A plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiation

Selvarajan, Sushma; Lund, Leif R.; Takeuchi, Toshihiko; Craik, Charles S.; Werb, Zena

doi:10.1038/35060059

Cited by 149 publications

(134 citation statements)

References 52 publications

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“…This work is highly related to the pioneering work of Werb and colleagues, who studied the molecular control of mammary gland involution following the cessation of lactation (Talhouk et al, 1992;Sympson et al, 1994;Werb et al, 1996). In this model, it is clear that ECM proteolysis plays a major role in epithelial tube regression as well as the development of adipose tissue to replace this regressing tissue (Selvarajan et al, 2001). Other studies Kokorine et al, 1996) have revealed an important role of MMP-1 in, for example, the menstrual cycle and endometrial shedding, where it was shown to be hormonally regulated and to be involved in this cyclical tissue regression event.…”

Section: Capillary Tube Formation and Maintenance: A Balance Between mentioning

confidence: 97%

Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

2002

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Although many studies have focused on blood vessel development and new blood vessel formation associated with disease processes, the question of how endothelial cells (ECs) assemble into tubes in three dimensions (i.e., EC morphogenesis) remains unanswered. EC morphogenesis is particularly dependent on a signaling axis involving the extracellular matrix (ECM), integrins, and the cytoskeleton, which regulates EC shape changes and signals the pathways necessary for tube formation. Recent studies reveal that genes regulating this matrix-integrin-cytoskeletal (MIC) signaling axis are differentially expressed during EC morphogenesis. The Rho GTPases represent an important class of molecules involved in these events. Cdc42 and Rac1 are required for the process of EC intracellular vacuole formation and coalescence that regulates EC lumen formation in three-dimensional (3D) extracellular matrices, while RhoA appears to stabilize capillary tube networks. Once EC tube networks are established, supporting cells, such as pericytes, are recruited to further stabilize these networks, perhaps by regulating EC basement membrane matrix assembly. Furthermore, we consider recent work showing that EC morphogenesis is balanced by a tendency for newly formed tubes to regress. This morphogenesis-regression balance is controlled by differential gene expression of such molecules as VEGF, angiopoietin-2, and PAI-1, as well as a plasmin-and matrix metalloproteinase-dependent mechanism that induces tube regression through degradation of ECM scaffolds that support EC-lined tubes. It is our hope that this review will stimulate increased interest and effort focused on the basic mechanisms regulating capillary tube formation and regression in 3D extracellular matrices. Anat Rec 268: 252-275, 2002.

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Section: Capillary Tube Formation and Maintenance: A Balance Between mentioning

confidence: 97%

Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

2002

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“…Recent studies have indicated that matrix degradation might be essential for adipogenesis. It has been proposed that serine proteases of the plasminogen system positively regulated adipocyte differentiation in vitro, as well as in vivo during mammary gland involution (10). Other studies have demonstrated that mature fat cells and cultured adipocytes secreted gelatinases A and B (MMP-2 and MMP-9, respectively), and that their proteolytic activities were induced during adipocyte differentiation (11,12).…”

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confidence: 99%

Matrix Metalloproteinases Are Differentially Expressed in Adipose Tissue during Obesity and Modulate Adipocyte Differentiation

Chavey¹,

Mari²,

Monthouel³

et al. 2003

Journal of Biological Chemistry

400

349

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“…ECM-degrading enzymes also contribute to adipogenesis. A plasma kallikrein-dependent plasminogen cascade, as well as stromelysin 1 (matrix metalloproteinase 3) have been implicated recently in the generation of adipose tissue during mammary-gland involution (11,12). Presumably, the capacity to remodel the ECM that surrounds preadipocytes influences the differentiation of stem cells into adipocytes.…”

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confidence: 99%

SPARC-null mice exhibit increased adiposity without significant differences in overall body weight

Bradshaw

Graves

Motamed

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

194

149

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Secreted protein acidic and rich in cysteine͞osteonectin͞BM-40 (SPARC) is a matrix-associated protein that elicits changes in cell shape, inhibits cell-cycle progression, and influences the synthesis of extracellular matrix (ECM). The absence of SPARC in mice gives rise to aberrations in the structure and composition of the ECM that result in generation of cataracts, development of severe osteopenia, and accelerated closure of dermal wounds. In this report we show that SPARC-null mice have greater deposits of s.c. fat and larger epididymal fat pads in comparison with wild-type mice. Similar to earlier studies of SPARC-null dermis, we observed a reduction in collagen I in SPARC-null fat pads in comparison with wild-type. Although elevated levels of serum leptin were observed in SPARC-null mice, their overall body weights were not significantly different from those of wild-type counterparts. The diameters of adipocytes from SPARC-null versus wild-type epididymal fat pads were 252 ؎ 61 and 161 ؎ 33 m (means ؎ SD), respectively, and there was an increase in adipocyte number within SPARC-null fat pads in comparison with wild-type pads. Thus the absence of SPARC appears to result in an increase in the size of individual adipocytes as well as an increase in the number of adipocytes per fat pad. In fat pads isolated from wild-type mice, SPARC mRNA was associated with both the stromal͞vascular and adipocyte fractions. We propose that SPARC limits the accumulation of adipose tissue in mice in part through its demonstrated effects on the regulation of cell shape and production of ECM.

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A plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiation

Cited by 149 publications

References 52 publications

Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

Matrix Metalloproteinases Are Differentially Expressed in Adipose Tissue during Obesity and Modulate Adipocyte Differentiation

SPARC-null mice exhibit increased adiposity without significant differences in overall body weight

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