RESUMO
OBJECTIVES: The present study aimed at investigating the prevalence of prefrailty and frailty in South American older adults according to the setting and region. DESIGN: A literature search combining the terms "frailty", "South America" or a specific country name was performed on PubMed, EMBASE, Lilacs, and Scielo to retrieve articles published in English, Portuguese or Spanish on or before August 2019. PARTICIPANTS: Older adults aged 60+ years from any setting classified as frail according to a validated scale were included in the study. MEASUREMENTS: Frailty assessment by a validated scale. RESULTS: One-hundred eighteen reports (98 performed from Brazil, seven from Chile, five from Peru, four from Colombia, two from Ecuador, one from Argentina, and one from Venezuela) were included in the study. The mean prevalence of prefrailty in South America was 46.8% (50.7% in older in-patients, 47.6% in the community, and 29.8% in nursing-home residents). The mean prevalence of frailty in South America was 21.7% (55.8% in nursing-home residents, 39.1% in hospitalized older adults, and 23.0% in the community). CONCLUSIONS: Prefrailty and frailty are highly prevalent in South American older adults, with rates higher than those reported in Europe and Asia. In the community, almost one-in-two is prefrail and one-in-five is frail, while hospitalized persons and nursing-home residents are more frequently affected. These findings indicate the need for immediate attention to avoid frailty progression toward negative health outcomes. Our findings also highlight the need for specific guidelines for the management of frailty in South America.
Assuntos
Fragilidade/epidemiologia , Humanos , Estudos Observacionais como Assunto , Prevalência , América do Sul/epidemiologiaRESUMO
OBJECTIVES: Frailty is characterized by a functioning decline in multiple systems accompanied by an increase in individual's vulnerability to stressors. It appears to be higher in low and middle-income countries compared with high-income ones. This study aimed to evaluate the prevalence of frailty in non-institutionalized Brazilian older adults. DESIGN: a systematic review and meta-analysis study. SETTING: Cross-sectional and prospective data from Brazil. PARTICIPANTS: non-institutionalized adults aged 60 and older. METHODS: Electronic searches were performed in PubMed/MEDLINE, LILACS, SCOPUS and Web of Science, considering the studies published between March 2001 and July 2018, using a combination of the following terms and correlates: "elder" AND "frail" AND "prevalence" AND "Brazil". Two independent reviewers selected studies according to the inclusion criteria. Disagreements were resolved by a third reviewer (title/abstract) and by consensus. Studies with samples ≥221 subjects were considered for meta-analysis. RESULTS: 28 studies were included, while 18 had the data meta-analyzed. The majority of studies (61%) included older adults only from the Southeastern region. The number of subjects ranged from 53 to 5,532 individuals (N = 17,604) and the average age ranged from 65.6 to 85.5 years. The overall prevalence of frailty was 24%. When considering the different assessment methods, the prevalence was lower for frailty phenotype (16%) compared with other criteria (40%). Regarding sex, the prevalence of frailty was similar for women (28%) and men (25%). The prevalence of frailty was higher in older adults recruited from health care services (30%) compared to community ones (22%). CONCLUSION: In Brazil, the overall prevalence of frailty in non-institutionalized older adults is higher than observed from more developed countries. However, it may vary according to the assessment methods and settings.
Assuntos
Idoso Fragilizado/estatística & dados numéricos , Fragilidade/epidemiologia , Idoso , Idoso de 80 Anos ou mais , Brasil , Estudos Transversais , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Prevalência , Estudos ProspectivosRESUMO
Sarcopenia has an important impact in elderly. Recently the European Working Group on Sarcopenia in Older People (EWGSOP) defined sarcopenia as the loss of muscle mass plus low muscle strength or low physical performance. Lack of clinical sounding outcomes (ie external validity), is one of the flaws of this algorithm. The aim of our study was to determine the association of sarcopenia and mortality in a group of Mexican elderly. A total of 345 elderly were recruited in Mexico City, and followed up for three years. The EWGSOP algorithm was integrated by: gait speed, grip strength and calf circumference. Other covariates were assessed in order to test the independent association of sarcopenia with mortality. Of the 345 subjects, 53.3% were women; with a mean age of 78.5 (SD 7) years. During the three year follow-up a total of 43 (12.4%) subjects died. Age, cognition, ADL, IADL, health self-perception, ischemic heart disease and sarcopenia were associated in the bivariate analysis with survival. Negative predictive value for sarcopenia regarding mortality was of 90%. Kaplan-Meier curves along with their respective log-rank test were significant for sarcopenia. The components of the final Cox-regression multivariate model were age, ischemic heart disease, ADL and sarcopenia. Adjusted HR for age was 3.24 (CI 95% 1.55-6.78 p 0.002), IHD 5.07 (CI 95% 1.89-13.59 p 0.001), health self-perception 5.07 (CI 95% 1.9-13.6 p 0.001), ADL 0.75 (CI 95% 0.56-0.99 p 0.048) and sarcopenia 2.39 (CI 95% 1.05-5.43 p 0.037).
