Differential protein abundance in promastigotes of nitric oxide-sensitive and resistantLeishmania chagasistrains

2016 ◽  
Vol 10 (11) ◽  
pp. 1132-1146 ◽  
Author(s):  
Pedro J. Alcolea ◽  
Gabriel I. L. Tuñón ◽  
Ana Alonso ◽  
Francisco García-Tabares ◽  
Sergio Ciordia ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Abundance ◽  
Differential Protein

Differential protein abundance during the first month of regeneration of the Caribbean star coral Montastraea cavernosa

Coral Reefs ◽  
2018 ◽  
Vol 38 (1) ◽  
pp. 45-61 ◽  
Author(s):  
Ryan A. Horricks ◽  
Christophe M. Herbinger ◽  
Brandon N. Lillie ◽  
Paul Taylor ◽  
John S. Lumsden
Keyword(s):  
Protein Abundance ◽  
Differential Protein ◽  
The Caribbean ◽  
Montastraea Cavernosa

scholarly journals Quantitative Proteomics and Differential Protein Abundance Analysis after the Depletion of PEX3 from Human Cells Identifies Additional Aspects of Protein Targeting to the ER

2021 ◽  
Vol 22 (23) ◽  
pp. 13028
Author(s):  
Richard Zimmermann ◽  
Sven Lang ◽  
Monika Lerner ◽  
Friedrich Förster ◽  
Duy Nguyen ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Protein Import ◽  
Protein Targeting ◽  
Human Cells ◽  
Protein Abundance ◽  
General Role ◽  
Differential Protein ◽  
Er Targeting ◽  
Dependent Pathway ◽  
Er Membrane

Protein import into the endoplasmic reticulum (ER) is the first step in the biogenesis of around 10,000 different soluble and membrane proteins in humans. It involves the co- or post-translational targeting of precursor polypeptides to the ER, and their subsequent membrane insertion or translocation. So far, three pathways for the ER targeting of precursor polypeptides and four pathways for the ER targeting of mRNAs have been described. Typically, these pathways deliver their substrates to the Sec61 polypeptide-conducting channel in the ER membrane. Next, the precursor polypeptides are inserted into the ER membrane or translocated into the ER lumen, which may involve auxiliary translocation components, such as the TRAP and Sec62/Sec63 complexes, or auxiliary membrane protein insertases, such as EMC and the TMCO1 complex. Recently, the PEX19/PEX3-dependent pathway, which has a well-known function in targeting and inserting various peroxisomal membrane proteins into pre-existent peroxisomal membranes, was also found to act in the targeting and, putatively, insertion of monotopic hairpin proteins into the ER. These either remain in the ER as resident ER membrane proteins, or are pinched off from the ER as components of new lipid droplets. Therefore, the question arose as to whether this pathway may play a more general role in ER protein targeting, i.e., whether it represents a fourth pathway for the ER targeting of precursor polypeptides. Thus, we addressed the client spectrum of the PEX19/PEX3-dependent pathway in both PEX3-depleted HeLa cells and PEX3-deficient Zellweger patient fibroblasts by an established approach which involved the label-free quantitative mass spectrometry of the total proteome of depleted or deficient cells, as well as differential protein abundance analysis. The negatively affected proteins included twelve peroxisomal proteins and two hairpin proteins of the ER, thus confirming two previously identified classes of putative PEX19/PEX3 clients in human cells. Interestingly, fourteen collagen-related proteins with signal peptides or N-terminal transmembrane helices belonging to the secretory pathway were also negatively affected by PEX3 deficiency, which may suggest compromised collagen biogenesis as a hitherto-unknown contributor to organ failures in the respective Zellweger patients.

Differential protein abundance associated with delayed regeneration of the scleractinian coral Montastraea cavernosa

Coral Reefs ◽  
2020 ◽  
Vol 39 (4) ◽  
pp. 1175-1186
Author(s):  
Ryan A. Horricks ◽  
Christophe M. Herbinger ◽  
Matthew K. Vickaryous ◽  
Paul Taylor ◽  
John S. Lumsden
Keyword(s):  
Scleractinian Coral ◽  
Protein Abundance ◽  
Differential Protein ◽  
Montastraea Cavernosa

Decreased ileal muscle contractility and increased NOS II expression induced by lipopolysaccharide

1996 ◽  
Vol 271 (3) ◽  
pp. G454-G460 ◽  
Author(s):  
N. W. Weisbrodt ◽  
T. A. Pressley ◽  
Y. F. Li ◽  
M. J. Zembowicz ◽  
S. C. Higham ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Longitudinal Muscle ◽  
Competitive Inhibitor ◽  
Mrna Abundance ◽  
Physiological Salt Solution ◽  
Protein Abundance ◽  
Full Thickness ◽  
Muscle Contractility ◽  
Oxide Synthase

