Altered levels of focal adhesion and extracellular matrix‐receptor interacting proteins were identified in Hailey‐Hailey disease by quantitative iTRAQ proteome analysis

2018 ◽  
Vol 120 (3) ◽  
pp. 3801-3812 ◽  
Author(s):  
Dingwei Zhang ◽  
Jia Huo ◽  
Ruilian Li ◽  
Yanfei Zhang ◽  
Zhenghui Wang ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Focal Adhesion ◽  
Proteome Analysis ◽  
Interacting Proteins ◽  
Receptor Interacting Proteins

scholarly journals Caspase-mediated Cleavage of p130cas in Etoposide-induced Apoptotic Rat-1 Cells

2000 ◽  
Vol 11 (3) ◽  
pp. 929-939 ◽  
Author(s):  
Seunghyi Kook ◽  
Sang Ryeol Shim ◽  
Soo Jeon Choi ◽  
Joohong Ahnn ◽  
Jae Il Kim ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Focal Adhesion ◽  
Caspase 3 ◽  
Morphological Changes ◽  
Point Mutations ◽  
Membrane Blebbing ◽  
Adhesion Sites ◽  
Focal Adhesion Proteins ◽  
Induced Apoptosis

Apoptosis causes characteristic morphological changes in cells, including membrane blebbing, cell detachment from the extracellular matrix, and loss of cell–cell contacts. We investigated the changes in focal adhesion proteins during etoposide-induced apoptosis in Rat-1 cells and found that during apoptosis, p130cas (Crk-associated substrate [Cas]) is cleaved by caspase-3. Sequence analysis showed that Cas contains 10 DXXD consensus sites preferred by caspase-3. We identified two of these sites (DVPD416G and DSPD748G) in vitro, and point mutations substituting the Asp of DVPD416G and DSPD748G with Glu blocked caspase-3-mediated cleavage. Cleavage at DVPD416G generated a 74-kDa fragment, which was in turn cleaved at DSPD748G, yielding 47- and 31-kDa fragments. Immunofluorescence microscopy revealed well-developed focal adhesion sites in control cells that dramatically declined in number in etoposide-treated cells. Cas cleavage correlated temporally with the onset of apoptosis and coincided with the loss of p125FAK (focal adhesion kinase [FAK]) from focal adhesion sites and the attenuation of Cas–paxillin interactions. Considering that Cas associates with FAK, paxillin, and other molecules involved in the integrin signaling pathway, these results suggest that caspase-mediated cleavage of Cas contributes to the disassembly of focal adhesion complexes and interrupts survival signals from the extracellular matrix.

scholarly journals Dopamine receptor interacting proteins: unraveling the receptor signalplex

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Lisa A Hazelwood ◽  
R Benjamin Free ◽  
David M Cabrera ◽  
David R Sibley
Keyword(s):  
Dopamine Receptor ◽  
Interacting Proteins ◽  
Receptor Interacting Proteins

scholarly journals Sperm Proteome after Interaction with Reproductive Fluids in Porcine: From the Ejaculation to the Fertilization Site

2020 ◽  
Vol 21 (17) ◽  
pp. 6060 ◽  
Author(s):  
Chiara Luongo ◽  
Leopoldo González-Brusi ◽  
Paula Cots-Rodríguez ◽  
Mª José Izquierdo-Rico ◽  
Manuel Avilés ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Proteome Analysis ◽  
Interacting Proteins ◽  
Sperm Transport ◽  
Two Fluids ◽  
Boar Sperm ◽  
Uterine Fluid ◽  
Proteome Changes ◽  
Oviductal Fluid

Ejaculated sperm are exposed to different environments before encountering the oocyte. However, how the sperm proteome changes during this transit remains unsolved. This study aimed to identify proteomic changes in boar sperm after incubation with male (seminal plasma, SP) and/or female (uterine fluid, UF; and oviductal fluid, OF) reproductive fluids. The following experimental groups were analyzed: (1) SP: sperm + 20% SP; (2) UF: sperm + 20% UF; (3) OF: sperm + 20% OF; (4) SP + UF: sperm + 20% SP + 20% UF; and (5) SP+OF: sperm + 20% SP + 20% OF. The proteome analysis, performed by HPLC-MS/MS, allowed the identification of 265 proteins. A total of 69 proteins were detected in the UF, SP, and SP + UF groups, and 102 proteins in the OF, SP, and SP + OF groups. Our results showed a higher number of proteins when sperm were incubated with only one fluid than when they were co-incubated with two fluids. Additionally, the number of sperm-interacting proteins from the UF group was lower than the OF group. In conclusion, the interaction of sperm with reproductive fluids alters its proteome. The description of sperm-interacting proteins in porcine species after co-incubation with male and/or female reproductive fluids may be useful to understand sperm transport, selection, capacitation, or fertilization phenomena.

scholarly journals Matrix Nanopatterning Regulates Mesenchymal Differentiation through Focal Adhesion Size and Distribution According to Cell Fate

Biomimetics ◽  
2019 ◽  
Vol 4 (2) ◽  
pp. 43 ◽  
Author(s):  
Ignasi Casanellas ◽  
Anna Lagunas ◽  
Yolanda Vida ◽  
Ezequiel Pérez-Inestrosa ◽  
José A. Andrades ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Fate ◽  
Focal Adhesion ◽  
Membrane Receptors ◽  
Extracellular Matrix Remodeling ◽  
Matrix Remodeling ◽  
Local Surface ◽  
Mesenchymal Differentiation ◽  
Cell Substrate ◽  
Arginine Glycine Aspartic Acid

