Identification of Treponema pallidum subspecies pallidum genes encoding signal peptides and membrane-spanning sequences using a novel alkaline phosphatase expression vector

1991 ◽  
Vol 5 (10) ◽  
pp. 2405-2415 ◽  
Author(s):  
D. R. Blanco ◽  
M. Giladi ◽  
C. I. Champion ◽  
D. A. Haake ◽  
G. K. Chikami ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Expression Vector ◽  
Treponema Pallidum ◽  
Signal Peptides ◽  
Genes Encoding ◽  
Membrane Spanning ◽  
Alkaline Phosphatase Expression

Intramembrane proteolysis and post-targeting functions of signal peptides

2003 ◽  
Vol 31 (6) ◽  
pp. 1243-1247 ◽  
Author(s):  
B. Martoglio
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Bilayer ◽  
Signal Peptide ◽  
Eukaryotic Cells ◽  
Endoplasmic Reticulum Membrane ◽  
Signal Peptides ◽  
Peptide Fragments ◽  
Intramembrane Proteolysis ◽  
Signal Sequences ◽  
Membrane Spanning

Signal sequences are the addresses of proteins destined for secretion. In eukaryotic cells, they mediate targeting to the endoplasmic reticulum membrane and insertion into the translocon. Thereafter, signal sequences are cleaved from the pre-protein and liberated into the endoplasmic reticulum membrane. We have recently reported that some liberated signal peptides are further processed by the intramembrane-cleaving aspartic protease signal peptide peptidase. Cleavage in the membrane-spanning portion of the signal peptide promotes the release of signal peptide fragments from the lipid bilayer. Typical processes that include intramembrane proteolysis is the regulatory or signalling function of cleavage products. Likewise, signal peptide fragments liberated upon intramembrane cleavage may promote such post-targeting functions in the cell.

Optimization of Yarrowia lipolytica-based consolidated biocatalyst through synthetic biology approach: transcription units and signal peptides shuffling

2020 ◽  
Author(s):  
Ewelina Celińska ◽  
Monika Borkowska ◽  
Paulina Korpys-Woźniak ◽  
Monika Kubiak ◽  
Jean-Marc Nicaud ◽  
...  
Keyword(s):  
Gene Copy Number ◽  
Regulatory Elements ◽  
Gene Copy ◽  
Signal Peptides ◽  
Synthetic Dna ◽  
Batch Bioreactor ◽  
Genes Encoding ◽  
Valuable Compounds ◽  
Synthetic Biology Approach ◽  
Lipids Accumulation

Abstract Background: Nowadays considerable effort is being pursued towards development of consolidated microbial biocatalysts that will be able to utilize complex, non-pretreated substrates and produce valuable compounds. In such engineered microbes, synthesis of extracellular hydrolases may be fine-tuned by different approaches, like strength of promoter, type of secretory tag, gene copy number etc. In this study, we investigated if organization of a multi-element expression cassette impacts the resultant Y. lipolytica transformants’ phenotype, presuming that different variants of the cassette are composed of the same regulatory elements and encode the same hydrolases. Results: To this end, Y. lipolytica cells were transformed with expression cassettes bearing a pair of genes encoding exactly the same mature amylases, but fused to four different signal peptides (SP), and located interchangeably in either first or second position of a synthetic DNA construction. The resultant strains were tested for growth on raw and pre-treated complex substrates of different plant origin for comprehensive examination of the strains’ acquired characteristics. The best strain’s performance was tested in batch bioreactor cultivations for growth and lipids accumulation. Conclusions: Based on the conducted research we concluded that the positional order of transcription units (TU) and the type of exploited SP affect final characteristics of the resultant consolidated biocatalyst strains, and thus could be considered as additional factors to be evaluated upon consolidated biocatalysts optimization.

Alkaline Phosphatase Expression in Human Chorionic Villi

Pathobiology ◽  
1987 ◽  
Vol 55 (1) ◽  
pp. 34-41 ◽  
Author(s):  
Giuseppe Novelli ◽  
Ferdinando Mannello ◽  
Ermelando V. Cosmi ◽  
Stefano Biagioni ◽  
Bruno Dallapiccola
Keyword(s):  
Alkaline Phosphatase ◽  
Chorionic Villi ◽  
Alkaline Phosphatase Expression

Root-end Filling Materials Alter Fibroblast Differentiation

2004 ◽  
Vol 83 (5) ◽  
pp. 408-413 ◽  
Author(s):  
S. Bonson ◽  
B.G. Jeansonne ◽  
T.E. Lallier
Keyword(s):  
Alkaline Phosphatase ◽  
Soft Tissues ◽  
Composite Resin ◽  
Mineral Trioxide Aggregate ◽  
Gingival Fibroblasts ◽  
Rt Pcr ◽  
Filling Materials ◽  
Polymerase Chain ◽  
Alkaline Phosphatase Expression ◽  
Expression And Activity

Root-end filling materials are commonly used following endodontic surgical procedures; however, their effect on adjacent soft tissues is poorly understood. We predict that, due to the differences in their chemical composition, these materials will have profoundly different effects on the survival and differentiation of fibroblasts. Many of the root-end filling materials examined were initially cytotoxic to both PDL and gingival fibroblasts in co-culture experiments; however, this was reduced after the materials were washed in either mineral trioxide aggregate (MTA) or hybrid ionomere composite resin (HICR) for 2 wks. Additionally, PDL fibroblasts displayed enhanced proliferation on MTA and survival on amalgam when compared with gingival fibroblasts. MTA preferentially induced alkaline phosphatase expression and activity in both PDL and gingival fibroblasts. In contrast, HICR inhibited alkaline phosphatase expression and activity. In addition, MTA and HICR repressed pleiotrophin in PDL fibroblasts, while HICR repressed periostin in both fibroblasts. Thus, root-end filling materials differentially affect periodontal fibroblast differentiation. Abbreviations: mineral trioxide aggregate (MTA), zinc-oxide eugenol cement (ZOEC), hybrid ionomer composite resin (HICR), reverse-transcriptase polymerase chain-reaction (RT-PCR).

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