Assuntos
Sarcopenia/diagnóstico , Sarcopenia/mortalidade , Atividades Cotidianas , Idoso , Idoso de 80 Anos ou mais , Algoritmos , Antropometria , Cognição/fisiologia , Estudos de Coortes , Feminino , Seguimentos , Avaliação Geriátrica , Humanos , Estimativa de Kaplan-Meier , Masculino , México , Atividade Motora , Análise Multivariada , Força Muscular , Isquemia Miocárdica/complicações , Isquemia Miocárdica/mortalidade , Prevalência , Modelos de Riscos Proporcionais , Fatores de Risco , Sarcopenia/complicações , Autoimagem , Fatores SocioeconômicosRESUMO
El inmunoensayo para la Fosfatasa Alcalina (IEFA) detecta la presencia de anticuerpos antifosfatasa alcalina de la membrana de los vermes adultos de schistosoma mansoni. Su valor disgnóstico fue probado con 1514 sueros de personas de tres comunidades diferentes del área endémica del interior de Venezuela y 322 sueros de personas del área capitalina de Caracas, encontrandose una sensibilidad de 91,1 por ciento-96,8 por ciento con respecto a la Elisa (con antígenos de huevo). El IEFA fue 100 por cierto específico con sueros de sujetos residentes en localidades no endémicas. Esta metodología mostró menor 84 por cierto de concordancia (Prueba "kappa" de cohen) con "western blot" de antígenos de membrana del adulto y concordancia positiva con la PPCO (40, 6-77,1 por ciento) y la ELISA (51,4-69,1 por ciento) en las poblaciones endémicas estudiadas. Los resultados indican que IEFA es aplicable a la pesquisa epidemiológica de la esquistosomiasis mansoni en zonas endémicas y que la prueba es muy sensible para la detección de casos con baja carga parasitaria (au)
Assuntos
Humanos , Esquistossomose mansoni , Testes Imunológicos/métodosRESUMO
Quenched fluorescence peptides were used to investigate the substrate specificity requirements for recombinant wild-type angiotensin I-converting enzyme (ACE) and two full-length mutants bearing a single functional active site (N- or C-domain). We assayed two series of bradykinin-related peptides flanked by o-aminobenzoic acid (Abz) and N-(2,4-dinitrophenyl)ethylenediamine (EDDnp), namely, Abz-GFSPFXQ-EDDnp and Abz-GFSPFRX-EDDnp (X = natural amino acids), in which the fluorescence appeared when Abz/EDDnp are separated by substrate hydrolysis. Abz-GFSPFFQ-EDDnp was preferentially hydrolyzed by the C-domain while Abz-GFSPFQQ-EDDnp exhibits higher N-domain specificity. Internally quenched fluorescent analogues of N-acetyl-SDKP-OH were also synthesized and assayed. Abz-SDK(Dnp)P-OH, in which Abz and Dnp (2,4-dinitrophenyl) are the fluorescent donor-acceptor pair, was cleaved at the D-K(Dnp) bond with high specificity by the ACE N-domain (k(cat)/K(m) = 1.1 microM(-)(1) s(-)(1)) being practically resistant to hydrolysis by the C-domain. The importance of hydroxyl-containing amino acids at the P(2) position for N-domain specificity was shown by performing the kinetics of hydrolysis of Abz-TDK(Dnp)P-OH and Abz-YDK(Dnp)P-OH. The peptides Abz-YRK(Dnp)P-OH and Abz-FRK(Dnp)P-OH which were hydrolyzed by wild-type ACE with K(m) values of 5.1 and 4.0 microM and k(cat) values of 246 and 210 s(-)(1), respectively, have been shown to be excellent substrates for ACE. The differentiation of the catalytic specificity of the C- and N-domains of ACE seems to depend on very subtle variations on substrate-specific amino acids. The presence of a free C-terminal carboxyl group or an aromatic moiety at the same substrate position determines specific interactions with the ACE active site which is regulated by chloride and seems to distinguish the activities of both domains.
Assuntos
Peptidil Dipeptidase A/química , Peptidil Dipeptidase A/metabolismo , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Domínio Catalítico , Cloretos/farmacologia , Corantes Fluorescentes , Humanos , Concentração de Íons de Hidrogênio , Técnicas In Vitro , Cinética , Mutação , Oligopeptídeos/química , Peptidil Dipeptidase A/genética , Estrutura Terciária de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Especificidade por SubstratoRESUMO
We have determined the kinetic parameters for the hydrolysis by cathepsin B of peptidyl-coumarin amide and intramolecularly quenched fluorogenic peptides with the general structures epsilonNH2-Cap-Leu-X-MCA and Abz-Lys-Leu-X-Phe-Ser-Lys-Gln-EDDnp, respectively. Abz (orthoaminobenzoic acid) and EDDnp (2,4-dinitrophenyl-ethylenediamine) are the fluorescent donor-acceptor pair, and X was Cys(SBzl), Ser(OBzl), and Thr(OBzl) containing benzyl group (Bzl) at the functional side chain of Cys, Ser, and Thr. The peptidyl-coumarin-containing Cys(SBz1), Ser(OBzl), and Thr(OBzl) have higher affinity cathepsin B, supporting the interpretation of the crystal structure of rat cathepsin B complexed with the inhibitor Z-Arg-Ser(OBzl)-CH2Cl that the benzyl group attached to Ser hydroxyl side chain occupies the enzyme S'(1) subsite [Jia et al. (1995), J. Biol. Chem. 270, 5527]. A similar effect of benzyl group was also detected in the internally quenched peptides. Finally, the benzyl group in substrates containing Cys(SBzl) amino acid at P1 seems to compensate the absence of adequate S2-P2 interaction in the hydrolysis of the peptides having Pro or Ala at P2 position.