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Black Lives Matter is a clarion call for racial equality and racial justice. With the arrival of Africans as slaves in 1619, a racial hierarchy was formed in the United States. However, slavery is commonly dismissed as that less than noble aspect of the United States' history without really confronting the legacies of racial inequality and racial injustice left in its wake. White supremacy, based on the myths of white superiority and Black inferiority, have obscured racial inequality and racial injustice, resulting in blaming the victims. Using Black Lives Matter as a platform, we focus on some key considerations for theory, research, education, training, and practice in clinical, community, and larger systems contexts. Broadly, we focus on Black Lives Matter, literally; Black dehumanization; historical oppression; healing; and implications for the field of family therapy. More specifically, we draw attention to health disparities, mass incarceration and aggressive policing, intergenerational racial trauma, restorative justice, and antiracist work.

El movimiento Black Lives Matter (Las vidas de los negros son importantes) es un llamamiento a la igualdad y la justicia racial. Con la llegada de los africanos como esclavos en el año 1619, se formó una jerarquía racial en los Estados Unidos. Sin embargo, la esclavitud generalmente se desestima como el aspecto menos noble de la historia de los Estados Unidos sin afrontar realmente los legados de desigualdad e injusticia raciales que dejó. La supremacía blanca, basada en los mitos de la superioridad blanca y la inferioridad negra, han ocultado la desigualdad y la injusticia raciales, lo cual condujo a la culpabilización de las víctimas. Utilizando el movimiento Black Lives Matter como plataforma, nos centramos en algunas consideraciones clave para la teoría, la investigación, la educación, la capacitación y la práctica en contextos clínicos, comunitarios y en sistemas más grandes. En líneas generales, nos centramos en Black Lives Matter, literalmente; en la deshumanización de los negros, la opresión histórica, la recuperación, y las consecuencias para el área de la terapia familiar. Más específicamente, visibilizamos las desigualdades sanitarias, el encarcelamiento masivo y la vigilancia policial agresiva, el trauma racial intergeneracional, la justicia reparadora y la labor antirracista.

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Previous research suggests that incarceration can have a negative effect on health. These health effects have an especially profound impact on HIV-positive individuals. As such, the current study investigates how incarceration affects the health of 12 African American HIV-positive formerly incarcerated males recruited via an AIDS Service Organization. Individuals were enrolled via purposive sampling and engaged in a series of in-depth interviews over a yearlong period (n=46). Participants ranged in age from 33 to 61 years. Most had finished high school, were not employed at time of first and last interview, and most were primarily residing at a homeless shelter. The time incarcerated ranged among participants from 3 months to 3 years. Findings suggest that health is impacted via limited and delayed access to medication, stigma, and poor quality of medical care while incarcerated. Health continues to worsen after release, largely due to incarceration's impact on individuals' social context. Macro-level policy limits opportunity to fulfill basic needs such as housing and hinders one's ability to be gainfully employed. Moreover, stigma, loss of social support, and a delay in accessing HIV-related services deleteriously impacts individuals' mental and physical health status. Implications for practice, policy and future research are also discussed.

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Our previous research characterized two phosphoenolpyruvate (PEP) carboxylase (PEPC) isoforms (PEPC1 and PEPC2) from developing castor oil seeds (COS). The association of a shared 107-kD subunit (p107) with an immunologically unrelated bacterial PEPC-type 64-kD polypeptide (p64) leads to marked physical and kinetic differences between the PEPC1 p107 homotetramer and PEPC2 p107/p64 heterooctamer. Here, we describe the production of antiphosphorylation site-specific antibodies to the conserved p107 N-terminal serine-6 phosphorylation site. Immunoblotting established that the serine-6 of p107 is phosphorylated in COS PEPC1 and PEPC2. This phosphorylation was reversed in vitro following incubation of clarified COS extracts or purified PEPC1 or PEPC2 with mammalian protein phosphatase type 2A and is not involved in a potential PEPC1 and PEPC2 interconversion. Similar to other plant PEPCs examined to date, p107 phosphorylation increased PEPC1 activity at pH 7.3 by decreasing its K(m)(PEP) and sensitivity to L-malate inhibition, while enhancing glucose-6-P activation. By contrast, p107 phosphorylation increased PEPC2's K(m)(PEP) and sensitivity to malate, glutamic acid, and aspartic acid inhibition. Phosphorylation of p107 was promoted during COS development (coincident with a >5-fold increase in the I(50) [malate] value for total PEPC activity in desalted extracts) but disappeared during COS desiccation. The p107 of stage VII COS became fully dephosphorylated in planta 48 h following excision of COS pods or following 72 h of dark treatment of intact plants. The in vivo phosphorylation status of p107 appears to be modulated by photosynthate recently translocated from source leaves into developing COS.

