PubMed HealthSearch

PubMed · 7004056

Hyperinsulinism.

Abstract

A 2-year-old boy had had severe intractable hypoglycaemia since birth. Transient success with diazoxide treatment delayed diagnosis until the age of 1 1/2 years. It was based on measurements of plasma insulin, blood glucose and urinary ketones at the end of a controlled fast, a normal glycaemic response to glucagon and an unusually high rate of glucose infusion necessary to maintain the blood sugar at a normal level. Subtotal pancreatectomy restored the blood sugar to normal without any impairment of exocrine pancreatic function.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

G Soltész, D Molnár, A Pintér, A Németh. 1980. Hyperinsulinism.. https://pubmed.ncbi.nlm.nih.gov/7004056/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Biological Mechanisms Underlying the Cardiovascular Effects of Branched-Chain Amino Acids: A Proteome-Wide Mendelian Randomization Study.

BACKGROUND: Ischemic heart disease (IHD) is the leading cause of morbidity and mortality. Branched-chain amino acids (BCAAs) are associated with higher IHD risk, but the underlying biological pathways remain unclear. OBJECTIVES: This study aims to explore these pathways using 2-step proteome-wide Mendelian randomization. METHODS: We examined the associations between genetic proxies for BCAAs and 2922 proteins in the United Kingdom Biobank Pharma Proteomics Project, supplemented by a meta-analysis with data from deCODE to identify proteins associated with BCAAs. Next, we tested their effects on IHD risk using Coronary Artery Disease Genome-wide Replication and Meta-analysis plus Coronary Artery Disease Genetics Consortium (122,733 cases and 424,528 controls) and replicated in FinnGen (31,640 cases and 187,152 controls). We conducted sensitivity analyses using genetic instruments from deCODE. Proteins associated with IHD risk and, in a consistent direction, with genetically predicted BCAAs were considered potential mediators. RESULTS: Genetic proxies for BCAAs were associated with 40 proteins. Among these, 6 proteins showed consistent evidence of mediation, including complement C1s subcomponent, coagulation factor II, granulin, proprotein convertase subtilisin/kexin type 9, sex hormone-binding globulin, and V-set and transmembrane domain-containing protein 2-like. These proteins are involved in inflammation, coagulation, lipid metabolism, and cellular stress response. All associations were robust across different analytical methods and replicated in independent datasets. Mediation analysis showed that these proteins accounted for 6.5% to 32.1% of the association between BCAAs and IHD risk. CONCLUSIONS: This study identified 6 proteins that potentially link BCAAs to IHD, implicating pathways related to inflammation, coagulation, lipid metabolism, and cellular stress responses. To our knowledge, these findings provide novel mechanistic insights into the BCAA-IHD relationship and highlight potential protein targets for future prevention and intervention strategies.

Amino Acids, Branched-Chain

Changes in the ratio of branched-chain to aromatic amino acids affect the secretion of albumin in cultured rat hepatocytes.

The effect of branched-chain amino acids (BCAAs) on the synthesis and secretion of albumin was studied in the primary cultures of rat hepatocytes. The changes in the normal BCAAs/aromatic amino acids (AAAs) ratio reduced the secretion of albumin without altering its mRNA levels. Protein-labeling and pulse-chase experiments showed that a low BCAAs/AAAs ratio reduced the biosynthesis, whereas a high ratio accelerated intracellular decay of albumin. These results suggest that normalization of the BCAAs/AAAs ratio improves albumin synthesis while the excess ratio may induce the degradation of albumin in the cells.

Amino Acids, Branched-Chain

Lipopolysaccharide (LPS) increases the in vivo oxidation of branched-chain amino acids in the rat: a cytokine-mediated effect.

Septic rats (as induced by cecal puncture and ligation) showed an increased rate of in vivo leucine oxidation as measured from the formation of 14CO2 from an intravenously injected [1-14C]leucine tracer dose. Acute lipopolysaccharide (LPS) administration (1 mg/kg) to rats caused a similar effect on the rate of in vivo leucine oxidation. Additionally, both tumour necrosis factor-alpha (TNF) and interleukin-1-alpha (IL-1), in an acute dose of 100 micrograms/kg, also increased the rate of the oxidation of the amino acid, although only IL-1 caused a similar increase to that observed following LPS. The observed increased leucine oxidation was related to lower leucine concentrations both in LPS- and cytokine-treated rats. Important decreases were also observed in the other branched-chain amino acids (valine and isoleucine) in the LPS- and IL-1-treated animals. Isolated incubated muscles from TNF- and IL-1-treated rats did not show any changes in the rate of leucine utilization, thus suggesting that the mechanism by which the cytokines stimulate whole-body leucine oxidation is not based on an increase in the activity of the enzymatic machinery responsible for leucine oxidation. Additionally, glucocorticoids do not seem to mediate the enhanced in vivo oxidation of the amino acid since, although they are increased by both LPS and cytokines, treatment of the animals with RU486 (a glucocorticoid antagonist) was not able to suppress the effects of the cytokine on in vivo leucine oxidation.

Amino Acids, Branched-Chain