Identification of a cysteine-rich receptor for fibroblast growth factors.

Burrus, Laura W.; Zuber, Michael E.; Lueddecke, B A; Olwin, Bradley B.

doi:10.1128/mcb.12.12.5600

Cited by 108 publications

(72 citation statements)

References 67 publications

(54 reference statements)

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“…The PAM-1 receptor was found to be a M r 130,000 integral membrane glycoprotein (15), homologous to cysteine-rich fibroblast growth factor receptor 1 (25). This post-transcriptionally modified receptor is expressed on nearly all epithelial cancers of every type and origin, but not on healthy tissue.…”

Section: Introductionmentioning

confidence: 99%

Lipoptosis

et al. 2004

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A balanced lipid metabolism is crucial for all cells. Disturbance of this homeostasis by nonphysiological intracellular accumulation of fatty acids can result in apoptosis. This was proven in animal studies and was correlated to some human diseases, like lipotoxic cardiomyopathy. Some metabolic mechanisms of lipo-apoptosis were described, and some causes were discussed, but reagents, which directly induce lipo-apoptosis, have thus far not been identified. The human monoclonal IgM antibody SAM-6 was isolated from a stomach cancer patient by using the conventional human hybridoma technology (trioma technique). The addition of SAM-6 to tumor cells leads to an increase in the intracellular accumulation of neutral lipids, followed by tumor cell apoptosis. The antibody SAM-6 does not react with noncancerous human epithelial and fibroblastic cells, because the M r 140,000 membrane molecule, recognized by the antibody, is specifically expressed on human malignant cells. The antibody is coded by the germ-line genes IgHV3-30.3*01 and IgLV3-1*01 and is a component of the innate immunity to cancer. In this article, we describe an antibodyinduced tumor-specific cell death, named lipoptosis. This is, to our knowledge, the first description of this specific form of lipo-apoptosis as an antibody-mediated mechanism of tumor cell killing.

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Section: Introductionmentioning

confidence: 99%

Lipoptosis

et al. 2004

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“…Despite the femtomole amount of the protein digest consumed for MALDI analysis, a database search matched 35 peptides to the CFR-1 sequence with a mass accuracy within 50 ppm. These peptides cover 29% of the CFR-1 sequence, thus definitively identifying the protein, which has a calculated molecular weight of approximately 134 kd (Burrus et al, 1992) (Fig. 1b).…”

Section: Purification and Identification Of Antigen 103/51mentioning

confidence: 96%

A Novel Proliferation-Associated Variant of CFR-1 Defined by a Human Monoclonal Antibody

Hensel

Brändlein

Eck

et al. 2001

Laboratory Investigation

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SUMMARY:The germline coded human monoclonal IgM antibody 103/51 was isolated from a gastric carcinoma patient. This antibody binds to a 130-kd membrane molecule and has a mitotic effect on tumor cells in vitro. To characterize the target, we sequenced the protein and showed that the antibody binds to the cysteine-rich fibroblast growth factor receptor (CFR)-1, which is highly homologous to MG-160 and the E-selectin-ligand (ESL)-1. The epitope was determined by glycosidase-digestion experiments to be an N-linked carbohydrate side chain. Immunohistochemistry was used to investigate the tissue distribution of CFR-1. Different healthy tissues were tested and only the collecting tubes of the kidney, the Golgi apparatus, and the glomerular and fascicular zones of the adrenal gland stained positive. However, on malignant tissue the receptor is overexpressed in nearly all tested stomach cancers (12 of 15) and other tested carcinomas (13 of 15). Most interestingly, the receptor is also present in Helicobacter pylori gastritis and gastric dysplasia, but absent on uninflamed stomach mucosa. This restricted tissue pattern indicates that antibody 103/51 reacts with a membrane-bound variant of CFR-1, which is mainly expressed on transformed cells and precursor lesions and is essential for proliferation processes. The possible activity of antibody 103/51 as an activating ligand in these proliferative changes of gastric epithelial mucosa is discussed. (Lab Invest 2001, 81:1097-1108.

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“…We previously reported that E-selectin ligand-1 (ESL-1) (also referred to as Cysteine-rich fibroblast growth factor receptor, golgi apparatus protein 1, Latent TGF-β complexed protein-1 or MG160) (15)(16)(17)(18) is an important regulator of TGF-β maturation in the Golgi apparatus during cartilage homeostasis (19). Loss of ESL-1 in mice led to accelerated TGF-β maturation and elevated TGF-β signaling in the growth plate.…”

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confidence: 99%

E-selectin ligand 1 regulates bone remodeling by limiting bioactive TGF-β in the bone microenvironment

Yang

Grafe

Bae

et al. 2013

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

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TGF-β is abundantly produced in the skeletal system and plays a crucial role in skeletal homeostasis. E-selectin ligand-1 (ESL-1), a Golgi apparatus-localized protein, acts as a negative regulator of TGF-β bioavailability by attenuating maturation of pro-TGF-β during cartilage homeostasis. However, whether regulation of intracellular TGF-β maturation by ESL-1 is also crucial during bone homeostasis has not been well defined. Here, we show that Esl-1 −/− mice exhibit a severe osteopenia with elevated bone resorption and decreased bone mineralization. In primary culture, Esl-1 −/− osteoclast progenitors show no difference in osteoclastogenesis. However, Esl-1 −/− osteoblasts show delayed differentiation and mineralization and stimulate osteoclastogenesis more potently in the osteoblast-osteoclast coculture, suggesting that ESL-1 primarily acts in osteoblasts to regulate bone homeostasis. In addition, Esl-1 −/− calvaria exhibit an elevated mature TGF-β/pro-TGF-β ratio, with increased expression of TGF-β downstream targets (plasminogen activator inhibitor-1, parathyroid hormone-related peptide, connective tissue growth factor, and matrix metallopeptidase 13, etc.) and a key regulator of osteoclastogenesis (receptor activator of nuclear factor κB ligand). Moreover, in vivo treatment with 1D11, a pan-TGF-β antibody, significantly improved the low bone mass of Esl-1 −/− mice, suggesting that elevated TGF-β signaling is the major cause of osteopenia in Esl-1 −/− mice. In summary, our study identifies ESL-1 as an important regulator of bone remodeling and demonstrates that the modulation of TGF-β maturation is pivotal in the maintenance of a homeostatic bone microenvironment and for proper osteoblast-osteoclast coupling.1D11 antibody | osteoblast mineralization | osteoporosis

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Identification of a cysteine-rich receptor for fibroblast growth factors.

Cited by 108 publications

References 67 publications

Lipoptosis

Lipoptosis

A Novel Proliferation-Associated Variant of CFR-1 Defined by a Human Monoclonal Antibody

E-selectin ligand 1 regulates bone remodeling by limiting bioactive TGF-β in the bone microenvironment

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