Factor XIII-A transglutaminase acts as a switch between preadipocyte proliferation and differentiation

Blood ◽  
2014 ◽  
Vol 124 (8) ◽  
pp. 1344-1353 ◽  
Author(s):  
Vamsee D. Myneni ◽  
Kiyotaka Hitomi ◽  
Mari T. Kaartinen
Keyword(s):  
Factor Xiii ◽  
Negative Regulator ◽  
Plasma Fibronectin ◽  
Matrix Assembly ◽  
Fibronectin Matrix ◽  
Key Points ◽  
Proliferation And Differentiation ◽  
Assembly Factor

Key Points Preadipocytes produce factor XIII-A, which acts as a negative regulator of adipogenesis by increasing plasma fibronectin matrix assembly. Factor XIII-A and plasma fibronectin matrix promote preadipocyte proliferation and proproliferative effects of insulin.

Sphingosine 1-Phosphate Stimulates Fibronectin Matrix Assembly Through a Rho-Dependent Signal Pathway

Blood ◽  
1999 ◽  
Vol 93 (9) ◽  
pp. 2984-2990 ◽  
Author(s):  
Qinghong Zhang ◽  
Olivier Peyruchaud ◽  
Kelly J. French ◽  
Magnus K. Magnusson ◽  
Deane F. Mosher
Keyword(s):  
Binding Sites ◽  
Signal Pathway ◽  
Bioactive Lipids ◽  
Surface Binding ◽  
Matrix Assembly ◽  
Fibronectin Matrix ◽  
Mg63 Cells ◽  
Sphingosine 1 Phosphate ◽  
Common Signal ◽  
Stimulation Of

Abstract Fibronectin matrix assembly is a cell-dependent process mediated by cell surface binding sites for the 70-kD N-terminal portion of fibronectin. We have shown that Rho-dependent cytoskeleton reorganization induced by lysophosphatidic acid (LPA) or the microtubule-disrupting agent nocodazole increases fibronectin binding (Zhang et al, Mol Biol Cell 8:1415, 1997). Sphingosine 1-phosphate (S1P) is a bioactive sphingolipid implicated in mitogenesis and cytoskeletal remodelling. Both LPA and S1P are present in increased amounts in serum as compared with plasma as a result of platelet activation. Addition of S1P to human osteosarcoma MG63 cells or human foreskin fibroblasts increased cell-mediated binding and assembly of fibronectin. MG63 cells expressed the Edg-2 and Edg-4 G-protein–coupled receptors for bioactive lipids, whereas foreskin fibroblasts expressed Edg-2, Edg-3, and Edg-4. The stimulatory effect of S1P on the binding of fibronectin or the N-terminal 70-kD fragment of fibronectin was dynamic and due to increases in both the number and affinity of binding sites. The stimulation of 70-kD fragment binding by nanomolar S1P, like stimulation of binding by LPA or nocodazole, was blocked by inactivation of Rho with C3 exotoxin but not by pertussis toxin-mediated inactivation of Gi. These results indicate a common signal pathway leading to control of cellular fibronectin matrix assembly by bioactive lipids generated during blood coagulation.

scholarly journals Ranking reactive glutamines in the fibrinogen αC region that are targeted by blood coagulant factor XIII

Blood ◽  
2016 ◽  
Vol 127 (18) ◽  
pp. 2241-2248 ◽  
Author(s):  
Kelly Njine Mouapi ◽  
Jacob D. Bell ◽  
Kerrie A. Smith ◽  
Robert A. S. Ariëns ◽  
Helen Philippou ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Key Points ◽  
Crosslinking Reactions

Key Points FXIIIa exhibits a preference for Q237 in crosslinking reactions within fibrinogen αC (233-425) followed by Q328 and Q366. None of the reactive glutamines in αC 233-425 (Q237, Q328, and Q366) are required to react first before the others can crosslink.

scholarly journals Cell Traction Forces Direct Fibronectin Matrix Assembly

2009 ◽  
Vol 96 (2) ◽  
pp. 729-738 ◽  
Author(s):  
Christopher A. Lemmon ◽  
Christopher S. Chen ◽  
Lewis H. Romer
Keyword(s):  
Matrix Assembly ◽  
Traction Forces ◽  
Cell Traction Forces ◽  
Fibronectin Matrix ◽  
Cell Traction

scholarly journals Sulfated hyaluronan affects fibronectin matrix assembly by human bone marrow stromal cells

