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Acta Crystallographica Section F: Structural Biology and Crystallization Communications (1)
Pediatric research (1)
Trends in molecular medicine (1)
Tooley, James E. (2)
Bewley, Maria C. (1)
Bosch, Jürgen (1)
Herold, Kevan C. (1)
Heroux, Annie (1)
Hill, R. Blake (1)
Khangulov, Victor (1)
Lees, Jonathan P. B. (1)
Liu, Xun (1)
Løberg, Else Marit (1)
Schlessman, Jamie L. (1)
Suleiman, M. Saadeh (1)
Thoresen, Marianne (1)
Tooley, James (1)
Waldron-Lynch, Frank (1)
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New and future immunomodulatory therapy in type 1 diabetes
Herold, Kevan C.
Trends in molecular medicine
Type 1 diabetes is a common autoimmune disease that affects millions of people worldwide and has an incidence that is increasing at a striking rate, especially in young children. It results from the targeted self-destruction of the insulin-secreting β cells of the pancreas and requires lifelong insulin treatment. The effects of chronic hyperglycemia – the result of insulin deficiency – include secondary endorgan complications. Over the past two decades our increased understanding of the pathogenesis of this disease has led to the development of new immunomodulatory treatments. None have yet received regulatory approval, but this report highlights recent progress in this area.
type 1 diabetes; immunotherapy; metabolic therapy; biologics
The 1.75 Å resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain
Lees, Jonathan P. B.
Schlessman, Jamie L.
Bewley, Maria C.
Hill, R. Blake
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
A 1.75 Å resolution crystal structure of the Fis1 cytoplasmic domain from Saccharomyces cerevisiae is reported which adopts a tetratricopeptide-repeat fold.
Fis1 mediates mitochondrial and peroxisomal fission. It is tail-anchored to these organelles by a transmembrane domain, exposing a soluble cytoplasmic domain. Previous studies suggested that Fis1 is autoinhibited by its N-terminal region. Here, a 1.75 Å resolution crystal structure of the Fis1 cytoplasmic domain from Saccharomyces cerevisiae is reported which adopts a tetratricopeptide-repeat fold. It is observed that this fold creates a concave surface important for fission, but is sterically occluded by its N-terminal region. Thus, this structure provides a physical basis for autoinhibition and allows a detailed examination of the interactions that stabilize the inhibited state of this molecule.
tetratricopeptide repeats; protein–protein interactions; tail-anchoring; mitochondria; peroxisomes; membrane dynamics
Immediate hypothermia reduces cardiac troponin I following hypoxic-ischemic encephalopathy in newborn pigs
Løberg, Else Marit
Suleiman, M. Saadeh
Neonatal hypoxic-ischemic encephalopathy (HIE) is a clinically defined neurological condition following lack of oxygen and often associated with cardiac dysfunction in term infants. Therapeutic hypothermia after birth is neuroprotective in infants with HIE. However, it is not known whether hypothermia (HT) is also cardioprotective. Four newborn pigs were used in the pilot study and a further 18 newborn pigs (randomly assigned to 72h-normothermia (NT) or 24h-HT followed by 48h-NT) were subjected to global HIE insults. Serum cTnI was measured prior to and post the HIE insult. Blood pressure, inotropic support, blood gases and heart rate (HR) were recorded throughout. Cardiac pathology was assessed from histological sections. Cooling reduced serum cTnI levels significantly in HT pigs by 6h (NT, 1.36±0.67; HT 0.34±0.23 ng/ml, p=0.0009). After rewarming, from 24 to 30h post insult, HR and cTnI increased in the HT group; from HR[24h]=117±22 to HR[30h]=218±32 beats/minute (p=0.0002) and from cTnI[24h]=0.23±0.12 to cTnI[30h]=0.65±0.53ng/ml, (p=0.05). There were fewer ischemic lesions on cardiac examination (37%) in the HT group compared to the NT group (70%). Hypothermia (24h) pigs did not have the post-insult cTnI increase seen in NT treated pigs. There was a trend that HT improved cardiac pathology in this 3-day survival model.
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