RESUMEN
OBJECTIVE: Obstructive sleep apnea (OSA) can influence the appearance and proliferation of some tumors. The Sleep Apnea In Lung Cancer Screening (SAILS) study (NCT02764866) evaluated the prevalence of OSA and nocturnal hypoxemia in a high-risk population enrolled in a lung cancer screening program. METHODS: This was a prospective study of the prevalence of OSA in a lung cancer screening program. Subjects met the National Lung Screening Trial (NLST) age and smoking criteria (age 55-75 years; pack-years >30). Participants in the study were offered annual screening with low-dose computed tomography (LDCT) and pulmonary function testing, as well as home sleep apnea testing (HSAT) and a sleep-specific questionnaire. Sleep study-related variables, symptoms, and epidemiologic data were recorded. RESULTS: HSAT was offered to 279 subjects enrolled in our lung cancer screening program. HSAT results were available for 236 participants (mean age 63.6 years; mean tobacco exposure: 45 pack-years), of whom 59% were male and 53% were active smokers. Emphysema (74%) and chronic obstructive pulmonary disease (COPD) (62%) were common and in most cases mild in severity. OSA, including moderate to severe disease, was very common in this patient population. AHI distributions were as follows: AHI <5 (22.5%); 5-15 (36.4%); 15-30 (23.3%); and >30 (17.8%). Nocturnal hypoxemia (T90) (p = 0.003), diffusing capacity for carbon monoxide (DLCO) (p = 0.01), tobacco exposure (p = 0.024), and COPD (p = 0.023) were associated with OSA severity. Positive screening findings (nodules ≥6 mm) were associated with nocturnal hypoxemia on multivariate analysis adjusted for confounders (OR = 2.6, 95% CI = 1.12-6.09, p = 0.027). CONCLUSION: Moderate to severe OSA is very prevalent in patients enrolled in a lung cancer screening program. Nocturnal hypoxemia more than doubles the risk of positive screening findings.
Asunto(s)
Detección Precoz del Cáncer , Hipoxia/complicaciones , Neoplasias Pulmonares/diagnóstico por imagen , Síndromes de la Apnea del Sueño/complicaciones , Femenino , Humanos , Masculino , Persona de Mediana Edad , Polisomnografía/métodos , Prevalencia , Estudios Prospectivos , Índice de Severidad de la Enfermedad , Encuestas y CuestionariosRESUMEN
Galectins are a taxonomically widespread family of glycan-binding proteins, defined by at least one conserved carbohydrate-recognition domain with a canonical amino acid sequence and affinity for beta-galactosides. Because of their anti-adhesive as well as pro-adhesive extracellular functions, galectins appear to be a novel class of adhesion-modulating proteins collectively known as matricellular proteins (which include thrombospondin, SPARC, tenascin, hevin, and disintegrins). Accordingly, galectins can display de-adhesive effects when presented as soluble proteins to cells in a strong adhesive state. In this context, the de-adhesive properties of galectins should be considered as physiologically relevant as the proadhesive effects of these glycan-binding proteins. This article focuses on the roles of mammalian galectins in cell adhesion, spreading, and migration, and the crossregulation of these functions. Although careful attention should be paid when examining individual galectin functions due to overlapping distributions, these intriguing glycan-binding proteins offer promising possibilities for the treatment and intervention of a wide variety of pathological processes, including cancer, inflammation, and autoimmunity.
Asunto(s)
Movimiento Celular , Galectinas/metabolismo , Polisacáridos/metabolismo , Animales , Adhesión Celular , Supervivencia Celular , HumanosAsunto(s)
Glucosa , Insulina/metabolismo , Lectinas de Unión a Manosa/farmacología , Lectinas de Plantas/farmacología , Receptor de Insulina/metabolismo , Animales , Sitios de Unión , Brasil , Canavalia , Cinética , Masculino , Fosforilación , Subunidades de Proteína/efectos de los fármacos , Subunidades de Proteína/metabolismo , Ratas , Ratas Wistar , Receptor de Insulina/efectos de los fármacosRESUMEN
The specificity of the sialic acid-binding lectin from ovine placenta was examined in detail by haemagglutination inhibition assays applying a panel of 32 synthetic sialic acid analogues. The carboxylic acid group is a prerequisite for the interaction with the lectin, the alpha-anomer of the methyl glycoside is only a little more effective as an inhibitor than the beta-anomer and the most potent inhibitor was 9-deoxy-10-carboxylic acid Neu5Ac, followed by 4-oxo-Neu5Ac. In contrast to the majority of known sialic acid-binding lectins, the N-acetyl group of Neu5Ac is not indispensable for binding, neither is the hydroxyl group at C-9 since substitutions at this carbon atom are well tolerated. Furthermore, all sulfur-containing substituents at C-9 enhanced the affinity of the lectin. This is the first sialic acid-binding lectin found to strongly bind thio derivatives.