Deficiency of Biglycan Causes Cardiac Fibroblasts to Differentiate into a Myofibroblast Phenotype

Melchior-Becker, Ariane; Dai, Guang; Ding, Zhaoping; Schäfer, Liliana; Schrader, Jürgen; Young, Marian F.; Fischer, Jens W.

doi:10.1074/jbc.m110.192682

Cited by 62 publications

(49 citation statements)

References 63 publications

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“…The biglycan gene is located on the X chromosome; hence, male wild-type mice are bgn +/0 and male biglycan null mice are bgn −/0 . This nomenclature is consistent with the original report characterizing these mice, as well as subsequent reports [18]–[20]. Mice were housed 2–3 to a cage.…”

Section: Methodssupporting

confidence: 60%

Biglycan Deletion Alters Adiponectin Expression in Murine Adipose Tissue and 3T3-L1 Adipocytes

Ward

Ajuwon

2012

PLoS ONE

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Obesity promotes increased secretion of a number of inflammatory factors from adipose tissue. These factors include cytokines and very lately, extracellular matrix components (ECM). Biglycan, a small leucine rich proteoglycan ECM protein, is up-regulated in obesity and has recently been recognized as a pro-inflammatory molecule. However, it is unknown whether biglycan contributes to adipose tissue dysfunction. In the present study, we characterized biglycan expression in various adipose depots in wild-type mice fed a low fat diet (LFD) or obesity-inducing high fat diet (HFD). High fat feeding induced biglycan mRNA expression in multiple adipose depots. Adiponectin is an adipokine with anti-inflammatory and insulin sensitizing effects. Due to the importance of adiponectin, we examined the effect of biglycan on adiponectin expression. Comparison of adiponectin expression in biglycan knockout (bgn−/0) and wild-type (bgn+/0) reveals higher adiponectin mRNA and protein in epididymal white adipose tissue in bgn−/0 mice, as well higher serum concentration of adiponectin, and lower serum insulin concentration. On the contrary, knockdown of biglycan in 3T3-L1 adipocytes led to decreased expression and secretion of adiponectin. Furthermore, treatment of 3T3-L1 adipocytes with conditioned medium from biglycan treated macrophages resulted in an increase in adiponectin mRNA expression. These data suggest a link between biglycan and adiponectin expression. However, the difference in the pattern of regulation between in vivo and in vitro settings reveals the complexity of this relationship.

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Section: Methodssupporting

confidence: 60%

Biglycan Deletion Alters Adiponectin Expression in Murine Adipose Tissue and 3T3-L1 Adipocytes

Ward

Ajuwon

2012

PLoS ONE

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“…A number of studies indicate that biglycan plays a critical role in cardiovascular diseases (Heegaard et al, 2007;Bereczki and Santha, 2008;Westermann et al, 2008;Csont et al, 2010;Melchior-Becker et al, 2011), stressing the importance of biglycan in stabilizing the collagen network of the heart to preserve cardiac hemodynamic function. Furthermore, biglycan has been suggested to promote atherosclerosis due to retention of atherogenic lipids and promotion of inflammation within atherosclerotic lesions (Little et al, 2008;Derbali et al, 2010;Lam et al, 2011).…”

Section: Biglycanmentioning

confidence: 99%

3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors

Merline¹,

Nastase²,

Iozzo³

et al. 2012

Extracellular Matrix: Pathobiology and Signaling

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“…Biglycan can bind to the N-terminal triple helix of collagen VI (Wiberg et al, 2001) and other collagen subtypes (Douglas et al, 2006, Reinboth et al, 2002, Schonherr et al, 1995, Wiberg et al, 2001, Wiberg et al, 2002, Wiberg et al, 2003), thereby promoting the assembly of supramolecular collagen complexes (Melchior-Becker et al, 2011, Reinboth et al, 2006, Wiberg et al, 2002). Zinc-dependent endopeptidases such as MMPs can degrade a broad-spectrum of ECM components including proteoglycans (Gross and Lapiere, 1962, Sternlicht and Werb, 2001, Stocker and Bode, 1995).…”

Section: Matrix Metalloproteinases Involved In the Generation Of Bmentioning

confidence: 99%

Soluble biglycan as a biomarker of inflammatory renal diseases

Hsieh

Nastase

Zeng-Brouwers

et al. 2014

The International Journal of Biochemistry & Cell Biology

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Chronic renal inflammation is often associated with a progressive accumulation of various extracellular matrix constituents, including several members of the small leucine-rich proteoglycan (SLRP) gene family. It is becoming increasingly evident that the matrix-unbound SLRPs strongly regulate the progression of inflammation and fibrosis. Soluble SLRPs are generated either via partial proteolytic processing of collagenous matrices or by de novo synthesis evoked by stress or injury. Liberated SLRPs can then bind to and activate Toll-like receptors, thus modulating downstream inflammatory signaling. Preclinical animal models and human studies have recently identified soluble biglycan as a key initiator and regulator of various inflammatory renal diseases. Biglycan, generated by activated macrophages, can enter the circulation and its elevated levels in plasma and renal parenchyma correlate with unfavorable renal function and outcome. In this review, we will focus on the critical role of soluble biglycan in inflammatory signaling in various renal disorders. Moreover, we will provide new data implicating proinflammatory effects of soluble decorin in unilateral ureteral obstruction. Finally, we will critically evaluate the potential application of soluble biglycan vis-à-vis other SLRPs (decorin, lumican and fibromodulin) as a promising target and novel biomarker of inflammatory renal diseases.

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Deficiency of Biglycan Causes Cardiac Fibroblasts to Differentiate into a Myofibroblast Phenotype

Cited by 62 publications

References 63 publications

Biglycan Deletion Alters Adiponectin Expression in Murine Adipose Tissue and 3T3-L1 Adipocytes

Biglycan Deletion Alters Adiponectin Expression in Murine Adipose Tissue and 3T3-L1 Adipocytes

3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors

Soluble biglycan as a biomarker of inflammatory renal diseases

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