2016 ◽  
Vol 4 ◽  
Author(s):  
Vogel Sarah ◽  
Moeller Stephanie ◽  
Arnoldini Simon ◽  
Samsonov Sergey ◽  
Schnabelrauch Matthias ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Stromal Cells ◽  
Bone Marrow Stromal Cells ◽  
Marrow Stromal Cells ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Matrix Assembly ◽  
Fibronectin Matrix

Gli2, but notGli1, is required for initial Shh signaling and ectopic activation of the Shh pathway

Development ◽  
2002 ◽  
Vol 129 (20) ◽  
pp. 4753-4761 ◽  
Author(s):  
C. Brian Bai ◽  
Wojtek Auerbach ◽  
Joon S. Lee ◽  
Daniel Stephen ◽  
Alexandra L. Joyner
Keyword(s):  
Signaling Pathway ◽  
Negative Regulator ◽  
Embryonic Patterning ◽  
Mouse Development ◽  
Shh Signaling ◽  
Shh Pathway ◽  
Cell Proliferation And Differentiation ◽  
Proliferation And Differentiation ◽  
Mammalian Tissues ◽  
Ectopic Activation

The Shh signaling pathway is required in many mammalian tissues for embryonic patterning, cell proliferation and differentiation. In addition, inappropriate activation of the pathway has been implicated in many human tumors. Based on transfection assays and gain-of-function studies in frog and mouse, the transcription factor Gli1 has been proposed to be a major mediator of Shh signaling. To address whether this is the case in mouse, we generated a Gli1 null allele expressing lacZ. Strikingly, Gli1 is not required for mouse development or viability. Of relevance, we show that all transcription of Gli1 in the nervous system and limbs is dependent on Shh and, consequently, Gli1 protein is normally not present to transduce initial Shh signaling. To determine whether Gli1 contributes to the defects seen when the Shh pathway is inappropriately activated and Gli1 transcription is induced, Gli1;Ptc double mutants were generated. We show that Gli1 is not required for the ectopic activation of the Shh signaling pathway or to the early embryonic lethal phenotype in Ptc null mutants. Of significance, we found instead that Gli2 is required for mediating some of the inappropriate Shh signaling in Ptc mutants. Our studies demonstrate that, in mammals, Gli1 is not required for Shh signaling and that Gli2 mediates inappropriate activation of the pathway due to loss of the negative regulator Ptc.

scholarly journals Polarized fibronectin secretion and localized matrix assembly sites correlate with subendothelial matrix formation

Blood ◽  
1990 ◽  
Vol 75 (12) ◽  
pp. 2335-2342 ◽  
Author(s):  
AP Kowalczyk ◽  
RH Tulloh ◽  
PJ McKeown-Longo
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Binding Sites ◽  
Affinity Binding ◽  
Apical Surface ◽  
Matrix Assembly ◽  
High Affinity Binding ◽  
High Affinity ◽  
Fibronectin Matrix ◽  
Subendothelial Matrix

Abstract Endothelial cells in vivo form the interface between the vascular and interstitial compartments and are strategically located to mediate vascular permeability and hemostasis. One mechanism endothelial cells use to maintain a nonthrombogenic surface is to polarize basement membrane constituents to the basolateral cell surface. In the present study, we began characterization of the mechanisms used by endothelial cells in the assembly of a subcellular fibronectin matrix. Immunofluorescence microscopy was used to localize extracellular matrix fibronectin in endothelial cell cultures. In contrast to preconfluent and newly confluent cultures, post-confluent cultures assembled a fibronectin matrix that was restricted to the basolateral cell surface. To determine if endothelial cells polarize fibronectin secretion, Millicell culture inserts were used to distinguish proteins secreted from apical and basal surfaces. Preconfluent and newly confluent cultures secreted fibronectin equally into apical and basal media. In contrast, post-confluent endothelial cells secreted fibronectin preferentially into the basal chamber. The degree to which fibronectin secretion was polarized varied with time in culture and with the ability of the monolayers to act as a barrier to the movement of 125I- fibronectin from the apical to basal chamber. In addition, high affinity binding sites for exogenous 125I-fibronectin were found to be present on the basolateral, but not apical, surface of post-confluent endothelial monolayers. These results indicate that subendothelial matrix assembly correlates with polarized fibronectin secretion, culture confluence, and expression of high affinity binding sites for fibronectin on the basolateral cell surface.

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