MLCPPase) in regulating myofibroblast contraction. In addition, the regulation of myofibroblast contraction was compared with that of smooth muscle cells. LPA-promoted myofibroblast contraction was inhibited by the myosin light chain kinase (MLCK) inhibitors KT5926 and ML-7; however, in contrast to that observed in smooth muscle cells, elevation of intracellular calcium alone was not sufficient to promote myofibroblast contraction. These results suggest that Ca(2+)-mediated activation of MLCK, while necessary, is not sufficient to promote myofibroblast contraction. The specific Rho inactivator C3-transferase and the Rho kinase inhibitor Y-27632 inhibited LPA-promoted myofibroblast contraction, suggesting that contraction depends on activation of the Rho/Rho kinase pathway. Calyculin, a type 1 phosphatase inhibitor known to inhibit MLCPPase, could promote myofibroblast contraction in the absence of LPA, as well as restore contraction in the presence of C3-transferase or Y-27632. Together these results support a model whereby Rho/Rho kinase-mediated inhibition of MLCPPase is necessary for LPA-promoted myofibroblast contraction, in contrast to smooth muscle cells in which Ca(2+) activation of MLCK alone is sufficient to promote contraction.

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗
PubMed2000

Light-dependent magnetoreception in birds: the effect of intensity of 565-nm green light.

In a previous study, Australian silvereyes tested in autumn under monochromatic 565-nm green light at intensities of 2.1 and 7.5 mW m-2 preferred their normal northerly migratory direction, whereas they showed a significantly different tendency towards northwest at 15.0 mW m-2. Repeating these experiments in spring with silvereyes migrating southward, we again observed well-oriented tendencies in the migratory direction at 2.1 and 7.5 mW m-2. At 15.0 mW m-2, however, the birds once more preferred northwesterly directions, i.e. their response under this condition proved to be independent of the migratory direction. This contradicts the interpretation that monochromatic green light of this high intensity leads to a rotation of compass information; instead, it appears to produce sensory input that causes birds to give up their migratory direction in favor of a fixed direction of as yet unknown origin.

Animals↗
PubMed2003

Myosin light chain kinase stimulates smooth muscle myosin ATPase activity by binding to the myosin heads without phosphorylating the myosin light chain.

Myosin light chain kinase (MLCK) is a multifunctional regulatory protein of smooth muscle contraction [IUBMB Life 51 (2001) 337, for review]. The well-established mode for its regulation is to phosphorylate the 20 kDa myosin light chain (MLC 20) to activate myosin ATPase activity. MLCK exhibits myosin-binding activity in addition to this kinase activity. The myosin-binding activity also stimulates myosin ATPase activity without phosphorylating MLC 20 [Proc. Natl. Acad. Sci. USA 96 (1999) 6666]. We engineered an MLCK fragment containing the myosin-binding domain but devoid of a catalytic domain to explore how myosin is stimulated by this non-kinase pathway. The recombinant fragment thus obtained stimulated myosin ATPase activity by V(max)=5.53+/-0.63-fold with K(m)=4.22+/-0.58 microM (n=4). Similar stimulation figures were obtained by measuring the ATPase activity of HMM and S1. Binding of the fragment to both HMM and S1 was also verified, indicating that the fragment exerts stimulation through the myosin heads. Since S1 is in an active form regardless of the phosphorylated state of MLC 20, we conclude that the non-kinase stimulation is independent of the phosphorylating mode for activation of myosin.

Binding Sites↗
PubMed2003

Differential signalling by muscarinic receptors in smooth muscle: m2-mediated inactivation of myosin light chain kinase via Gi3, Cdc42/Rac1 and p21-activated kinase 1 pathway, and m3-mediated MLC20 (20 kDa regulatory light chain of myosin II) phosphorylation via Rho-associated kinase/myosin phosphatase targeting subunit 1 and protein kinase C/CPI-17 pathway.

