Proof of Life

Well I made it home and finished the Japanese Maple Lego — to be honest it was about the easiest build I have done. I was warned by my medical team that being home would result in fatigue and not t…

Crushing Goals (Treatment Days 158-159)

Thursday It was my last day of rehab at the Flinders Medical Centre. It was a day of tests and surveys. Being the overachiever that I am, my original 4-week intensive was bumped up to 6 weeks. In 1…

Bluesky

Bluesky

Bluesky

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy - Laboratory Investigation

Transthyretin (TTR)-related familial amyloidotic polyneuropathy (FAP) is characterized by systemic accumulation of amyloid fibrils caused by a point mutation in the TTR gene. Despite the urgent need for alternative therapeutic strategies, the pathogenesis of FAP still remains elusive. In our study reported here, we focused on albumin, the most abundant protein in plasma, and described the role of albumin in the TTR amyloid-formation process. Patients with FAP evidenced significantly decreased serum albumin levels as the disease progressed. Biacore analysis showed that albumin had a binding affinity for TTR and exhibited higher affinity for TTR amyloid than native TTR. Albumin functioning as an antioxidant effectively suppressed TTR amyloid formation. In patients with FAP, albumin was significantly oxidized as the disease progressed. Moreover, loss of functional albumin accelerated TTR deposition in analbuminemic rats possessing a human variant TTR gene. Taken together, these results indicate that albumin may have an inhibitory role in the TTR amyloid-formation process.

Amyloidosis of the heart reversed in 3 patients for the first time

Researchers have observed spontaneous reversal of the devastating heart condition transthyretin cardiac amyloidopathy for the first time, edging closer to a cure.