Heparan Sulfate Stimulates Extracellular Matrix Protein Synthesis by Mesangial Cells in Culture

Nephron ◽  
1995 ◽  
Vol 71 (2) ◽  
pp. 197-202 ◽  
Author(s):  
Gerald C. Groggel ◽  
M. Laurette Hughes
Keyword(s):  
Extracellular Matrix ◽  
Protein Synthesis ◽  
Heparan Sulfate ◽  
Matrix Protein ◽  
Mesangial Cells ◽  
Extracellular Matrix Protein ◽  
Cells In Culture

Initial characterization of anosmin-1, a putative extracellular matrix protein synthesized by definite neuronal cell populations in the central nervous system

1996 ◽  
Vol 109 (7) ◽  
pp. 1749-1757 ◽  
Author(s):  
N. Soussi-Yanicostas ◽  
J.P. Hardelin ◽  
M.M. Arroyo-Jimenez ◽  
O. Ardouin ◽  
R. Legouis ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Extracellular Matrix ◽  
Nervous System ◽  
Cell Membrane ◽  
Heparan Sulfate ◽  
Matrix Protein ◽  
Neuronal Cell ◽  
Extracellular Matrix Protein ◽  
Cell Populations

The KAL gene is responsible for the X-chromosome linked form of Kallmann's syndrome in humans. Upon transfection of CHO cells with a human KAL cDNA, the corresponding encoded protein, KALc, was produced. This protein is N-glycosylated, secreted in the cell culture medium, and is localized at the cell surface. Several lines of evidence indicate that heparan-sulfate chains of proteoglycan(s) are involved in the binding of KALc to the cell membrane. Polyclonal and monoclonal antibodies to the purified KALc were generated. They allowed us to detect and characterize the protein encoded by the KAL gene in the chicken central nervous system at late stages of embryonic development. This protein is synthesized by definite neuronal cell populations including Purkinje cells in the cerebellum, mitral cells in the olfactory bulbs and several subpopulations in the optic tectum and the striatum. The protein, with an approximate molecular mass of 100 kDa, was named anosmin-1 in reference to the deficiency of the sense of smell which characterizes the human disease. Anosmin-1 is likely to be an extracellular matrix component. Since heparin treatment of cell membrane fractions from cerebellum and tectum resulted in the release of the protein, we suggest that one or several heparan-sulfate proteoglycans are involved in the binding of anosmin-1 to the membranes in vivo.

scholarly journals Glucagon-like peptide-1 receptor pathway inhibits extracellular matrix production by mesangial cells through store-operated Ca2+ channel

2019 ◽  
Vol 244 (14) ◽  
pp. 1193-1201 ◽  
Author(s):  
Linjing Huang ◽  
Rong Ma ◽  
Tingting Lin ◽  
Sarika Chaudhari ◽  
Parisa Y Shotorbani ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
High Glucose ◽  
Protein Production ◽  
Matrix Protein ◽  
Mesangial Cells ◽  
Collagen Iv ◽  
Extracellular Matrix Protein ◽  
Human Mesangial Cells ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

