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Post-Translational Regulation of C-Reactive Protein Secretion
Published in Andrzej Mackiewicz, Irving Kushner, Heinz Baumann, Acute Phase Proteins, 2020
Stephen S. Macintyre, Patricia A. Kalonick
The results presented here illustrate a novel mechanism which could effectively reroute the intracellular trafficking of a secretory protein under differing physiologic conditions. What might be the function of such a regulated retention mechanism for CRP? On the basis of previous findings,34 as well as the pulse-chase data and in vitro binding assays reported here, it is apparent that effective retention of CRP within the ER occurs preferentially in hepatocytes synthesizing CRP at relatively low rates. As a result, the cell accumulates a small pool of CRP within the ER. Since the retention (or retrieval) of CRP is calcium dependent, this pool would be rapidly mobilizable in response to transient decreases in local calcium concentration resulting, for example, from signal transduction during the early acute phase response. While there is controversy regarding the effects of calcium ionophores on the fate of ER resident proteins,73,74 local calcium fluxes within the ER appear to be of great potential physiologic significance.75 Whether a rapid secretory burst of intracellular CRP might play a role in the early acute phase response is presently unknown.
Composition of The Chromaffin Cell
Published in Stephen W. Carmichael, Susan L. Stoddard, The Adrenal Medulla 1986 - 1988, 2017
Stephen W. Carmichael, Susan L. Stoddard
Immunochemical characterization of a novel secretory protein was performed by Krisch, Horvat, Krisch et al. (1988). This protein is defined by monoclonal antibody HISL-19. Extracts of human pheochromocytoma and other tumors were found to contain a protein immunoreactive with this antibody. The protein was found to be similar to chromogranins but distinct from chromogranins A, B, and C.
INTRODUCTION
Published in David M. Gibson, Robert A. Harris, Metabolic Regulation in Mammals, 2001
David M. Gibson, Robert A. Harris
(b) Another major parameter is the provision of substrates through membrane transport systems, e.g. the influx of glucose into the muscle cell by a specific transport protein (Chapter 6). Indeed membrane-bounded compartments of eukaryotic cells (ligure I.I) dramatically influence the pattern of metabolic flows by the separation of multienzyme systems: fatty acid oxidation and oxidative phosphorylation in mitochondria; fatty acid synthesis and glycolysis in the cytosol; secretory protein maturation in the golgi and endoplasmic reticulum; acidic proteolysis in Ivsosomcs; and the separation ol gene expression (transcription) in the nucleus from protein synthesis (transía tion) in the cytosol. Various controlling mechanisms regulate the traffic of metabolites and proteins passing from one compartment to another.
Immunoinformatics driven construction of multi-epitope vaccine candidate against Ascaris lumbricoides using its entire immunogenic epitopes
Published in Expert Review of Vaccines, 2021
Rimanpreet Kaur, Naina Arora, Suraj Singh Rawat, Anand Kumar Keshri, Neha Singh, Sumit Kumar Show, Pramod Kumar, Amit Mishra, Amit Prasad
The membrane proteins and excretory/secretory proteins are the first parasitic antigens that interact with the host immune system and induce an immunological response (activation/suppression). The signal peptides present on the N-terminal of proteins determine their fate to mark as secretory protein or to be located on the cell membrane. The Signal P 5.0 server (http://www.cbs.dtu.dk/services/SignalP/index.php) was used for this purpose [19]. The signal peptide prediction alone does not define the exact location of the proteins, so other servers were also used to find the membrane proteins, Deeploc server (http://www.cbs.dtu.dk/services/DeepLoc-1.0/index.php) and WolfPsort (https://wolfpsort.hgc.jp/), it predicted the subcellular localizations of proteins in the cell and the common membrane proteins thus identified were used for further analysis [20,21].
Club cell protein (CC16) in plasma, bronchial brushes, BAL and urine following an inhaled allergen challenge in allergic asthmatics
Published in Biomarkers, 2018
Henning Stenberg, Erik Wadelius, Subhabrata Moitra, Ida Åberg, Jaro Ankerst, Zuzana Diamant, Leif Bjermer, Ellen Tufvesson
Club cell 16 kDa secretory protein (CC16) is primarily produced by the non-ciliated club cells found in the epithelium of bronchi and bronchioles (Singh et al.1988). The exact function of CC16 is unknown, although evidence points towards an anti-inflammatory and immunomodulatory role within the airways (Levin et al.1986, Miele et al.1987, Dierynck et al.1995). A polymorphism in the CC16 gene has been linked to an increased risk of developing asthma during childhood (Laing et al.1998) and is associated with lower plasma levels of CC16 (Laing et al.2000). Lower circulating levels are also seen in asthmatic subjects compared to healthy controls (Shijubo et al.1999b), as well as fewer CC16-positive epithelial cells in small airways (Shijubo et al.1999a). Lower levels of CC16 have also been linked to a more rapid decline of lung function in patients with COPD (Park et al.2013) and in the general population (Guerra et al.2015).
Molecular therapeutics of hemophilia A and B
Published in Expert Review of Hematology, 2022
Jie Gong, Hao-Lin Wang, Lung-Ji Chang
The efficiency of protein secretion is correlated with stable interaction with a luminal protein in the ER identified as the molecular chaperone BiP. BiP is a member of the heat-shock protein 70 (hsp70) family and a glucose-regulated protein of 78 kDa (GRP78) [52]. BiP promotes FVIII solubility in the ER to produce functionally secreted FVIII [53,54]. Induction of secretory protein synthesis can induce BiP expression [55,56]. The residue Phe (309) within the FVIII A1-domain involves high affinity interaction between HC and LC and is correlated with BiP-binding. Significantly, mutation of Phe309Ser (F309S) increases FVIII secretion by 3-fold [36]. Moreover, the addition of betaine to improve the transport of FVIII from ER to Golgi can result in increased secretion [57,58].