Lown–Ganong–Levine syndrome (LGL) is a pre-excitation syndrome of the heart. Those with LGL syndrome have episodes of abnormal heart racing with a short PR interval and normal QRS complexes seen on their electrocardiogram when in a normal sinus rhythm. LGL syndrome was originally thought to be due to an abnormal electrical connection between the atria and the ventricles, but is now thought to be due to accelerated conduction through the atrioventricular node in the majority of cases. The syndrome is named after Bernard Lown, William Francis Ganong, Jr., and Samuel A. Levine. Signs and symptoms
Pathophysiology
LGL syndrome was originally thought to involve a rapidly conducting accessory pathway (bundle of James) that connects the atria directly to the bundle of His, bypassing the slowly conducting atrioventricular node. However, the majority of those with LGL in whom electrophysiological studies have been performed do not have any evidence of an accessory pathway or structural abnormality. Whilst in a minority of cases some form of intranodal or paranodal fibers that bypass all or part of the atrioventricular node can be found with subsequent conduction down the normal His-Purkinje system, in most cases the short PR interval is caused by accelerated conduction through the atrioventricular node. LGL syndrome is therefore felt to represent a clinical syndrome with multiple different underlying causes.
Mechanism
Diphtheria toxin (DT) is produced only by C. diphtheriae infected with a certain type of bacteriophage. Toxinogenicity is determined by phage conversion (also called lysogenic conversion); i.e, the ability of the bacterium to make DT changes as a consequence of infection by a particular phage. DT is encoded by the tox gene. Strains of corynephage are either tox+ (e.g., corynephage β) or tox- (e.g., corynephage γ). The tox gene becomes integrated into the bacterial genome. The chromosome of C. diphtheriae has two different but functionally equivalent bacterial attachment sites (attB) for integration of β prophage into the chromosome. Diphtheria toxin precursor is a protein of molecular weight 60 kDa. Certain proteases, such as trypsin, selectively cleave DT to generate two peptide chains, amino-terminal fragment A (DT-A) and carboxyl-terminal fragment B (DT-B), which are held together by a disulfide bond. DT-B is a recognition subunit that gains entry of DT into the host cell by binding to the EGF-like domain of heparin-binding EGF-like growth factor  on the cell surface. This signals the cell to internalize the toxin within an endosome via receptor-mediated endocytosis. Inside the endosome, DT is split by a trypsin-like protease into DT-A and DT-B. The acidity of the endosome causes DT-B to create pores in the endosome membrane, thereby catalysing the release of DT-A into the cytoplasm.Fragment A inhibits the synthesis of new proteins in the affected cell by catalyzing ADP-ribosylation of elongation factor EF-2—a protein that is essential to the translation step of protein synthesis.