Hyperacidification-induced, clear appearance of venules caused by the swelling of erythrocytes in microcirculation

In the mesenterium of rats it was found that an overacidity of the blood flowing in the area of microcirculation and caused by irrigation with acid media may be objectively represented in the clearing of venols measurable by means of video technique. The cause of this clearing process is the swelling of erythrocytes setting in at lower pH-values. According to in-vitro findings this swelling of erythrocytes will lead to an increase of the apparent viscosity of the blood fluid or blood cell suspension respectively in conformity with the increase of hematocrit connected with it.     

Starch Binding Domain-containing Protein 1/Genethonin 1 Is a Novel Participant in Glycogen Metabolism

Stbd1 is a protein of previously unknown function that is most prevalent in liver and muscle, the major sites for storage of the energy reserve glycogen. The protein is predicted to contain a hydrophobic N terminus and a C-terminal CBM20 glycan binding domain. Here, we show that Stbd1 binds to glycogen in vitro and that endogenous Stbd1 locates to perinuclear compartments in cultured mouse FL83B or Rat1 cells. When overexpressed in COSM9 cells, Stbd1 concentrated at enlarged perinuclear structures, co-localized with glycogen, the late endosomal/lysosomal marker LAMP1 and the autophagy protein GABARAPL1. Mutant Stbd1 lacking the N-terminal hydrophobic segment had a diffuse distribution throughout the cell. Point mutations in the CBM20 domain did not change the perinuclear localization of Stbd1, but glycogen was no longer concentrated in this compartment. Stable overexpression of glycogen synthase in Rat1WT4 cells resulted in accumulation of glycogen as massive perinuclear deposits, where a large fraction of the detectable Stbd1 co-localized. Starvation of Rat1WT4 cells for glucose resulted in dissipation of the massive glycogen stores into numerous and much smaller glycogen deposits that retained Stbd1. In vitro, in cells, and in animal models, Stbd1 consistently tracked with glycogen. We conclude that Stbd1 is involved in glycogen metabolism by binding to glycogen and anchoring it to membranes, thereby affecting its cellular localization and its intracellular trafficking to lysosomes.     

Is ageing the result of dominant and co-dominant mutations?

A number of unexplained features of ageing can be accounted for if cellular ageing is due to dominant or co-dominant mutations. The experimental evidence both for and against this hypothesis is weak, but experiments involving direct testing are possible.