RELATION OF BODY MASS INDEX WITH IgE LEVELS, ALLERGIC SENSITIZATION AND LUNG FUNCTION IN ASTHMATIC CHILDREN: OUR EXPERIENCE AND REVISION OF LITERATURE.

In recent decades, there has been an increase in the prevalence of asthma and obesity in pediatric age. In this regard several studies have provided controversial data to demonstrate the link between Body Mass Index (BMI) and asthma, both in adults and in children. In this prospective study we evaluated the relationship between body mass index value, total IgE immunoglobulin E levels, skin prick test (SPT) sensitization and lung function in children affected by asthma.

EXHALED BREATH TEMPERATURE IN ASTHMATIC CHILDREN.

Asthma is characterized by chronic inflammation of airways. Currently, no traditional method allows an easy daily evaluation of the degree of airway inflammation. Measuring inflammatory biomarkers in the breath is a very attractive approach to monitor asthma inflammation.

Growth hormone receptors in hypothalamic and extra-hypothalamic tissues.

Central GH receptors (GHR) have been identified in hypothalamic and extra-hypothalamic tissues of rabbit and chicken brains. Plasma membranes of the rabbit brain demonstrated specific saturable high-affinity, low-capacity binding sites for 125I-labelled GH. RNA extracted from hypothalamic and extra-hypothalamic tissues of rabbit and chicken brains contained mRNA that hybridized with a cDNA probe for the rabbit liver GHR.

Homologous and heterologous regulation of somatostatin-binding sites on chicken adenohypophysial membranes.

Binding of 125I-labelled [Tyr1]-somatostatin (125I-[Tyr1]-SRIF) to pituitary caudal lobe membranes was suppressed in immature chickens 1 and 2 h after i.v. administration of unlabelled SRIF at concentrations of 1-100 micrograms/kg.

Somatostatin binding to chicken adenohypophysial membranes.

[125I-Tyr1]-Somatostatin (SRIF)-binding sites were demonstrated on crude plasma membrane preparations from chicken pituitary glands. These binding sites were saturable and of high affinity (dissociation constant less than 1.0 nM) and low capacity (maximal binding capacity less than 200 fmol/mg protein) and were specific for SRIF moieties.