Signalling via m3 and m2 receptors in smooth muscles involved activation of two G-protein-dependent pathways by each receptor. m2 receptors were coupled via Gbetagammai3 with activation of phospholipase C-beta3, phosphoinositide 3-kinase and Cdc42/Rac1 (where Cdc stands for cell division cycle) and p21-activated kinase 1 (PAK1), resulting in phosphorylation and inactivation of myosin light chain kinase (MLCK). Each step was inhibited by methoctramine and pertussis toxin. PAK1 activity was abolished in cells expressing both Cdc42-DN (where DN stands for dominant negative) and Rac1-DN. MLCK phosphorylation was inhibited by PAK1 antibody, and in cells expressing Cdc42-DN and Rac1-DN. m3 receptors were coupled via Galpha(q/11) with activation of phospholipase C-beta1 and via RhoA with activation of Rho-associated kinase (Rho kinase), phospholipase D and protein kinase C (PKC). Rho kinase and phospholipase D activities were inhibited by C3 exoenzyme and in cells expressing RhoA-DN. PKC activity was inhibited by bisindolylmaleimide, and in cells expressing RhoA-DN; PKC activity was also inhibited partly by Y27632 (44+/-5%). PKC-induced phosphorylation of PKC-activated 17 kDa inhibitor protein of type 1 phosphatase (CPI-17) at Thr38 was abolished by bisindolylmaleimide and inhibited partly by Y27632 (28+/-3%). Rho-kinase-induced phosphorylation of myosin phosphatase targeting subunit (MYPT1) and was abolished by Y27632. Sustained phosphorylation of 20 kDa regulatory light chain of myosin II (MLC20) and contraction were abolished by bisindolylmaleimide Y27632 and C3 exoenzyme and in cells expressing RhoA-DN. The results suggest that Rho-kinase-dependent phosphorylation of MYPT1 and PKC-dependent phosphorylation and enhancement of CPI-17 binding to the catalytic subunit of MLC phosphatase (MLCP) act co-operatively to inhibit MLCP activity, leading to sustained stimulation of MLC20 phosphorylation and contraction. Because Y27632 inhibited both Rho kinase and PKC activities, it could not be used to ascertain the contribution of MYPT1 to inhibition of MLCP activity. m2-dependent phosphorylation and inactivation of MLCK precluded its involvement in sustained MLC20 phosphorylation and contraction.

Animals↗
PubMed2005

AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence.

Degradation of the most abundant membrane protein on earth, the light-harvesting complex of Photosystem II (LHC II), is highly regulated under various environmental conditions, e.g., light stress, to prevent photochemical damage to the reaction center. We identified the LHC II degrading protease in Arabidopsis thaliana as a Zn(2+)-dependent metalloprotease, activated by the removal of unknown extrinsic factors, similar to the proteolytic activity directed against Lhcb3 in barley. By using a reversed genetic approach, the chloroplast-targeted protease FtsH6 was identified as being responsible for the degradation. T-DNA KO A. thaliana mutants, lacking ftsH6, were unable to degrade either Lhcb3 during dark-induced senescence or Lhcb1 and Lhcb3 during highlight acclimation. The A. thaliana ftsH6 gene has a clear orthologue in the genome of Populus trichocarpa. It is likely that FtsH6 is a general LHC II protease and that FtsH6-dependent LHC II proteolysis is a feature of all higher plants.

Acclimatization↗
PubMed1999

Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain.

Myosin light-chain kinase (MLCK) of smooth muscle is multifunctional, being composed of N-terminal actin-binding domain, central kinase domain, and C-terminal myosin-binding domain. The kinase domain is the best characterized; this domain activates the interaction of smooth-muscle myosin with actin by phosphorylating the myosin light chain. We have recently shown that the Met-1-Pro-41 sequence of MLCK binds to actin to inhibit this interaction. However, it is not known whether the myosin-binding domain modifies the actin-myosin interaction. We designed MLCK.cDNA to overexpress the Asp-777-Glu-972 sequence in Escherichia coli. The purified Asp-777-Glu-972 fragment, although devoid of the kinase activity, exerted a stimulatory effect on the ATPase activity of dephosphorylated myosin (Vmax = 7.36 +/- 0.44-fold, Km = 1.06 +/- 0. 20 microM, n = 4). When the N-terminal 39 residues of the fragment were deleted from the fragment, the resultant fragment, Met-816-Glu-972, lost the stimulatory activity. We synthesized the Ala-777-Ser-815 peptide that was deleted from the fragment and confirmed its stimulatory effect of the peptide (Vmax = 3.03 +/- 0. 22-fold, Km = 6.93 +/- 1.61 microM, n = 3). When this peptide was further divided into Asp-777-Met-795 and Ala-796-Ser-815 peptides, the stimulatory activity was found in the latter. We confirmed that the myosin phosphorylation did not occur during the experiments with the above fragments and peptides. Therefore, we suggest that phosphorylation is not obligatory for smooth-muscle myosin not to be active.