Glomerular mesangial cell is the major source of mesangial matrix. Our previous study demonstrated that store-operated Ca2+ channel signaling suppressed extracellular matrix protein production by mesangial cells. Recent studies demonstrated that glucagon-like peptide-1 receptor (GLP-1R) pathway had renoprotective effects. However, the underlying mechanism(s) remains unclear. The present study was aimed to determine if activation of GLP-1R decreased extracellular matrix protein production by mesangial cells through upregulation of store-operated Ca2+ function. Experiments were conducted in cultured human mesangial cells. Liraglutide and exendin 9–39 were used to activate and inhibit GLP-1R, respectively. Store-operated Ca2+ function was estimated by evaluating the SOC-mediated Ca2+ entry (SOCE). We found that liraglutide treatment reduced high glucose-stimulated production of fibronectin and collagen IV. The inhibitory effects of liraglutide were not observed in the presence of exendin 9–39. Exendin-4, another GLP-1R agonist also blunted high glucose-stimulated fibronectin and collagen IV production. Treatment of human mesangial cells with liraglutide for 24 h significantly attenuated the high glucose-induced reduction of Orai1 protein. Consistently, Ca2+ imaging experiments showed that the inhibition of high glucose on SOCE was significantly attenuated by liraglutide. However, in the presence of exendin 9–39, liraglutide failed to reverse the high glucose effect. Furthermore, liraglutide effects on fibronectin and collagen IV protein abundance were significantly attenuated by GSK-7975A, a selective blocker of store-operated Ca2+. Taken together, our findings suggest that GLP-1R signaling inhibited high glucose-induced extracellular matrix protein production in mesangial cells by restoring store-operated Ca2+ function. Impact statement Diabetic kidney disease continues to be a major challenge to health care system in the world. There are no known therapies currently available that can cure the disease. The present study provided compelling evidence that activation of GLP-1R inhibited extracellular matrix protein production by glomerular mesangial cells. We further showed that the beneficial effect of GLP-1R was attributed to upregulation of store-operated Ca2+ channel function. Therefore, we identified a novel mechanism contributing to the renal protective effects of GLP-1R pathway. Activation of GLP-1R pathway and/or store-operated Ca2+ channel signaling in MCs could be an option for patients with diabetic kidney disease.

Thromboxane stimulates synthesis of extracellular matrix proteins in vitro

1991 ◽  
Vol 261 (3) ◽  
pp. F488-F494 ◽  
Author(s):  
L. A. Bruggeman ◽  
E. A. Horigan ◽  
S. Horikoshi ◽  
P. E. Ray ◽  
P. E. Klotman
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Mesangial Cells ◽  
Extracellular Matrix Proteins ◽  
Cellular Protein ◽  
Matrix Proteins ◽  
Extracellular Matrix Protein ◽  
Renal Diseases ◽  
Glomerular Mesangial Cells

The vasoconstrictor eicosanoid thromboxane plays an important role in the pathogenesis of several renal diseases. As an autacoid, its local release alters blood flow and induces platelet aggregation. We report a direct stimulatory effect of thromboxane on extracellular matrix protein production and gene expression in vitro. Treatment of two cell types, differentiated mouse teratocarcinoma cells (F9+) and human glomerular mesangial cells, with two different thromboxane analogues resulted in increased production of components of the extracellular matrix including fibronectin and the basement membrane proteins laminin and type IV collagen. These responses to thromboxane were not the result of a mitogenic effect of thromboxane nor the result of an increase in total cellular protein. The increased production of extracellular matrix proteins was, at least in part, due to an increase in the steady-state level of mRNA for these genes. Furthermore, the effect of thromboxane was markedly inhibited by cotreatment with a thromboxane-receptor antagonist. These results suggest a new potential role for thromboxane as a mediator of the sclerotic and fibrotic responses to injury.

Semiquantitative measurement of total extracellular matrix protein produced by cultured mesangial cells

Nephrology ◽  
1998 ◽  
Vol 4 (5-6) ◽  
pp. 379-383 ◽  
Author(s):  
Tetsuya OOTAKA ◽  
Nobert KRAFT ◽  
Takao SAITO ◽  
Robert C ATKINS
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Mesangial Cells ◽  
Extracellular Matrix Protein

A porous PCL scaffold promotes the human chondrocytes redifferentiation and hyaline-specific extracellular matrix protein synthesis

2008 ◽  
Vol 85A (4) ◽  
pp. 1082-1089 ◽  
Author(s):  
N. Garcia-Giralt ◽  
R. Izquierdo ◽  
X. Nogués ◽  
M. Perez-Olmedilla ◽  
P. Benito ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Protein Synthesis ◽  
Matrix Protein ◽  
Human Chondrocytes ◽  
Extracellular Matrix Protein
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