Dr. Liliana  Hernandez  Dds image

Dr. Liliana Hernandez Dds

860 W. Valley Pkwy Ste. 100
Escondido CA 92025
760 332-2266
Medical School: Other - Unknown
Accepts Medicare: No
Participates In eRX: No
Participates In PQRS: No
Participates In EHR: No
License #: 44891
NPI: 1124111885
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Serum and glucocorticoid-regulated kinase 1 promotes vascular smooth muscle cell proliferation via regulation of β-catenin dynamics. - Cellular signalling
In response to arterial intimal injury vascular smooth muscle cells (VSMCs) within the vessel wall proliferate upon exposure to growth factors, accumulate, and form a neointima that can occlude the vessel lumen. Serum and glucocorticoid inducible kinase 1 (SGK1) is a growth factor-responsive kinase; however its role in VSMC proliferation is not fully understood. Here, we examined growth factor-dependent regulation of SGK1 and defined a molecular role for SGK1 in stimulation of VSMC proliferation. We found that stimulation of VSMCs with the pro-proliferative growth factor, platelet-derived growth factor BB (PDGF) significantly increased SGK1 mRNA, protein, and kinase activity in aortic VSMCs in vitro. To test the hypothesis that activation of SGK1 activity promotes VSMC proliferation, we examined the effects of stable expression of constitutively active (S422D) and kinase-defective (S422A) mutants of SGK1 on VSMC growth. We found that activation of SGK1 increased, whereas interference of SGK1 signaling inhibited VSMC growth in vitro. Consistent with these findings, expression of the S422D mutant augmented both basal and PDGF-induced BrdU uptake in VSMCs. Conversely, PDGF-induced BrdU uptake was attenuated in VSMCs expressing S422A. Furthermore, we determined that activated SGK1 enhanced basal and PDGF-dependent G1→S cell cycle transition, whereas dominant-negative SGK1 abrogated G1→S cell cycle transition under similar conditions. Downstream signaling by active SGK1 induced basal and PDGF-induced phosphorylation of glycogen synthase kinase 3β, an effect which was attenuated when SGK1 activity was blocked by expression of the kinase-defective mutant, S422A. We also found that transfection of S422D enhanced β-catenin-nuclear localization and activation of the TOP/Flash and cyclin D1 transcriptional reporters. These effects were significantly blunted in VSMCs transfected with the S422A mutant. Our results provide compelling evidence of a role for SGK1 in stimulation of arterial VSMC growth via regulation of β-catenin dynamics and implicate SGK1 in the progression of intimal narrowing following arterial injury. Hence, the findings presented here point to inhibition of SGK1 activity as a novel therapeutic approach for the treatment of occlusive vascular diseases.Copyright © 2014 Elsevier Inc. All rights reserved.
Ethanol reforming on Co(0001) surfaces: a density functional theory study. - The journal of physical chemistry. A
A computational study using density functional theory is carried out to investigate the reaction mechanism of ethanol steam reforming on Co(0001) surfaces. The adsorption properties of the reactant, possible intermediates, and products are carefully examined. The reaction pathway and related transition states are also analyzed. According to our calculations, the reforming mechanism primarily consisting of dehydrogenation steps of ethanol, ethoxy, methanol, methoxy, and formic acid, is feasible on Co(0001) surfaces. It is also found that the reaction of formaldehyde yielding formic acid and hydrogen may not be an elementary reaction. The dehydrogenation of ethoxy possesses the highest barrier and is accordingly identified as the rate-determining step.
Purification of human prostatic-specific antigen (hPSA) from seminal plasma by immunoaffinity chromatography using a monoclonal antibody anti total PSA. - Hybridoma (2005)
Human prostate-specific antigen (hPSA) is found in serum and semen in a variety of forms, is form-free and complex, and has clinical importance to prostate cancer diagnosis. Here, a simple procedure is described for the efficient purification of hPSA from seminal plasma. The semen was clarified by centrifugation, and the isolation of PSA was carried out by immunoaffinity chromatography using the monoclonal antibody anti total PSA CB-PSA.4. The recuperation of PSA from seminal plasma by this procedure was 66.4%, and a purification factor of 65.8 was reached. The specificity activity obtained was 0.79 mg PSA/mg protein, and the preparation appeared homogeneous by SDS-PAGE and immunoelectrophoresis. A molecular weight of preparation was 30.46 kDa by SDS-PAGE, similar to the commercial PSA. These results indicate that immunoaffinity purification of PSA by means of this monoclonal antibody is a simple one-step procedure for the production of biologically active, highly purified human PSA.
Evaluation of the hydroxynitrile lyase activity in cell cultures of capulin (Prunus serotina). - Sheng wu gong cheng xue bao = Chinese journal of biotechnology
Enzymatic preparations obtained from young plants and cell cultures of capulin were screened for hydroxynitrile lyase activity. The three week old plants, grown under sterile conditions, were used to establish a solid cell culture. Crude preparations obtained from this plant material were evaluated for the transformation of benzaldehyde to the corresponding cyanohydrin (mandelonitrile). The results show that the crude material from roots, stalks, and leaves of young plants and calli of roots, stalks, internodes and petioles biocatalyzed the addition of hydrogen cyanide (HCN) to benzaldehyde with a modest to excellent enantioselectivity.
Monoclonal antibody against human trypsin: production, characterization, and use for diagnosis. - Hybridoma and hybridomics
A monoclonal antibody (MAb) directed against human immunoaffinity purified trypsinogen has been produced by hybridization of myeloma cells with spleen cells of BALB/c immunized mice. Antibodies were screened by ultramicro-enzyme-linked immunosorbent assay (UMELISA). The MAb was purified by affinity chromatography on protein A-sepharose, and MAb had a high affinity for trypsinogen with the affinity constant equal 2.06 x 10(9) L/mol. Specificity was studied by UMELISA using cross-reactant proteins; MAb gave a positive reaction with native trypsinogen-1 but did not react with the same protein after reduction. The antibody seem to be directed against conformational epitope. The MAb obtained was characterized immunologically and used to develop UMELISA for detection Trypsin. This monoclonal assay enabled the detection of 2.8 ng/mL.
Specific monoclonal antibody against human trypsin. - Hybridoma and hybridomics
A monoclonal antibody (MAb) directed against human trypsin-1 has been produced by hybridization of myeloma cells with spleen cells of BALB/c immunized mice. Antibodies were screened by ultramicro enzymelinked immunosorbent assay (UMELISA). MAb was purified by affinity chromatography on protein A-Sepharose, and MAb had a high affinity for trypsin-1 with the affinity constant equal 1.79 x 10(9) L/mol. Specificity was studied by UMELISA using cross-reactant proteins; MAb gave a positive reaction with native trypsinogen-1 and with the same protein after reduction. Antibody appeared to be directed against sequential epitope. One-step purification is described. The method evolved the adsorption of the enzyme onto a Sepharose-MAb(3H9) affinity column. The collected fraction was characterized and is available for immunization of BALB/c mice and for the preparation of a standard for immunoenzymatic assay.

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