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Background: Thyroid ailments are frequently encountered endocrine disorders next to diabetes. They arise either due to functional aberrations of the thyroid gland resulting in over or under secretion of thyroid hormone or due to structural anomalies. People have varied constitutional, non-specific manifestations that cause abnormal metabolic functioning of the thyroid gland. Objectives: 1. To describe the socio-demographic characteristics of patients with thyroid disorders. 2. To analyze the clinical features, laboratory findings, and clinical outcomes of these patients. Methodology: This hospital-based descriptive study was conducted at the Government Wenlock Hospital in Mangalore. The study included patients admitted with thyroid disorders in the last 2 years. Data extraction sheet was developed from patient medical records. The sheet comprised three sections: socio-demographic information, clinical features at admission, and investigations and outcomes. Results: Most of the patients (52.8%) belonged to the 20-40 age group, followed by 30.5% in the 40-60 age group. Females comprised 81.5% of the study population, males -18.5%. 74.8% had swelling, 3.2% had facial puffiness. 1.8% had weight gain, only 1.2% had weight loss .16.3% had other comorbid conditions. 31.5% had low TSH levels 49.3% had normal TSH levels, 64.5 % - normal T3 levels, 63.2% - normal T4 levels. Anaemia was reported in 15.2% o, while 7.2% developed oedema. 34.2% had multinodular goitre, 20.2% - hypothyroidism 9.5 % - hyperthyroidism and 11.1% - malignancy. Out of the total 97% recovered 1% died 1% had discharge against medical advice and 1 % got discharged on request. Conclusion: Majority were females in the 20-40 age group. Majority of them had swelling followed by facial puffiness. Most of them had normal TSH, T3 and T4 levels, anaemia and oedema was also reported in few. Majority had multinodular goitre followed by hypothyroidism, malignancy, and hyperthyroidism. Majority had recovered.

Offers information on idiopathic portal hypertension (IPH) and noncirrhotic portal fibrosis (NCPF). Difference between IPH and NCPF; Etiology of the diseases; Pathological mechanisms involved in IPH and NCPF; Signs and symptoms of IPH and NCPF.

The present study shows that scanty hair distribution over the trunk is a specific finding in patients with alcoholic liver disease (ALD), and is not seen in alcoholic pancreatitis. This observation not only provides a useful clinical marker of individuals at increased risk of developing alcohol-related liver disease, but from the pathogenetic viewpoint, it suggests that at the tissue level, the male sex hormones protect the liver against ethanol-related damage.

We have previously established that the eleven cytosolic peptides phosphorylated in response to acute glucagon challenge in isolated rat hepatocytes undergo rapid dephosphorylation following transfer to medium free of 32PO4(3-). This dephosphorylation, far from being a simple process, is complex and asynchronous. This novel finding of asynchrony raises the question of whether, by analogy to glucagon, protein dephosphorylation is asynchronous during the recovery phase from acute challenge with noradrenaline, vasopressin or angiotensin II. One-dimensional SDS-PAGE of hepatocyte extracts indicates that noradrenaline stimulates the phosphorylation of ten cytosolic peptides, whereas vasopressin and angiotensin II stimulate the phosphorylation of six cytosolic peptides. Transfer of the hormone-challenged hepatocytes to medium devoid of 32PO4(3-) and hormone led to the rapid net dephosphorylation of the 32P-labelled phosphopeptides, albeit at different rates. In all instances, the most rapidly dephosphorylated phosphopeptide was glycogen phosphorylase. Statistical analysis indicates that during recovery from noradrenaline challenge three distinct groups of phosphopeptides can be delineated on the basis of their rates of dephosphorylation. Despite the fact that vasopressin and angiotensin II stimulate the phosphorylation of the same sub-set of phosphopeptides, there were differences in the rates of dephosphorylation of these phosphopeptides during the recovery phase from acute hormonal challenge.

Ethanol has profound acute effects on hepatic metabolism. While many of these effects are mediated via the redox imbalance that accompanies hepatic ethanol oxidation via the alcohol dehydrogenase (ADH) pathway, there is increasing evidence that ethanol also perturbs hepatic metabolism via its modulation of cyclic AMP-mediated signalling pathways. This paper examines the effects of ethanol on glucagon-stimulated protein phosphorylation using SDS-PAGE to analyse the 32P-labelling of cytosolic peptides in isolated rat hepatocytes pre-equilibrated with 32PO4(3-). We show that ethanol has biphasic effects on glucagon-stimulated protein phosphorylation. At a low concentration (50 mM), ethanol decreased the phosphorylation of certain peptides, whereas at higher concentrations (100-200 mM) it increased the 32P-labelling of all of the eleven glucagon-stimulated cytosolic peptides. The non-metabolizable alcohol 2-methylpyrazole-2-ol had no effects on glucagon-stimulated protein phosphorylation. The ADH inhibitor 4-methylpyrazole at 150 mM ethanol concentration abolished the potentiating effect of ethanol on the glucagon-stimulated phosphorylation of most peptides. In conclusion, the results indicate that ethanol alters glucagon-receptor-dependent protein phosphorylation in isolated hepatocytes via a complex mechanism that is partially dependent on ethanol oxidation via ADH.

The perivenous and periportal zones of the liver acinus differ in enzyme complements and capacities for gluconeogenesis, glycolysis and other metabolic processes. The biochemical factors governing this metabolic zonation are still poorly understood. Glucagon-mediated protein phosphorylation is an important factor in the regulation of hepatic metabolism. Here we show, by comparing the 32P-labelling pattern of isolated periportal and perivenous hepatocytes, that glucagon promotes the phosphorylation of zone-specific peptides as well as three common peptides (glycogen phosphorylase, glycogen synthase and pyruvate kinase) in the two cell types. We propose that the zone-specific phosphorylation of peptides is an important factor governing the shortterm zonation of metabolic processes in the liver.

One-dimensional SDS-PAGE of cytosolic phosphopeptides confirms that glucagon promotes the phosphorylation of 11 phosphopeptides in isolated rat hepatocytes pre-equilibrated with 32PO4(3-). Nine of these phosphopeptides are tentatively identified, whereas two phosphopeptides (48 kDa and 46 kDa) remain unidentified. Transfer of the glucagon-challenged hepatocytes to medium free of 32PO4(3-) and glucagon led to the rapid net dephosphorylation of the phosphopeptides and to a rapid decline in the specific radioactivity of the [32P]ATP pool. There were profound differences between the post-glucagon rates of net dephosphorylation of the different hepatic phosphopeptides, consistent with net dephosphorylation being asynchronous during the recovery phase from acute glucagon challenge. On the basis of descending rates of dephosphorylation, four major groups of phosphopeptides were delineated. Okadaic acid, a potent inhibitor of protein phosphatase 2A and to a lesser extent protein phosphatase 1, inhibited the dephosphorylation of all of the phosphopeptides. A role for protein phosphatase 2A in protein dephosphorylation may be indicated by the observation that spermine, a specific activator of protein phosphatase 2A, stimulates the dephosphorylation of some, but not all, of the glucagon-stimulated phosphopeptides. Although phosphorylation during the recovery phase from glucagon challenge may be a complicating factor, the results suggest that post-glucagon dephosphorylation is a complex asynchronous process. The physiological consequences of this asynchrony may be that the suppression of glycogenolysis and gluconeogenesis and the activation of glycolysis are early events in the recovery process.