Insulin stimulates the acute release of adipsin from 3T3-L1 adipocytes

Kitagawa, Kouichiro; Rosen, Barry; Spiegelman, Bruce M.; Lienhard, Gustav E.; Tanner, L I

doi:10.1016/0167-4889(89)90244-9

Cited by 51 publications

(37 citation statements)

References 22 publications

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“…It was originally isolated as an mRNA species that was up-regulated over 200-fold during the adipocyte conversion process (38). It was also shown subsequently to be up-regulated at the protein level (39) and is secreted in two forms that differ in their glycosylation patterns, 37 and 44 kDa (40); both of these alternative forms of adipsin were identified in our study. Entactin/nidogen was another protein that we identified as an up-regulated protein.…”

Section: Figmentioning

confidence: 82%

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: Figmentioning

confidence: 82%

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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“…In AP-18, the early constitutive coexpression of PPARγ and C/EBPα might lead to the induction of expression of aP2 prior to differentiation. Adipsin is found in human plasma and is produced and secreted in vitro by human adipocytes and by differentiated 3T3-L1 cells (Kitagawa et al 1989;Baldo et al 1993), thus making this gene a marker for terminally differentiated adipocytes. Adipsin was not detected in undifferentiated AP-18 cells, however, it was expressed at day…”

Section: Discussionmentioning

confidence: 99%

A New Preadipocyte Cell Line, AP-18, Established from Adult Mouse Adipose Tissue

Doi

Nio

Takahashi

et al. 2005

Tohoku J. Exp. Med.

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Establishing preadipocyte cell lines from mature adipose tissues could help lead to a better understanding of adipogenesis. We have established a unique preadipocyte cell line, AP-18, derived from the subepidermal layer of ear skin from an adult C3H/HeM mouse. AP-18 cells exhibit fibroblast-like morphology, slow growth, and contact inhibition. The doubling time of AP-18 cells is 50-60 h, which is about 2-fold longer than that of well-known 3T3-L1 cells derived from mouse embryos. A small population of AP-18 cells spontaneously differentiates into adipocytes by 8 days after confluence, as judged by the accumulation of triglyceride droplets. Treatment of confluent AP-18 preadipocytes with adipogenic agents, containing dexamethasone, 3-methyl-1-isobutylxanthine, and insulin, increased triglyceride contents about 5-fold compared to the contents in untreated cells. We also analyzed mRNA expression profiles for key transcription factors involved in adipocyte differentiation, peroxisome proliferator-activated receptor (PPAR)γ and the CCAAT/enhancer binding protein (C/EBP) family, and for differentiation markers, aP2, adipocyte-specific fatty acid-binding protein and adipsin, adipocyte-specific serine protease. AP-18 preadipocytes express mRNAs for C/EBPβ , C/EBPα , PPARγ , and aP2 before differentiation, but not adipsin mRNA. Expression of aP2 mRNA was increased in fully differentiated AP-18 cells. Likewise, expression of adipsin mRNA was increased after induced differentiation of AP-18 cells and reached the highest level in fully differentiated adipocytes. Thus, differentiation of AP-18 cells is associated with the increased expression of aP2 and adipsin mRNAs. The newly established AP-18 cell line provides a useful model for investigating adipocyte differentiation and adipogenesis.preadipocyte; mouse; proliferation; differentiation; adipogenesis © 2005 Tohoku University Medical PressThe first cell lines capable of differentiating into adipocytes were derived from the established murine 3T3 cell line. These lines, 3T3-L1 and 3T3-F442A, were derived from immortalized embryonic fibroblast cells of mesenchymal origin and are morphologically indistinguishable from fibroblasts (Green and Meuth 1974; Kehinde 1975, 1976). Other preadipocyte cell lines have also been studied, including Ob1771 and HGFu (Negrel et al. 1978;Forest et al. 1983).

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“…Interestingly, however, adipocytes secrete a variety of other proteins such as adipsin, complement factors C3 and B, the complement-related protein Acrp30, tumor necrosis factor-␣, leptin, and others (3)(4)(5)(6). Despite the relatively large volume of vesicle traffic in adipocytes, the pathways and molecular components governing exocytosis of these factors remain undescribed.…”

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confidence: 99%

Pantophysin Is a Phosphoprotein Component of Adipocyte Transport Vesicles and Associates with GLUT4-containing Vesicles

Brooks¹,

Scherer²,

Cleveland³

et al. 2000

Journal of Biological Chemistry

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Pantophysin, a protein related to the neuroendocrinespecific synaptophysin, recently has been identified in non-neuronal tissues. In the present study, Northern blots showed that pantophysin mRNA was abundant in adipose tissue and increased during adipogenesis of 3T3-L1 cells. Immunoblot analysis of subcellular fractions showed pantophysin present exclusively in membrane fractions and relatively evenly distributed in the plasma membrane and internal membrane fractions. Sucrose gradient ultracentrifugation demonstrated that pantophysin and GLUT4 exhibited overlapping distribution profiles. Furthermore, immunopurified GLUT4 vesicles contained pantophysin, and both GLUT4 and pantophysin were depleted from this vesicle population following treatment with insulin. Additionally, a subpopulation of immunopurified pantophysin vesicles contained insulin-responsive GLUT4. Consistent with the interaction of synaptophysin with vesicle-associated membrane protein 2 in neuroendocrine tissues, pantophysin associated with vesicle-associated membrane protein 2 in adipocytes. Furthermore, in [ Adipocytes undergo agonist-stimulated exocytosis that is best characterized by the insulin-stimulated translocation of the GLUT4 glucose transporter from a unique intracellular vesicle pool to the plasma membrane (PM) 1 (1, 2). Interestingly, however, adipocytes secrete a variety of other proteins such as adipsin, complement factors C3 and B, the complement-related protein Acrp30, tumor necrosis factor-␣, leptin, and others (3-6). Despite the relatively large volume of vesicle traffic in adipocytes, the pathways and molecular components governing exocytosis of these factors remain undescribed. The transport and recycling of vesicles have been studied in depth using yeast, neuronal and neuroendocrine systems to identify molecular components involved in protein trafficking pathways, and molecular mechanisms of vesicle docking and fusion (7-9). With respect to the insulin-stimulated translocation of GLUT4 in adipocytes, several SNARE complex proteins recently have been shown to be functionally involved in the docking of GLUT4 vesicles. These include the v-SNARE VAMP2 and the t-SNAREs syntaxin-4 and synaptosome-associated protein-23 (10 -15). Potential modulators of SNARE complex formation also have been identified in adipocytes and these include several members of the Rab family of small GTP-binding proteins, members of the Munc18 family of proteins, and synaptotagmin-5 (16 -22). Adipocytes also express the N-ethylmaleimide-sensitive fusion protein and ␣-synaptosome-associated proteins involved in catalyzing vesicle membrane fusion events (23).Another potential modulator of SNARE complex formation is the integral membrane protein synaptophysin. Synaptophysin is a neuroendocrine-specific protein and is characteristically associated with synaptic vesicles as well as small vesicles in these cell types (24,25). The in vivo function of synaptophysin is unclear; however, in vitro studies suggest that synaptophysin may play a role in regulating inter...

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Insulin stimulates the acute release of adipsin from 3T3-L1 adipocytes

Cited by 51 publications

References 22 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

A New Preadipocyte Cell Line, AP-18, Established from Adult Mouse Adipose Tissue

Pantophysin Is a Phosphoprotein Component of Adipocyte Transport Vesicles and Associates with GLUT4-containing Vesicles

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