iASPP protects the heart from ischemia injury by inhibiting p53 expression and cardiomyocyte apoptosis.

Currently, there remains a great need to elucidate the molecular mechanism of acute myocardial infarction in order to facilitate the development of novel therapy. Inhibitor of apoptosis-stimulating protein of p53 (iASPP) is a member of the ASPP family proteins and an evolutionarily preserved inhibitor of p53 that is involved in many cellular processes, including apoptosis of cancer cells. The purpose of this study was to investigate the possible role of iASPP in acute myocardial infarction.

[Production of humanized F(ab’)2 fragment of rabies blocking antibodies in Pichia pastoris yeast].

The yeast strain Pichia pastoris, a producer of humanized F(ab’)2 fragments of rabies-blocking antibodies, has been obtained. Human chaperone BiP coexpression caused a twofold increase of the immunoglobulins secretion level. The use of Fos and Jun zippers in the composition of heavy chains facilitated the dimerization of F(ab’)2 fragments of the shared pool of secreted immunoglobulins up to 75%.

[Engineering of a System for the Production of Mutant Human Alpha-Fetoprotein in the Methylotrophic Yeast Pichia pastoris].

A system for the production of mutant recombinant human alpha-fetoprotein (rhAFPO) lacking the glycosylation site has been engineered in the yeast Pichia pastoris. A strain of the methylotrophic yeast Pichia pastoris GS 115/pPICZ?A/rhAFP0, which produces unglycosylated rhAFPO and secretes it to the culture medium, has been constructed. Optimization and scale-up of the fermentation technology have resulted in an increase in the rhAFP0 yield to 20 mg/L.

Antibody fragments may be incorrectly processed in the yeast Pichia pastoris.

We have studied the efficiency of N-terminal processing of the antibody light chain depending on the structure of the leader sequence when expressed in the yeast Pichia pastoris. The humanized light kappa-chain of the murine antibody H3-1 and the Saccharomyces cerevisiae alpha-factor pre-pro-leader sequence (pre-pro-alpha-F) were used as models. The use of pre-region of the pre-pro-alpha-F alone or together with the Glu-Ala-linker leads to the slightly increased yield of the secreted L-chain but was accompanied by the incomplete N-terminal processing of the secreted product.