[Clinical analysis of pharynx and larynx mycosis infection defective diagnosis].
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Adult↗
Biomedical subjects
Yanqiu Liu
Publications and source records attributed to Yanqiu Liu.
Matrix-specific activation of Src and Rho initiates capillary morphogenesis of endothelial cells.
Interstitial collagen I stimulates microvascular endothelial cells to form solid cords that imitate precapillary structures found during angiogenesis. Time-lapse microscopy identified cell retraction and disruption of cell-cell contacts as early critical steps in collagen I-induced capillary morphogenesis. These early stages paralleled collagen I activation of Src kinase and GTPase Rho through beta1 integrins. The Src inhibitor PP2, dominant-negative Src, and Rho inhibitor exoenzyme C3 transferase each inhibited collagen I induction of actin stress fibers that mediate cell retraction and each inhibited capillary morphogenesis. Collagen I also disrupted VE-cadherin from intercellular junctions through a Src-dependent mechanism; both the Src inhibitor PP2 and dominant-negative Src preserved VE-cadherin localization to regions of cell-cell contact. An active Src mutant disrupted VE-cadherin and cell-cell contacts similarly to collagen I. In sharp contrast, laminin-1 did not induce capillary morphogenesis, and laminin-1 did not induce activation of Src or Rho. Rather, laminin-1 induced persistent activation of the GTPase Rac. Thus, these studies identify activation of Src and Rho as key mechanisms by which collagen I provokes capillary morphogenesis of microvascular endothelial cells, and they define marked differences between the functions of collagen I and laminin-1 in regulating endothelial cell morphogenesis.
ADP Ribose Transferases↗
[Effects of soil temperature and moisture on soil respiration in different forest types in Changbai Mountain].
The effects of soil temperature (0, 5, 15, 25, 35 degrees C) and water content on soil respiration in three forest types in Changbai Mountain were evaluated in laboratory condition. The results indicated that the soil respiration rate was positively correlated to soil temperature from 0 to 35 degrees C and it increased with soil water content from 0.21 to 0.37 kg.kg-1. The soil respiration rate decreased with soil water content when water content was over the range. The result suggested the interactive effects of temperature and water content on soil respiration. There were significant differences in soil respiration among the various forest types and the highest was in broad leaf Korean pine forest, then in erman's birch forest, and it was the lowest in dark coniferous forest. The optimal condition for soil respiration in broad-leaved Korean pine forest was at 35 degrees C under 0.37 kg.kg-1 water content, and it was at 25 degrees C under 0.21 kg.kg-1 in dark coniferous forest and at 35 degrees C under 0.37 kg.kg-1 water content in erman's birch forest. Because the forests of broad leaf Korean pine, dark coniferous and erman's birch are located at various altitudes, the soil temperatures had 4-5 degrees C variation in different forest types during the same period. The soil respiration rates measured in brown pine mountain soil were lower than those in dark brown forest and they were higher in mountain grass forest soil than those in brown pine mountain soil.
Carbon Dioxide↗
Activated SRC oncogene phosphorylates R-ras and suppresses integrin activity.
One of the prominent effects of the Src kinase is to reduce cell adhesion. The small GTPase, R-Ras, affects cell adhesion by maintaining integrin activity, and the ability of R-Ras to do so can be regulated by phosphorylation of a tyrosine residue located in its effector domain by an Eph receptor kinase (Zou, J. X., Wang, B., Kalo, M. S., Zisch, A. H., Pasquale, E. B., and Ruoslahti, E. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13813-13818). Here we show that Src regulates cell adhesion through R-Ras and integrins. Reduced substrate attachment of 293T cells transfected with the cDNA for an activated form of Src (v-Src) was accompanied by phosphorylation of endogenous R-Ras. v-Src also phosphorylated R-Ras in vitro. An activated form of Src similar to one that has been found in human cancers, Src527, shared with v-Src the ability to phosphorylate R-Ras. Stronger R-Ras phosphorylation was seen in Madin-Darby canine kidney cells cells transformed with temperature-sensitive v-Src at the permissive temperature than at the non-permissive temperature, and R-Ras and Src co-immunoprecipitated at the permissive temperature. Mutation analysis showed that the Src phosphorylation site in R-Ras was tyrosine 66, the position critical to the ability of R-Ras to support integrin activity. Finally, activated R-Ras in which tyrosine 66 is mutated to phenylalanine rendered cells partially resistant to the effects of Src on cell adhesion. Regulation of cell adhesion by Src through R-Ras may be at least partially responsible for the reduced adhesion and the resulting increased invasiveness of Src-transformed cells.
Animals↗