Identification and Characterization of a Fibroblast Growth Factor (FGF) Binding Domain in the Cysteine-rich FGF Receptor

Zhou, Zhaohui Sunny; Zuber, Michael E.; Burrus, Laura W.; Olwin, Bradley B.

doi:10.1074/jbc.272.8.5167

Cited by 26 publications

(17 citation statements)

References 55 publications

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“…Although ESL-1 primarily localizes in the Golgi apparatus, a minor portion of ESL-1 is also exported to the plasma membrane, perhaps because of differential processing of the C-terminal domain. 68 70,74 and it modulates intracellular processing and secretion of TGF-␤. 75 Consequently, mice deficient in ESL-1 show growth retardation and skeletal dysplasia.…”

Section: Leukocyte Ligands For Endothelial Selectins 6745mentioning

confidence: 99%

Leukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flow

Zarbock

Ley

McEver

et al. 2011

Blood

418

393

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Reversible interactions of glycoconjugates on leukocytes with P-and E-selectin on endothelial cells mediate tethering and rolling of leukocytes in inflamed vascular beds, the first step in their recruitment to sites of injury. Although selectin ligands on hematopoietic precursors have been identified, here we review evidence that PSGL-1, CD44, and ESL-1 on mature leukocytes are physiologic glycoprotein ligands for endothelial selectins. Each ligand has specialized adhesive functions during tethering and rolling. Furthermore, PSGL-1 and CD44 induce signals that activate the ␤2 integrin LFA-1 and promote slow rolling, whereas ESL-1 induces signals that activate the ␤2 integrin Mac-1 in adherent neutrophils. We also review evidence for glycolipids, CD43, L-selectin, and other glycoconjugates as potential physiologic ligands for endothelial selectins on neutrophils or lymphocytes. Although the physiologic characterization of these ligands has been obtained in mice, we also note reported similarities and differences with human selectin ligands. (Blood. 2011;118(26):6743-6751) IntroductionThe selectins mediate adhesion of hematopoietic cells to vascular surfaces and to each other. 1 These interactions are important for host defense, hematopoiesis, immune cell surveillance, hemostasis, and inflammation. Each of the 3 selectins is a type I transmembrane protein with an N-terminal C-type lectin domain, an epidermal growth factor-like domain, a series of consensus repeats, a transmembrane domain, and a short cytoplasmic tail. L-selectin is constitutively expressed on most leukocytes. P-selectin is rapidly mobilized from secretory granules to the plasma membranes of platelets and endothelial cells on stimulation. E-selectin expression on endothelial cells is regulated at the transcriptional level by inflammatory mediators, such as tumor necrosis factor-␣.The rolling cell adhesion mediated by selectins is a dynamic process that requires rapid formation and breakage of bonds under flow. 2 Rolling enables cells to receive signals that activate integrins, another class of adhesion receptors, which cause the cells to roll slower and to arrest. 3 Here we discuss how leukocytes, particularly neutrophils, interact with endothelial selectins during inflammation. We review evidence that surprisingly few neutrophil glycoproteins are physiologic selectin ligands, defined by their ability to mediate rolling adhesion. Rolling can be studied with flow chambers in vitro or ex vivo and in transparent tissues or by epifluorescence in vivo.The selectins are Ca 2ϩ -dependent lectins. The minimal glycan determinant for selectin binding is sialyl Lewis x (sLe x ; NeuAc␣2,3Gal␤1,4[Fuc␣1,3]GlcNAc␤1-R). 1 The fucose moiety of sLe x expressed on selectin ligands forms critical interactions with the Ca 2ϩ -coordination site on the lectin domain of selectins. 2 Leukocytes from mice lacking the 2 ␣1,3-fucosyltransferases that add fucose to form sLe x on hematopoietic cells cannot roll on Pand E-selectin. 4 Because sLe x can potentially cap N-and O-gl...