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Antibodies against Brassica napus cytosolic pyruvate kinase (PKc) (EC 2.7.1.40) were employed to examine PKc subunit composition and developmental profiles in castor and soybean seeds. A 56-kDa immunoreactive polypeptide was uniformly detected on immunoblots of clarified extracts from developing castor endosperm or soybean embryos. Maximal PKc activities occurred early in castor oil seed (COS) and soybean development (7.1 and 5.5 (micromol of pyruvate produced/min) g(-1) FW, respectively) and were up to 25-fold greater than those of fully mature seeds. Time-course studies revealed a close correlation between extractable PKc activity and the relative amount of the immunoreactive 56-kDa PKc polypeptide. PKc from developing COS was purified 1,874-fold to homogeneity and a final specific activity of 73.1 (micromol of pyruvate produced/min) mg(-1) protein. Gel filtration and SDS-PAGE indicated that this PKc exists as a 230-kDa homotetramer composed of 56-kDa subunits. The mass fingerprint of tryptic peptides of the 56-kDa COS PKc subunit best matched three putative PK(c)s from Arabidopsis thaliana. The purified enzyme was relatively heat-stable and displayed a broad pH optimum of 6.4. However, more efficient substrate utilization (in terms of Vmax /Km for phosphoenolpyruvate or ADP) was observed at pH 7.4. Glutamate was the most effective inhibitor, whereas aspartate functioned as an activator by partially relieving glutamate inhibition. Together with our previous studies, the results: (1) allow a model to be formulated regarding the coordinate allosteric control of PKc and phosphoenolpyruvate carboxylase by aspartate and glutamate in developing COS, and (2) provide further biochemical evidence that castor plant PKc exists as tissue-specific isozymes that exhibit substantial differences in their respective physical and regulatory properties.

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NADH kinase (NADHK; ATP:NADH 2'-phosphotransferase; EC 2.7.1.86), an enzyme that preferentially utilizes NADH as the diphosphonicotinamide nucleotide donor, has been identified for the first time in plants. Low activity (0.4 nmol of NADPH produced/min per mg of protein) was observed in clarified protein extracts from Arabidopsis thaliana (thale cress) cell suspension cultures. However, unlike an NADHK from yeast (Saccharomyces cerevisiae) (POS5), the enzyme from Arabidopsis did not associate with the mitochondria. NADHK was cloned (gi:30699338) from Arabidopsis and studied as a recombinant protein following affinity purification from Escherichia coli. The enzyme had a pH optimum for activity of 7.9 and a subunit molecular mass of 35 kDa. Analytical gel filtration demonstrated that the recombinant enzyme exists as a dimer. Hyperbolic saturation kinetics were observed for the binding of NADH, ATP, free Mg2+ and NAD+, with respective K(m) values of 0.042, 0.062, 1.16, and 2.39 mM. While NADHK could phosphorylate NADH or NAD+, the specificity constant (V(max)/K(m)) for NADH was 100-fold greater than for NAD+. The enzyme could utilize UTP, GTP and CTP as alternative nucleotides, although ATP was the preferred substrate. PP(i) or poly-P(i) could not substitute as phospho donors. PP(i) acted as a mixed inhibitor with respect to both NADH and ATP. NADHK was inactivated by thiol-modifying reagents, with inactivation being decreased in the presence of NADH or ATP, but not NAD+. This study suggests that, in Arabidopsis, NADP+/NADPH biosynthetic capacity could, under some circumstances, become uncoupled from the redox status of the diphosphonicotinamide nucleotide pool.

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This research is based on in-depth ethnographic interviews and focus groups with 88 African American family caregivers from various regions of the United States during a stressful time in their family development--caregiving at the end-of-life--and the grieving during the aftermath. The study employed a stratified purposeful sampling strategy. Subjects were African Americans from the Northern, Southern, and Midwestern United States. Formal care is complicated by the distrust that many African Americans hold toward the health care system, which has resulted from years of exclusion, racism and discrimination. The findings highlight the importance of hearing from African American families to gain an understanding of what services, including family therapy and other psychotherapy, they will need during this process.