This study was designed to determine if an increase in nitric oxide synthase (NOS) activity induced by lipopolysaccharide (LPS) is associated with increases in NOS II protein and mRNA abundance and with altered ileal longitudinal muscle contractility. Strips of muscle taken from LPS-treated, but not control, animals exhibited reduced in vitro contractility when L-arginine was a component of the physiological salt solution. This reduction was reversed by N omega-nitro-L-arginine (L-NNA), a competitive inhibitor of NOS. Full-thickness segments of jejunum, ileum, and colon taken 5 h after LPS injection exhibited increased NOS activity, NOS II immunoreactivity, and NOS II mRNA abundance. Increased NOS II immunoreactivity and mRNA abundance also were detected in ileal muscle strips taken from LPS-treated animals. These data confirm the reported effects of LPS on intestinal NOS activity and indicate that it can be attributed, at least in part, to an increase in NOS II mRNA and protein abundance. Furthermore, the data suggest that an LPS-induced increase in NOS II may lead to a decrease in ileal muscle contractility.

scholarly journals Differential protein abundance and function of UT-B urea transporters in human colon

2010 ◽  
Vol 298 (3) ◽  
pp. G345-G351 ◽  
Author(s):  
D. Collins ◽  
D. C. Winter ◽  
A. M. Hogan ◽  
L. Schirmer ◽  
A. W. Baird ◽  
...  
Keyword(s):  
Intestinal Bacteria ◽  
Human Colon ◽  
Immunoblot Analysis ◽  
Cellular Level ◽  
Gut Bacteria ◽  
Protein Abundance ◽  
Urea Transport ◽  
Ascending Colon ◽  
Differential Protein ◽  
Descending Colon

Facilitative UT-B urea transporters enable the passage of urea across cell membranes. Gastrointestinal urea transporters are thought to play a significant role in the urea nitrogen salvaging process that occurs between mammalian hosts and their gut bacteria. This study investigated the expression of UT-B urea transporters in different segments of human colon. Immunoblot analysis showed that human colon expressed a 35-kDa glycosylated UT-B protein in the colonic mucosa. The 35-kDa UT-B transporter was predominantly located in plasma membrane-enriched samples ( P < 0.001; n = 6), and its expression was greater in the ascending colon compared with the descending colon ( P < 0.01; n = 3). At the cellular level, UT-B transporters were located throughout colonocytes situated in the upper portion of the colonic crypts. Bidirectional trans-epithelial urea transport was significantly greater in the ascending colon than the descending colon ( P < 0.05; n = 6). In addition, the facilitative urea transporter inhibitor 1,3,dimethylurea significantly reduced urea transport in the ascending colon ( P < 0.05; n = 6) but had no effect in the descending colon (NS; n = 6). These results illustrate differential protein abundance of functional UT-B protein in different sections of the human colon, strongly correlating to regions that contain the largest populations of intestinal bacteria. This study suggests an important role for UT-B urea transporters in maintaining the symbiotic relationship between humans and their gut bacteria.

scholarly journals Detecting differential protein abundance by combining peptide level P-values

2020 ◽  
Vol 16 (6) ◽  
pp. 554-562
Author(s):  
Bryan J. Killinger ◽  
Vladislav A. Petyuk ◽  
Aaron T. Wright
Keyword(s):  
Protein Abundance ◽  
P Values ◽  
Differential Protein ◽  
Peptide Level ◽  
Brown's Method ◽  
P Application ◽  
Differentially Abundant Proteins

Application of empirical Brown's method to peptide intensities from comparative LC-MS proteomics experiments accurately detects differentially abundant proteins.

Identification of Putative Genes Involved in Bisphenol A Degradation Using Differential Protein Abundance Analysis of Sphingobium sp. BiD32

2015 ◽  
Vol 49 (20) ◽  
pp. 12232-12241 ◽  
Author(s):  
Nicolette A. Zhou ◽  
Henrik Kjeldal ◽  
Heidi L. Gough ◽  
Jeppe L. Nielsen
Keyword(s):  
Bisphenol A ◽  
Protein Abundance ◽  
Differential Protein

scholarly journals Pendrin protein abundance in the kidney is regulated by nitric oxide and cAMP