Extracellular matrix remodeling plays a pivotal role during mesenchyme patterning into different lineages. Tension exerted from cell membrane receptors bound to extracellular matrix ligands is transmitted by the cytoskeleton to the cell nucleus inducing gene expression. Here, we used dendrimer-based arginine–glycine–aspartic acid (RGD) uneven nanopatterns, which allow the control of local surface adhesiveness at the nanoscale, to unveil the adhesive requirements of mesenchymal tenogenic and osteogenic commitments. Cell response was found to depend on the tension resulting from cell–substrate interactions, which affects nuclear morphology and is regulated by focal adhesion size and distribution.

Acute pancreatitis causes induction of receptor interacting proteins (RIP)

Pancreatology ◽  
2013 ◽  
Vol 13 (3) ◽  
pp. S54
Author(s):  
Dominique Schmidt ◽  
Susanne Kistner ◽  
Joachim Mössner ◽  
Sebastian Gaiser
Keyword(s):  
Acute Pancreatitis ◽  
Interacting Proteins ◽  
Receptor Interacting Proteins

Focal Adhesion Kinase Regulates Critical Functions in Hematopoiesis.

Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 1407-1407
Author(s):  
Sasidhar Vemula ◽  
Benjamin P. Abratigue ◽  
Premchand Gandra ◽  
John T. O’Malley ◽  
Ayek-Nati N. Ahyi ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Extracellular Matrix ◽  
Growth Factor ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Egf Receptor ◽  
Bone Marrow Cells ◽  
Focal Adhesions ◽  
Growth Factor Receptors ◽  
Fold Reduction

Abstract Focal adhesion kinase (FAK) initially identified as a unique cytoplasmic tyrosine kinase involved in focal adhesions, has been studied extensively in fibroblasts. In these cells, FAK has been shown to play an essential role in bridging signals between integrin and growth factor receptors such as the PDGF and the EGF receptor. In fibroblasts, FAK localizes to regions of the cell that attach to the extracellular matrix and coordinates signals from integrins, cytokines, growth factor receptors, and oncogenes. In some tumors, FAK is over-expressed or constitutively activated, which correlates with increased motility, invasiveness, and proliferation. More recently, expression of FAK in acute myeloid leukemia was associated with enhanced blast migration, increased cellularity, and poor prognosis. However, virtually nothing is known about FAKs role in normal hematopoiesis. FAK is expressed in blood cells, including in bone marrow derived KIT+, Gr-1+, Mac-1+, CD4+, CD8+ and B220+ cells. To determine how loss of FAK affects hematopoiesis, we have generated a mouse model with hematopoietic restricted deletion of FAK. We deleted FAK in bone marrow cells by crossing the FAK-flox mice to Mx.Cre+ expressing mice and by treating Mx.cre+FAK+/+ and Mx.cre+FAKflox/flox mice with poly (I)-poly(C) and then analyzing mice 1 month after the last injection. After one month of poly(I)-poly(C) induction, the progeny failed to express detectable levels of FAK in bone marrow, spleen as well as in bone marrow derived macrophages as determined by PCR and western blotting. Evaluation of peripheral blood counts in control and FAK deleted mice revealed modest but significant differences in different lineages (WBC k/μl: FAK; 14 vs. FAK−/−; 10.3, n=7, *p<0.05, LY k/μl: FAK; 10.48 vs. FAK−/−; 7.26, n=7, *p<0.005, RBC k/μl: FAK; 9.76 X106 vs. FAK−/−;8.58 X106 n=7 *p<0.003, PLT k/μl: FAK; 644 vs. FAK−/−; 434 n=7 *p<0.007). Since macrophages express abundant levels of FAK and are rapidly recruited in large numbers to sites of infection, we initially examined the role of FAK in macrophages by creating a well studied model of aseptic thioglycolate-induced peritonitis. Our results demonstrate a ∼1.5 fold reduction in the migration of macrophages to the peritoneal cavity of FAK−/− mice compared to controls (n=5, FAK; 1.8 X 106 vs. FAK−/−; 1.213 X106, *p<0.03). The reduction in recruitment of FAK−/− macrophages was observed in spite of comparable levels of F4/80 expression (WT; 92.98% vs. FAK−/−; 94.55%) as well as integrin (α4β1 & α5β1) expression (WT; 68% & 83.79% vs. FAK−/−; 60.39% & 83.17%, respectively) between WT and FAK−/− macrophages. Further analysis of FAK−/− macrophages revealed a significant decrease in extracellular matrix/integrin directed migration of these cells in response to M-CSF on fibronectin (40% reduction), laminin (55% reduction) and collagen (60% reduction) (n=3, *p<0.004) coated plates as well as a decrease in migration in a wound healing assay (n=3, *p<0.003). The reduction in migration of FAK−/− macrophages was associated with a significant decrease in adhesion on fibronectin (63%), laminin (52%) and collagen (56%) as well as spreading (n=3, *p<0.03). Taken together, our results provide a critical physiologic role for FAK in regulating several adhesive and migratory functions in cells of myeloid lineage. Additional functions of FAK in other hematopoietic lineages will be discussed.

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