Regulation of fibronectin, integrin and cytoskeleton expression in differentiating adipocytes: inhibition by extracellular matrix and polylysine

Fernández, José Luis Rodríguez; Ben-Ze’ev, Avri

doi:10.1111/j.1432-0436.1989.tb00608.x

Cited by 121 publications

(52 citation statements)

References 49 publications

(33 reference statements)

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“…3 shows the spectra that were obtained by tandem mass spectrometric analysis. We identi-fied fibronectin as a down-regulated protein (band 1) that has been shown previously to be down-regulated at the mRNA level (28,29). Down-regulation of fibronectin at the protein level was demonstrated recently and shown to be critical for adipocyte differentiation (30).…”

Section: Identification Of Secreted Molecules That Are Differentiallymentioning

confidence: 89%

A Proteomic Approach for Identification of Secreted Proteins during the Differentiation of 3T3-L1 Preadipocytes to Adipocytes

Kratchmarova

Kalume

Blagoev

et al. 2002

Molecular & Cellular Proteomics

236

187

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We have undertaken a systematic proteomic approach to purify and identify secreted factors that are differentially expressed in preadipocytes versus adipocytes. Using one-dimensional gel electrophoresis combined with nanoelectrospray tandem mass spectrometry, proteins that were specifically secreted by 3T3-L1 preadipocytes or adipocytes were identified. In addition to a number of previously reported molecules that are up-or down-regulated during this differentiation process (adipsin, adipocyte complement-related protein 30 kDa, complement C3, and fibronectin), we identified four secreted molecules that have not been shown previously to be expressed differentially during the process of adipogenesis. Pigment epithelium-derived factor, a soluble molecule with potent antiangiogenic properties, was found to be highly secreted by preadipocytes but not adipocytes. Conversely, we found hippocampal cholinergic neurostimulating peptide, neutrophil gelatinase-associated lipocalin, and haptoglobin to be expressed highly by mature adipocytes. We also used liquid chromatography-based separation followed by automated tandem mass spectrometry to identify proteins secreted by mature adipocytes. Several additional secreted proteins including resistin, secreted acidic cysteine-rich glycoprotein/osteonectin, stromal cell-derived factor-1, cystatin C, gelsolin, and matrix metalloprotease-2 were identified by this method. To our knowledge, this is the first study to identify several novel secreted proteins by adipocytes by a proteomic approach using mass spectrometry. Molecular & Cellular Proteomics 1:213-222, 2002.

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Section: Identification Of Secreted Molecules That Are Differentiallymentioning

confidence: 89%

A Proteomic Approach for Identification of Secreted Proteins during the Differentiation of 3T3-L1 Preadipocytes to Adipocytes

Kratchmarova

Kalume

Blagoev

et al. 2002

Molecular & Cellular Proteomics

236

187

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“…We have studied a-actinin, since it is a major component involved in microfilament stabilization and in linking microfilaments to AJs (34). In addition, a-actinin expression is modulated during growth activation and differentiation (21)(22)(23)(24) and is significantly decreased in SVT2 cells. The relationship between a-actinin expression and the tumorigenic phenotype was addressed directly by elevating a-actinin levels in tumor cells that express diminished amounts of this protein.…”

Section: Discussionmentioning

confidence: 99%

Suppression of tumorigenicity in simian virus 40-transformed 3T3 cells transfected with alpha-actinin cDNA.

Glück

Kwiatkowski

Ben-Ze’ev

1993

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

140

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Human cytoskeletal a-actinin cDNA was transfected into highly malignant simian virus 40-transformed BALB/c 3T3 (SVT2) cells that express 6-fold lower levels of a-actinin than nontransformed BALB/c 3T3 cells. SVT2 clones expressing various levels of a-actinin were isolated and their structure and tumorigenic properties were determined. Transfected SVT2 clones expressing a-actinin at levels found in nontumorigenic 3T3 cells displayed a flatter phenotype, a decreased ability to grow in suspension culture in soft agar, and a marked reduction in their ability to form tumors in syngeneic BALB/c mice and in athymic nude mice. Clones overexpressing a-actinin at the highest level (about 2-fold higher than 3T3 cells) were completely suppressed in their ability to form tumors in syngeneic BALB/c mice. The results suggest that a-actinin, an actin-crosslinking protein that is also localized in cell junctions, may have an effective suppressive ability on the transformed phenotype.Malignant transformation of cells is characterized by alterations in cell growth, adhesion, motility, and cell shape (1). Among the more conspicuous morphological alterations in transformed cells are a round phenotype and a decrease in the number of microfilament bundles (2, 3). The disorganization of the actin filaments in transformed cells is often associated with a reduced expression of microfilament proteins such as tropomyosin (4), gelsolin (5), and vinculin (6). These changes in microfilaments correlate with the ability of cells to grow in suspension in semisolid medium (7).Previous studies have demonstrated a reversion in the transformed phenotype of cancer cells in the presence of a variety of agents and a return to the original malignant behavior upon their removal (8). This "reverse transformation" includes a reversible modulation in cell shape and the organization of the cytoskeleton (9). However, the relationships between the changes in growth properties and the altered cell structure of transformed cells are still unknown (10). Do the characteristic changes in cell morphology of transformed cells result from alterations in the rate of growth or are changes in cell adhesion and cytostructure responsible for disruption of the adhesion-dependent growth control? In this study we addressed this question directly by modulating the expression ofa single actin-associated protein a-actinin in a tumorigenic cell line and determined the consequences of altered a-actinin expression on the phenotype of the cells. a-Actinin is an abundant cytoplasmic actin-binding protein (11) that crosslinks actin filaments in vitro and is found in both muscle and nonmuscle cells (12,13). In striated muscle cells, a-actinin is localized in Z-disks; in smooth muscle cells, it is in dense plaques; and in nonmuscle cells, a-actinin is found along microfilaments (14) and in adherens junctions (AJs), at sites where actin filaments attach to the membrane (15)(16)(17). The role of a-actinin in mediating actin attachment to the membrane is not completely understood. ...

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“…Some of these modulating factors that are pertinent to the diabetic context include insulin, 47,48 insulin-like growth factor-1 (IGF-1), 49 extracellular proteins including collagen and fibronectin, 50,51 and tumor necrosis factor-a (TNF-a). 52,53 Shifts in the expression or function of these and other effectors disrupt the homeostatic balance between adipogenic and osteogenic differentiation of MPCs.…”

Section: Mechanisms Of Enhanced Marrow Adipogenesis In Diabetesmentioning

confidence: 99%

Pathophysiological role of enhanced bone marrow adipogenesis in diabetic complications

Piccinin

Khan

2014

Adipocyte

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Regulation of fibronectin, integrin and cytoskeleton expression in differentiating adipocytes: inhibition by extracellular matrix and polylysine

Cited by 121 publications

References 49 publications

A Proteomic Approach for Identification of Secreted Proteins during the Differentiation of 3T3-L1 Preadipocytes to Adipocytes

A Proteomic Approach for Identification of Secreted Proteins during the Differentiation of 3T3-L1 Preadipocytes to Adipocytes

Suppression of tumorigenicity in simian virus 40-transformed 3T3 cells transfected with alpha-actinin cDNA.

Pathophysiological role of enhanced bone marrow adipogenesis in diabetic complications

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