China
Africa
Explore chapters and articles related to this topic
Evaluating the Interactions of Silver Nanoparticles and Mammalian Cells Based on Biomics Technologies
Published in Huiliang Cao, Silver Nanoparticles for Antibacterial Devices, 2017
Our research group further carried out proteomics analysis of Ag NPs on HDFs based on 2D-DIGE and mass identification. Twenty-five functional proteins were finally obtained after 200 μM Ag NP treatment for 1, 4 and 8 h (Table 10.3) (Huang et al. 2014). Comparing the protein and gene expression data, it was found that the number of differentially expressed proteins (25) was far less than that of differentially expressed genes (1593). Table 10.4 lists the expression pattern of 25 differentially expressed proteins and encoding mRNAs in HDFs treated with Ag NPs. Among them, only four differentially expressed mRNA–protein pairs were obtained (FH, HSPA8, EMC1 and HN1), with not exactly the same expression patterns.
The Endometrial Factor in Recurrent Pregnancy Loss
Published in Howard J.A. Carp, Recurrent Pregnancy Loss, 2020
Luiza Borges Manna, Ying Cheong
The selectivity of the endometrium does not stop at the implantation window and, in the event of failure of this first checkpoint of quality control, there are other mechanisms to avoid compromised embryos. Once the luminal epithelium is breached for implantation, the decidua engages in a molecular dialog with the conceptus and is capable of tailoring its microenvironment accordingly [16,17]. The decidua is therefore much more than a passive bystander subject to the embryo's invasive potential; instead, the decidua has an active role in implantation by acting as a biosensor of developmentally competent embryos. Molecular cues to this blastocyst-decidual interaction have been studied in in vitro models. A study that compared the response of decidualized endometrial cells to different quality embryos showed that those adequately developed trigger a surprisingly modest decidual response, whereas poor-quality embryos led to the inhibition of several factors important to early pregnancy [18]. Similarly, genome-wide expression profiling showed that whereas only 15 decidual genes were differentially expressed in response to high-grade embryos, 449 were altered in response to developmentally incompetent embryos [19]. It is thought that the latter downregulate the expression of key molecules such as HSPA8, which triggers an endoplasmic reticulum stress response that compromises the secretion of PRL and IGFBP-1 [4,19]. In addition, these embryos inhibit the secretion of several interleukins known to be key implantation factors and immunomodulators [18]. The decidual response is therefore stronger in response to abnormal embryos, which are likely to have more intense metabolic activity [1]. Moreover, endometrial stromal cells are programmed to undergo directional migration to encapsulate the blastocyst to ensure that, if developmentally competent, they become embedded in a nurturing environment [16]. While healthy endometrial stromal cells show reduced migration toward compromised blastocysts and change their secretome into a less favorable one once the surface epithelium is breached by a poor-quality embryo, the same has not been observed in the endometrium from RPL subjects [16,17].
HSC70 is a novel binding partner involved in the capture of immunoglobulins on B cells in the NOD mouse
Published in Autoimmunity, 2022
Emma Renman, Rifat Ekici, Mia Sundström, Kristina Lejon
Applying a bait-based isolation of the presumptive immunoglobulin binding partner on splenocytes we found HSC70 as the sole candidate. HSC70, also referred to as HSP73 or HSPA8, is a constitutively expressed, highly versatile protein belonging to the heat shock 70 protein family mainly localised in the cytosol and nucleus [21]. In the cytosol, HSC70 is involved in several processes including protein folding, translocation, clathrin-mediated endocytosis as well as in multiple autophagy pathways, where it plays a key role in chaperone-mediated autophagy (CMA) [21–23]. HSC70 is also involved in the presentation of peptides by major histocompatibility complex (MHC) class II on antigen presenting cells affecting availability and/or loading of peptides [24,25]. HSC70 has further been found on the cell surface of various cell types [26,27], including mouse lymphocytes [28]. Additionally, HSC70 can act as a plasma membrane receptor for cell surface binding and infection of multiple viruses [26,29,30] where blockage of HSC70 by antibodies or by HSC70 binding molecules reduce viral infection [26,30,31]. It has also been suggested that secreted HSC70 can function as an immunomodulator [32,33].