Biosynthesis and Expression of a Disintegrin-like and Metalloproteinase Domain with Thrombospondin-1 Repeats-15

Dancevic, Carolyn M.; Fraser, Fiona; Smith, Audrey; Stupka, Nicole; Ward, Alister C.; McCulloch, Daniel R.

doi:10.1074/jbc.m112.418624

Cited by 53 publications

(44 citation statements)

References 52 publications

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“…Most of the genes encoding basement membrane proteins (laminin-5 and -1, nidogen-2) and proteins that anchor ECM proteins to the basement membrane of cells (prolargin, fibulin-1 and -5, tenascin-X, transforming growth factor beta-induced protein ig-h3, cartilage oligomeric matrix protein) are expressed more in Vis ASCs. Among proteinases, the family members of a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS), i.e., Adamts-1, -5, -8, -9, and -15, which may cleave aggrecan (Verma and Dalal, 2011) or versican (Dancevic et al, 2013) and act as angiogenesis inhibitors (Vázquez et al, 1999), are expressed more in Vis than SQ ASCs (Table 1). Latent transforming growth factor beta-binding proteins are expressed more in Vis ASCs along with BMP4, which plays a key role in adipogenesis (Macotela et al, 2012) and brown fat-like phenotype (Qian et al, 2013).…”

Section: Resultsmentioning

confidence: 99%

Fat depot-specific gene signature and ECM remodeling of Sca1high adipose-derived stem cells

Tokunaga¹,

Inoue²,

Yi-bin³

et al. 2014

Matrix Biology

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Stem Cell Antigen-1 (Sca1 or Ly6A/E) is a cell surface marker that is widely expressed in mesenchymal stem cells, including adipose-derived stem cells (ASCs). We hypothesized that the fat depot-specific gene signature of Sca1high ASCs may play the major role in defining adipose tissue function and extracellular matrix (ECM) remodeling in a depot-specific manner. Herein we aimed to characterize the unique gene signature and ECM remodeling of Sca1high ASCs isolated from subcutaneous (inguinal) and visceral (epididymal) adipose tissues. Sca1high ASCs are found in the adventitia and perivascular area of adipose tissues. Sca1high ASCs purified with magnetic-activated cell sorting (MACS) demonstrate dendrite or round shape with the higher expression of cytokines and chemokines (e.g., Il6, Cxcl1) and the lower expression of a glucose transporter (Glut1). Subcutaneous and visceral fat-derived Sca1high ASCs particularly differ in the gene expressions of adhesion and ECM molecules. While the expression of the major membrane-type collagenase (MMP14) is comparable between the groups, the expressions of secreted collagenases (MMP8 and MMP13) are higher in visceral Sca1high ASCs than subcutaneous ASCs. Consistently, slow but focal MMP-dependent collagenolysis was observed with subcutaneous Sca1high ASCs, whereas rapid and bulk collagenolysis was observed with visceral Sca1high ASCs in MMP-dependent and –independent manners. These results suggest that the fat depot-specific gene signatures of ASCs may contribute to the distinct patterns of ECM remodeling and adipose function in different fat depots.

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Section: Resultsmentioning

confidence: 99%

Fat depot-specific gene signature and ECM remodeling of Sca1high adipose-derived stem cells

Tokunaga¹,

Inoue²,

Yi-bin³

et al. 2014

Matrix Biology

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“…54 Proteolytic processing of versican occurs by several different members of the ADAMTS (A Disintegrin-like and Metalloproteinase with Thrombospondin-1 motifs) family of enzymes. ADAMTS-1, -4, -5, -9, -15, and -20 have all been demonstrated to cleave versican [55][56][57][58] and by homology, ADAMTS-8 is presumed to also. This cluster of ADAMTS enzymes represents slightly less than half of the ADAMTS family and is considered the proteoglycan cleaving 'super-clade'.…”

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confidence: 99%

Versican: a novel modulator of hepatic fibrosis

Bukong

Maurice

Chahal

et al. 2016

Laboratory Investigation

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Little is known about the deposition and turnover of proteoglycans in liver fibrosis, despite their abundance in the extracellular matrix. Versican plays diverse roles in modulating cell behavior in other fibroproliferative diseases, but remains poorly described in the liver. Hepatic fibrosis was induced by carbon tetrachloride treatment of C57BL/6 mice over 4 weeks followed by recovery over a 28-day period. Primary mouse hepatic stellate cells (HSCs) were activated in culture and versican was transiently knocked down in human (LX2) and mouse HSCs. Expression of versican, A Disintegrinlike and Metalloproteinase with Thrombospondin-1 motifs (ADAMTS)-1, -4, -5, -8, -9, -15, and -20, and markers of fibrogenesis were studied using immunohistochemistry, real-time quantitative PCR, and western blotting. Immunohistochemistry showed increased expression of versican in cirrhotic human livers and the mouse model of fibrosis. Carbon tetrachloride treatment led to significant increases in versican expression and the proteoglycanases ADAMTS-5, -9, -15, and -20, alongside TNF-α, α-smooth muscle actin (α-SMA), collagen-1, and TGF-β expression. During recovery, expression of many of these genes returned to control levels. However, expression of ADAMTS-5, -8, -9, and -15 showed delayed increases in expression at 28 days of recovery, which corresponded with decreases in versican V0 and V1 cleavage products (G1-DPEAAE 1401 and G1-DPEAAE 441 ). Activation of primary HSCs in vitro significantly increased versican, α-SMA, and collagen-1 expression. Transient knockdown of versican in HSCs led to decreases in markers of fibrogenesis and reduced cell proliferation, without inducing apoptosis. Versican expression increases during HSC activation and liver fibrosis, and proteolytic processing occurs during the resolution of fibrosis. Knockdown studies in vitro suggest a possible role of versican in modulating hepatic fibrogenesis.

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“…Subsequently, ADAMTS5, ADAMTS9, ADAMTS15, and ADAMTS20 have been found to cleave this site (41)(42)(43). Analysis of mice lacking Adamts1, Adamts5, Adamts9, and Adamts20 identified anomalies in ovulation, interdigital web regression, skin pigmentation, cardiac development, and palate formation that were associated with reduced versican processing (16, 17, 19, 33, 44 -48).…”

mentioning

confidence: 99%

Determinants of Versican-V1 Proteoglycan Processing by the Metalloproteinase ADAMTS5

Foulcer

Nelson

Quintero

et al. 2014

Journal of Biological Chemistry

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Background:The mechanisms of versican proteolysis by ADAMTS proteases are unknown. Results: The ADAMTS5 ancillary domain and specific chondroitin sulfate chains of versican are required for proteolysis. Conclusion: Docking between the ADAMTS5 ancillary domain and CS chains is a major mechanism underlying versican proteolysis. Proteolysis by ADAMTS1 has a similar requirement for GAG chains. Significance: The findings suggest strategies for blocking versican cleavage.

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Biosynthesis and Expression of a Disintegrin-like and Metalloproteinase Domain with Thrombospondin-1 Repeats-15

Cited by 53 publications

References 52 publications

Fat depot-specific gene signature and ECM remodeling of Sca1high adipose-derived stem cells

Fat depot-specific gene signature and ECM remodeling of Sca1high adipose-derived stem cells

Versican: a novel modulator of hepatic fibrosis

Determinants of Versican-V1 Proteoglycan Processing by the Metalloproteinase ADAMTS5

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