Animals↗
PubMed1999

Role of the N-terminal region of the regulatory light chain in the dephosphorylation of myosin by myosin light chain phosphatase.

Myosin regulatory light chain (RLC) is phosphorylated at various sites at its N-terminal region, and heterotrimeric myosin light chain phosphatase (MLCP) has been assigned as a physiological phosphatase that dephosphorylates myosin in vivo. Specificity of MLCP toward the various phosphorylation sites of RLC was studied, as well as the role of the N-terminal region of RLC in the dephosphorylation of myosin by MLCP. MLCP dephosphorylated phosphoserine 19, phosphothreonine 18, and phosphothreonine 9 efficiently with almost identical rates, whereas it failed to dephosphorylate phosphorylated serine 1/serine 2. Deletion of the N-terminal seven amino acid residues of RLC markedly decreased the dephosphorylation rate of phosphoserine 19 of RLC incorporated in the myosin molecule, whereas this deletion did not significantly affect the dephosphorylation rate of isolated RLC. On the other hand, deletion of only four N-terminal amino acid residues showed no effect on dephosphorylation of phosphoserine 19 of incorporated RLC. The inhibition of dephosphorylation by deletion of the seven N-terminal residues was also found with the catalytic subunit of MLCP. Phosphorylation at serine 1/serine 2 and threonine 9 did not influence the dephosphorylation rate of serine 19 and threonine 18 by MLCP. These results suggest that the N-terminal region of RLC plays an important role in substrate recognition of MLCP.

Amino Acid Sequence↗
PubMed2005

Light curing time reduction: in vitro evaluation of new intensive light-emitting diode curing units.

The aim of the present in vitro study was to establish the minimum necessary curing time to bond stainless steel brackets (Mini Diamond Twin) using new, intensive, light-emitting diode (LED) curing units. Seventy-five bovine primary incisors were divided into five equal groups. A standard light curing adhesive (Transbond XT) was used to bond the stainless steel brackets using different lamps and curing times. Two groups were bonded using an intensive LED curing lamp (Ortholux LED) for 5 and 10 seconds. Two more groups were bonded using another intensive LED curing device (Ultra-Lume LED 5) also for 5 and 10 seconds. Finally, a high-output halogen lamp (Optilux 501) was used for 40 seconds to bond the final group, which served as a positive control. All teeth were fixed in hard acrylic and stored for 24 hours in water at 37 degrees C. Shear bond strength (SBS) was measured using an Instron testing machine. Weibull distribution and analysis of variance were used to test for significant differences. The SBS values obtained were significantly different between groups (P < 0.001). When used for 10 seconds, the intensive LED curing units achieved sufficient SBS, comparable with the control. In contrast, 5 seconds resulted in significantly lower SBS. The adhesive remnant index (ARI) was not significantly affected.A curing time of 10 seconds was found to be sufficient to bond metallic brackets to incisors using intensive LED curing units. These new, comparatively inexpensive, curing lamps seem to be an advantageous alternative to conventional halogen lamps for bonding orthodontic brackets.

Animals↗
PubMed2005

Temperature and Light modulate the trans-delta3-hexadecenoic acid content of phosphatidylglycerol: light-harvesting complex II organization and non-photochemical quenching.

The interaction of light and temperature in the modulation of the trans-delta3-hexadecenoic acid (trans-16:1) content of phosphatidylglycerol (PG) in winter rye (Secale cereale L.) was assessed and related to the organization of light-harvesting complex II (LHCII). Increasing the growth irradiance from 50 to 800 micromol m(-2) s(-1) at 20 degrees C resulted in a 1.8-fold increase in the trans-16:1 content in PG which favoured a greater preponderance of oligomeric LHCII, measured in vitro as the ratio of oligomer : monomer. Similar irradiance-dependent increases were observed during growth at 5 degrees C; however, 1.4-fold lower trans-16:1 contents and lower LHCII oligomer : monomer ratios were observed compared with growth at 20 degrees C and the same irradiance. These trends were also observed under natural field conditions. Thus, the accumulation of trans-16:1, as well as the organization of LHCII are modulated by both growth irradiance and growth temperature in an independent but additive manner. We also examined how changes in the supramolecular organization of LHCII affected the capacity for non-photochemical quenching (q(N)) and photoprotection via antenna quenching (q(O)). While q(O) was positively correlated with q(N), there was no correlation with either LHCII organization or xanthophyll cycle activity under the steady-state growth conditions examined.

