188 research outputs found

    Shifting Identity: Process and Change in Identity of Aging Mexican-American Males

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    This article addresses the shift in machismo identity that occurs in Mexican-American male identity and the developmental process and the change in one\u27s role as an elderly Mexican-American man. Socialization of male-ism in Mexican-American boys begins with the cultural expectation that a young boy is and will be a man. There are also explicit expectations that girls should be respected but that, in contrast to boys, girls should be submissive and obedient. This is the beginning of machismo and the separation of being a man versus being a woman. Aging results in a loss of machismo and this is evident by the manner in which elderly males interact with their spouse and adult children. Towards the latter part of life, decision-making becomes a shared process between spouses. Quite often, Mexican-American elderly males are seen accompanying their spouse\u27s at flea markets, garage sales, grocery shopping and even assisting with baby sitting grandchildren

    Gary L. Villereal Photo Album

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    Vietnam War, 1961-1975 Branch of Service: Army Unit of Service: 1st Cavalry Division; II Field Forces Location of Service: Fort Bragg, North Carolina; Fort Sill, Oklahoma; III Corps, Vietnam; Phouc Vinh, Vietnam; Tan Son Nhut, Vietnam; Fire Support Base Buttons, Vietnam; Special Forces Camp Bu Dop, Vietnam; Song Be, Vietnam; Phuoc Luu, Vietnam; Duc Hue, Vietnam Highest Rank: Specialist Five Dates of Service: 1968-1970 Entrance into Service: Drafted Military Status: Veteranhttps://scholarworks.utrgv.edu/veterans/1024/thumbnail.jp

    Tetrapandins, a New Class of Scorpion Toxins That Specifically Inhibit Store-operated Calcium Entry in Human Embryonic Kidney-293 Cells

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    Venoms from 14 snakes and four scorpions were screened for inhibitory activities toward store-operated Ca2+ entry (SOCE) in human embryonic kidney-293 cells. An inhibitory activity was found in venom from the African scorpion Pandinus imperator. The active agent of this venom was purified by gel filtration and reverse-phase high pressure liquid chromatography methods. Sequence information on the purified fraction, by automatic Edman degradation and mass spectrometry analysis, identified the activity as being contained in two tetrapeptides, which we have named tetrapandins. We demonstrate that synthesized tetrapandins have inhibitory activity for SOCE in human embryonic kidney-293 cells while having no effect on either thapsigargin- or carbachol-stimulated release of Ca2+ stores. These toxins should be extremely useful in future studies to determine downstream events regulated by SOCE as well as to determine whether multiple pathways exist for thapsigargin-stimulated Ca2+ entry

    Audiovisual Alacrity: Managing Timely Access to Audiovisual Collections

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    Joint presentation given at the Society of American Archivists Conference on August 16, 2014; session 707

    TRPC6 channel translocation into phagosomal membrane augments phagosomal function

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    Defects in the innate immune system in the lung with attendant bacterial infections contribute to lung tissue damage, respiratory insufficiency, and ultimately death in the pathogenesis of cystic fibrosis (CF). Professional phagocytes, including alveolar macrophages (AMs), have specialized pathways that ensure efficient killing of pathogens in phagosomes. Phagosomal acidification facilitates the optimal functioning of degradative enzymes, ultimately contributing to bacterial killing. Generation of low organellar pH is primarily driven by the V-ATPases, proton pumps that use cytoplasmic ATP to load H(+) into the organelle. Critical to phagosomal acidification are various channels derived from the plasma membrane, including the anion channel cystic fibrosis transmembrane conductance regulator, which shunt the transmembrane potential generated by movement of protons. Here we show that the transient receptor potential canonical-6 (TRPC6) calcium-permeable channel in the AM also functions to shunt the transmembrane potential generated by proton pumping and is capable of restoring microbicidal function to compromised AMs in CF and enhancement of function in non-CF cells. TRPC6 channel activity is enhanced via translocation to the cell surface (and then ultimately to the phagosome during phagocytosis) in response to G-protein signaling activated by the small molecule (R)-roscovitine and its derivatives. These data show that enhancing vesicular insertion of the TRPC6 channel to the plasma membrane may represent a general mechanism for restoring phagosome activity in conditions, where it is lost or impaired.Fil: Riazanski, Vladimir. University of Chicago; Estados UnidosFil: Gabdoulkhakova, Aida G.. University of Chicago; Estados UnidosFil: Boynton, Lin S.. University of Chicago; Estados UnidosFil: Eguchi, Raphael R.. University of Chicago; Estados UnidosFil: Deriy, Ludmila V.. University of Chicago; Estados UnidosFil: Hogarth, D. Kyle. University of Chicago; Estados UnidosFil: Loaëc, Nadège. ManRos Therapeutics; FranciaFil: Oumata, Nassima. ManRos Therapeutics; FranciaFil: Galons, Hervé. Universite de Paris; FranciaFil: Brown, Mary E.. University of Chicago; Estados UnidosFil: Shevchenko, Pavel. University of Chicago; Estados UnidosFil: Gallan, Alexander J.. University of Chicago; Estados UnidosFil: Yoo, Sang Gune. University of Chicago; Estados UnidosFil: Naren, Anjaparavanda P.. Cincinnati Children’s Hospital Medical Center; Estados UnidosFil: Villereal, Mitchel L.. University of Chicago; Estados UnidosFil: Beacham, Daniel W.. Thermo Scientific; Estados UnidosFil: Bindokas, Vytautas P.. University of Chicago; Estados UnidosFil: Birnbaumer, Lutz. National Institute of Environmental Health Sciences; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Meijer, Laurent. ManRos Therapeutics; FranciaFil: Nelson, Deborah J.. University of Chicago; Estados Unido
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