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Protease Treatment

ABSTRACT: Determine if transcripts are released by protease treatment Keywords: Comparison of protease treatments

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE3686 | GEO | 2005/12/01

SECONDARY ACCESSION(S): PRJNA93829

REPOSITORIES: GEO

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Protease Treatment

Project description:Determine if transcripts are released by protease treatment During total RNA isolation cell free lysates from stationary-phase cultures or exponential cultures were treated with one of three proteases or buffer alone. All experimental samples are over a common reference. There are two replicates for each sample.

2010-06-30 | E-GEOD-3686 | biostudies-arrayexpress

Protease-activated receptor 2 links protease activity with calcium waves during egg activation and blastomere cleavage

Project description:Successful initiation of animal development requires activation of the egg immediately prior to fusion of gamete pronucleii. In all taxa, this is initiated by waves of calcium transients which transverse across the egg. Calcium waves also occur at cleavage furrows during later blastula cytokinesis. Calcium is released from the endoplasmic reticulum through activation of 1,4,5-trisphosphate (IP3) receptors. Only a subset of the mechanisms employed to generate IP3 during vertebrate egg activation are defined, with strong evidence that other critical mechanisms exist. Serine proteases have been long implicated in egg activation and fertilisation. Here we report that treatment of zebrafish eggs with serine protease inhibitors leads to defective calcium wave propagation and failed egg activation. We further show that mutation of zebrafish Protease-activated receptor 2a (Par2a) also results in severe disruption of egg activation, leading to failed chorion elevation and ooplasmic segregation. Milder par2a mutants progress further, but then show abnormal blastomere cleavage. We observed that par2a mutants show decreased amplitude and duration of calcium transients. Restoring Ca++ or direct injection of IP3 ligand rescues egg activation aborted by either serine protease inhibitor treatment or by mutation of Par2a. We thus show that serine protease activity is a critical regulator of IP3 and subsequent calcium wave amplification during zebrafish egg activation, and link this to intracellular calcium release via the protease receptor, Par2a. This constitutes a novel signalling pathway critical for successful fertilisation.

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Enzymatic treatment using trypsin and cold-active protease for C2C12 myoblasts

Project description:We have comprehensively profiled the time-series changes in gene expression dependent on enzymatic treatment using trypsin, and attempted to elucidate the global changes suppressed by treatment with cold active protease in a low-temperature environment.

2022-06-20 | GSE168452 | GEO

Heat-treatments affect protease activities and peptide profiles of ruminants’ milk

Project description:Proteases present in milk are heat-sensitive, and their activities increase or decrease depending on the intensity of the thermal treatment applied. The thermal effects on the protease activity are well-known for bovine milk but poorly understood for ovine and caprine milk. This study aimed to determine the nonspecific and specific protease activities in casein and whey fractions isolated from raw bovine, ovine and caprine milk collected in early lactation, and to determine the effects of low-temperature, long-time (63°C for 30 min) and high-temperature, short-time (85°C for 5 min) treatments on protease activities within each milk fraction.

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microRNA profile of control vehicle- and coagulation protease factor VIIa-released endothelial extracellular vesicles

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Polytopic protease downregulation effect on the brain (rogae-affy-arabi-492460)

Project description:Regulation of AD-related genes. Presenilins are intramembrane polytopic proteases. These proteases are critical proteins in pathogenesis of Alzheimer's disease. The function of other polytopic proteases expressed in brains is unknown. Proteins that may potentially interact with PS pathway are of interest to elucidate. In this project we will determine gene expression patterns in the brains of mice with altered expression of polytopic protease. We hypothesize that family of polytopic proteases expressed in brain may potentially interact with presenilin pathway. We will examine 4 RNA samples isolated from brains of mice with significant downregulation of polytopic protease and control animals. Total RNA was extracted, purified according to the manufacturer's protocol and stored at -80C. Keywords: polytopic protease, brain

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Protease-activated receptor-2 promotes osteogenesis in skeletal mesenchymal stem cells at the expense of adipogenesis

Project description:Osteoblast-like cells isolated from the calvariae of wildtyope and protease-activated receptor-2 null were treated with unconditioned medium (Control) or medium conditionedby the prostate cancer cell line MDA-PCa-2b (MDA). RNAseq analysis was performed to identify differntially gene expression in wildtype and protease-activated receptor-2 null in response to factors released by prostate cancer cells.

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C/EBPa Regulates Protease/anti-protease Balance and Mediates Bronchiolar Cell Recovery After Injury

Project description:In the present study, we hypothesized that C/EBPa (CCAAT/enhancer-binding protein alpha) plays a role in cell regeneration in response to bronchiolar epithelial cell injury. C/EBPa mediated ciliated cell regeneration after naphthalene bronchiolar epithelial cell injury in vivo. Furthermore, we demonstrated that C/EBPa regulates protease/anti-protease balance after lung injury, and intratracheal treatment with anti-protease (BPTI) restored ciliated cell regeneration after naphthalene injury in CebpaD/D mice.

2012-05-13 | GSE29285 | GEO

Enzymatic treatment using trypsin and cold-active protease for C2C12 myoblasts

Project description:Enzymatic treatment using trypsin and cold-active protease for C2C12 myoblasts

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C/EBPa Regulates Protease/anti-protease Balance and Mediates Bronchiolar Cell Recovery After Injury

2012-05-12 | E-GEOD-29285 | biostudies-arrayexpress