Light↗
PubMed1995

Light-harvesting chlorophyll a/b-binding protein inserted into isolated thylakoids binds pigments and is assembled into trimeric light-harvesting complex.

The light-harvesting chlorophyll a/b-binding protein (LHCP) is largely protected against protease (except for about 1 kD on the N terminus) in the thylakoid membrane; this protease resistance is often used to assay successful insertion of LHCP into isolated thylakoids in vitro. In this paper we show that this protease resistance is exhibited by trimeric light-harvesting complex of photosystem II (LHCII) but not by monomeric LHCII in which about 5 kD on the N terminus of LHCP are cleaved off by protease. When a mutant version of LHCP that is unable to trimerize in an in vitro reconstitution assay is inserted into isolated thylakoids, it gives rise to only the shorter protease digestion product indicative of monomeric LHCII. We conclude that more of the N-terminal domain of LHCP is shielded in trimeric than in monomeric LHCII and that this difference in protease sensitivity can be used to distinguish between LHCP assembled in LHCII monomers or trimers. The data presented prove that upon insertion of LHCP into isolated thylakoids at least part of the protein spontaneously binds pigments to form LHCII, which then is assembled in trimers. The dependence of the protease sensitivity of thylakoid-inserted LHCP on the oligomerization state of the newly formed LHCII justifies caution when using a protease assay to verify successful insertion of LHCP into the membrane.

Amino Acid Sequence↗
PubMed1962

Self-regulated exposure to light by dark-or light-treated rats.

Rats allowed to expose themselves to light do so for a rather constant length of time each day. This duration of exposure depends upon both the brightness of the light used for testing and the illumination in which the rats were maintained before testing.

Animals↗
PubMed2000

Myosin light chain kinase transference induces myosin light chain activation and endothelial hyperpermeability.

The actomyosin complex is the major cytoskeletal component that controls cell contraction. In this study, we investigated the effects of actomyosin interaction on endothelial barrier function and gap formation. Activated myosin light chain kinase (MLCK) protein was transferred into coronary venular endothelial cell (CVEC) monolayers. Uptake of the activated protein resulted in a significant shift in myosin light chain (MLC) from an unphosphorylated to a diphosphorylated form. In addition, MLCK induced a hyperpermeability response of the monolayer as measured by albumin transendothelial flux. Microscopic examination of MLCK-treated CVECs revealed widespread gap formation in the monolayer, loss of peripheral beta-catenin, and increases in actin stress fibers. Inhibition of all of the above responses by a specific MLCK inhibitor suggests they are the direct result of exogenously added MLCK. These data suggest that activation of MLCK in CVECs causes phosphorylation of MLC and contraction of CVECs, resulting in gap formation and concomitant increases in permeability. This study uses a novel technique to measure the effects of an activated kinase on both its substrate and cellular morphology and function through direct transference into endothelial cells.

Actins↗
PubMed1978

Induction of persistent estrus by constant light: effects of neonatal constant light and Harderian gland function.

The effect of constant light on the age at onset of persistent estrus was compared in rats exposed to constant light since birth (LL-0) and those exposed beginning at 70 days of age (LL-70). Persistent estrus occurred about 27 days later in the LL-0 rats than in the LL-70 rats. Exposure to LL for just the 1st 15 days of life (LL-0-15) and then subsequent exposure to LL at 71 days also delayed the induction of persistent estrus. Neonatal injection of a Harderian gland (HG) homogenate to LL-0-15 rats reduced the age of vaginal opening and 1st estrus and reduced the delayed onset of persistent estrus caused by the neonatal LL. Harderianectomy of LL-0 or hematoporphyrin injections in LL-0-15 rats had no effect on the onset of LL-induced persistent estrus.

Animals↗