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Recently, some family scholars have developed greater sensitivity to the relative neglect of families of color in clinical and empirical research. Consequently, a proliferation of research elucidating many nuances of ethnic families has come to the forefront, containing a wealth of knowledge with useful implications for family therapists and other mental health providers. The findings of these studies hold enormously important implications for how family therapists can better engage and accommodate families of color in therapy. In this article we discuss some of the etiological and methodological issues associated with planning, conducting, and disseminating family-based prevention and intervention research programs with ethnic minority families.

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NAD kinase (NADK; ATP:NAD 2'-phosphotransferase, EC 2.7.1.23), an enzyme found in both prokaryotes and eukaryotes, generates the important pyridine nucleotide NADP from substrates ATP and NAD. The role of NADKs in plants is poorly understood, and cDNAs encoding plant NADKs have not previously been described to our knowledge. We have cloned two cDNAs from Arabidopsis predicted to encode NADK isoforms, designated NADK1 and NADK2, respectively. Expressed as recombinant proteins in bacteria, both NADK1 and NADK2 were catalytically active, thereby confirming their identity as NADKs. Transcripts for both isoforms were detected in all tissues examined and throughout development. Although the predicted catalytic regions for NADK1 and NADK2 show sequence similarity to NADKs from other organisms, NADK2 possesses a large N-terminal extension that appears to be unique to plants. Using recombinant glutathione-S-transferase fusion proteins and calmodulin (CaM)-affinity chromatography, we delineated a Ca2+-dependent CaM-binding domain to a 45-residue region within the N-terminal extension of NADK2. Although recombinant NADK2 was not responsive to CaM in vitro, immunoblot analysis suggests that native NADK2 is a CaM-binding protein. In Arabidopsis crude extracts, CaM-dependent NADK activity was much greater than CaM-independent activity throughout development, particularly in young seedlings. A native CaM-dependent NADK was partially purified from Arabidopsis seedlings (Km NAD=0.20 mM, Km Mg2+ -ATP=0.17 mM). The enzyme was fully activated by conserved CaM (S0.5 = 2.2 nm) in the presence of calcium but displayed differential responsiveness to eight CaM-like Arabidopsis proteins. Possible roles for NADKs in plants are discussed in light of our observations.

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Pyrophosphate-dependent phosphofructokinase (PFP; EC 2.7.1.90) and two isoforms of ATP-dependent phosphofructokinase (PFK I and PFK II; EC 2.7.1.11) from ripened banana ( Musa cavendishii L. cv. Cavendish) fruits were resolved via hydrophobic interaction fast protein liquid chromatography (FPLC), and further purified using anion-exchange and gel filtration FPLC. PFP was purified 1,158-fold to a final specific activity of 13.9 micromol fructose 1,6-bisphosphate produced (mg protein)(-1) x min(-1). Gel filtration FPLC and immunoblot analyses indicated that this PFP exists as a 490-kDa heterooctomer composed of equal amounts of 66- (alpha) and 60-kDa (beta) subunits. PFP displayed hyperbolic saturation kinetics for fructose 6-phosphate (Fru 6-P), PPi, fructose 1,6-bisphosphate, and Pi ( K(m) values = 32, 9.7, 25, and 410 microM, respectively) in the presence of saturating (5 microM) fructose 2,6-bisphosphate, which elicited a 24-fold enhancement of glycolytic PFP activity ( K(a)=8 nM). PFK I and PFK II were each purified about 350-fold to final specific activities of 5.5-6.0 micromol fructose 1,6-bisphosphate produced (mg protein)(-1) x min(-1). Analytical gel filtration yielded respective native molecular masses of 210 and 160 kDa for PFK I and PFK II. Several properties of PFK I and PFK II were consistent with their respective designation as plastid and cytosolic PFK isozymes. PFK I and PFK II exhibited: (i) pH optima of 8.0 and 7.3, respectively; (ii) hyperbolic saturation kinetics for ATP ( K(m)=34 and 21 microM, respectively); and (iii) sigmoidal saturation kinetics for Fru 6-P ( S0.5=540 and 90 microM, respectively). Allosteric effects of phospho enolpyruvate (PEP) and Pi on the activities of PFP, PFK I, and PFK II were characterized. Increasing concentrations of PEP or Pi progressively disrupted fructose 2,6-bisphosphate binding by PFP. PEP potently inhibited PFK I and to a lesser extent PFK II ( I50=2.3 and 900 microM, respectively), while Pi activated PFK I by reducing its sensitivity to PEP inhibition. Our results are consistent with: (i) the respiratory climacteric being regulated by fine (allosteric) control of pre-existing enzymes; and (ii) primary and secondary glycolytic flux control being exerted at the levels of PEP and Fru 6-P metabolism, respectively.

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