2012 ◽  
Vol 303 (6) ◽  
pp. F812-F820 ◽  
Author(s):  
Monika Thumova ◽  
Vladimir Pech ◽  
Otto Froehlich ◽  
Diana Agazatian ◽  
Xiaonan Wang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Pressor Response ◽  
Fluorescent Microscopy ◽  
Phosphodiesterase Inhibitor ◽  
Protein Abundance ◽  
No Donor ◽  
Camp Content

Pendrin is a Cl−/HCO3− exchanger, expressed in the apical regions of some intercalated cell subtypes, and is critical in the pressor response to angiotensin II. Since angiotensin type 1 receptor inhibitors reduce renal pendrin protein abundance in mice in vivo through a mechanism that is dependent on nitric oxide (NO), we asked if NO modulates renal pendrin expression in vitro and explored the mechanism by which it occurs. Thus we quantified pendrin protein abundance by confocal fluorescent microscopy in cultured mouse cortical collecting ducts (CCDs) and connecting tubules (CNTs). After overnight culture, CCDs maintain their tubular structure and maintain a solute gradient when perfused in vitro. Pendrin protein abundance increased 67% in CNT and 53% in CCD when NO synthase was inhibited ( NG-nitro-l-arginine methyl ester, 100 μM), while NO donor (DETA NONOate, 200 μM) application reduced pendrin protein by ∼33% in the CCD and CNT. When CNTs were cultured in the presence of the guanylyl cyclase inhibitor 1H-[1,2,4] oxadiazolo[4,3-a]quinoxalin-1-one (10 μM), NO donors did not alter pendrin abundance. Conversely, pendrin protein abundance rose when cAMP content was increased by the application of an adenylyl cyclase agonist (forskolin, 10 μM), a cAMP analog (8-bromo-cAMP, 1 mM), or a phosphodiesterase inhibitor (BAY60-7550, 50 μM). Since NO reduces cellular cAMP in the CNT, we asked if NO reduces pendrin abundance by reducing cAMP. With blockade of cGMP-stimulated phosphodiesterase II, NO did not alter pendrin protein abundance. We conclude that NO acts through cAMP to reduce pendrin total protein abundance by enhancing cAMP degradation.

Differential protein abundance of a basolateral MCT1 transporter in the human gastrointestinal tract

2016 ◽  
Vol 40 (12) ◽  
pp. 1303-1312 ◽  
Author(s):  
Hashemeya Al-mosauwi ◽  
Elizabeth Ryan ◽  
Alison McGrane ◽  
Stefanie Riveros-Beltran ◽  
Caragh Walpole ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Protein Abundance ◽  
Human Gastrointestinal Tract ◽  
Differential Protein

scholarly journals Renal nitric oxide production in rat pregnancy: role of constitutive nitric oxide synthases

2010 ◽  
Vol 299 (4) ◽  
pp. F830-F836 ◽  
Author(s):  
Cheryl A. Smith ◽  
Beth Santymire ◽  
Aaron Erdely ◽  
Vasuki Venkat ◽  
György Losonczy ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Renal Cortex ◽  
Soluble Fraction ◽  
Splice Variants ◽  
Normal Pregnancy ◽  
No Production ◽  
Protein Abundance ◽  
Functional Studies ◽  
Enos Protein

Functional studies show that increased renal nitric oxide (NO) mediates the renal vasodilation and increased glomerular filtration rate that occur during normal pregnancy. We investigated whether changes in the constitutive NO synthases (NOS), endothelial (eNOS) and neuronal (nNOS), were associated with the increased renal NO production in normal midterm pregnancy in the rat. In kidneys from midterm pregnant (MP: 11–13 days gestation), late-term pregnant (LP: 18–20 days gestation), and similarly aged virgin (V) rats, transcript and protein abundance for eNOS and the nNOSα and nNOSβ splice variants, as well as the rate of l-arginine-to-l-citrulline conversion, were determined as a measure of NOS activity. At MP, renal cortical abundance of the total eNOS protein and phosphorylated (Ser1177) eNOS was reduced, and l-arginine-to-l-citrulline conversion in the cortical membrane fraction was decreased; these declines were also seen in LP. There were no changes in the eNOS transcript. In contrast, l-arginine-to-l-citrulline conversion in the soluble fraction of renal cortex increased at MP and then declined at LP. This MP increase was ablated by S-methylthiocitrulline, a nNOS inhibitor. Using Western blotting, we did not detect a change in the protein abundance or transcript of the 160-kDa nNOSα, but protein abundance and transcript of the nNOSβ were increased at MP in cortex. Collectively, these studies suggest that the soluble nNOSβ is responsible for the increased renal cortical NO production during pregnancy.

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