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Section: Leukocyte Ligands For Endothelial Selectins 6745mentioning

confidence: 99%

Leukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flow

Zarbock

Ley

McEver

et al. 2011

Blood

418

393

View full text Add to dashboard Cite

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“…Previously, only CFR and MG-160 have been shown to bind FGF-2 [11,15]. Zhou et al [39] have shown that CFR possibly harbours two distinct FGF-binding sites ; one of these is heparin-dependent, whereas the other is not. It is noteworthy that CFR may be implicated in FGF-2 intracellular transport [39] and in the regulation of intracellular FGF-1 and FGF-2 levels [18].…”

Section: Discussionmentioning

confidence: 99%

“…Zhou et al [39] have shown that CFR possibly harbours two distinct FGF-binding sites ; one of these is heparin-dependent, whereas the other is not. It is noteworthy that CFR may be implicated in FGF-2 intracellular transport [39] and in the regulation of intracellular FGF-1 and FGF-2 levels [18]. These interactions may be independent of the release of FGF-1 from cytosol, shown to involve synaptotagmin-1 ( [40] and references therein), or that of FGF-2 via a pathway implicating the catalytic subunit of Na + ,K + -ATPase [41].…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain

Chevet

Cailleret

Dahan

et al. 1999

Biochemical Journal

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The fibroblast growth factor (FGF) family is composed of polypeptides with sequence identity which signal through transmembrane tyrosine kinase receptors. We report here the purification from bovine brain microsomes of an FGF-2-binding complex composed of three proteins of apparent molecular masses 150 kDa, 79 kDa and 46 kDa. Only the 150 kDa and 79 kDa proteins bound FGF-2 in cross-linking and ligandblotting experiments. Binding of FGF-2 to p79 is enhanced in the presence of calcium. Peptide sequences allowed the identification of p150 and the cloning of the cDNAs encoding p79 and p46. The deduced amino acid sequence of p79 reveals high similarity to those of gastrin-binding protein and mitochondrial enoyl-

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“…We speculate that this may be related to the additional roles that E-selectin plays in the hematopoietic niche, functions that may require a more specialized ligand endowed with additional signaling properties. 15 ESL-1, which shares functional and structural homology with receptors for the fibroblast growth factor, 19,31 may thus represent a more suitable ligand in the immature compartment.…”

Section: Discussionmentioning

confidence: 99%

Coordinated and unique functions of the E-selectin ligand ESL-1 during inflammatory and hematopoietic recruitment in mice

Sreeramkumar

Leiva

Stadtmann

et al. 2013

Blood

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• ESL-1 and PSGL-1 cooperate to mediate E-selectin binding, myeloid homeostasis, and inflammatory cell recruitment.• ESL-1 dominates E-selectin binding and homing of hematopoietic progenitors.Beyond its well-established roles in mediating leukocyte rolling, E-selectin is emerging as a multifunctional receptor capable of inducing integrin activation in neutrophils, and of regulating various biological processes in hematopoietic precursors. Although these effects suggest important homeostatic contributions of this selectin in the immune and hematologic systems, the ligands responsible for transducing these effects in different leukocyte lineages are not well defined. We have characterized mice deficient in E-selectin ligand-1 (ESL-1), or in both P-selectin glycoprotein-1 (PSGL-1) and ESL-1, to explore and compare the contributions of these glycoproteins in immune and hematopoietic cell trafficking. In the steady state, ESL-1 deficiency resulted in a moderate myeloid expansion that became more prominent when both glycoproteins were eliminated. During inflammation, PSGL-1 dominated E-selectin binding, rolling, integrin activation, and extravasation of mature neutrophils, but only the combined deficiency in PSGL-1 and ESL-1 completely abrogated leukocyte recruitment. Surprisingly, we find that the levels of ESL-1 were strongly elevated in hematopoietic progenitor cells. These elevations correlated with a prominent function of ESL-1 for E-selectin binding and for migration of hematopoietic progenitor cells into the bone marrow. Our results uncover dominant roles for ESL-1 in the immature compartment, and a functional shift toward PSGL-1 dependence in mature neutrophils. (Blood. 2013;122(24): 3993-4001)

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Identification and Characterization of a Fibroblast Growth Factor (FGF) Binding Domain in the Cysteine-rich FGF Receptor

Cited by 26 publications

References 55 publications

Leukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flow

Leukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flow

Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain

Coordinated and unique functions of the E-selectin ligand ESL-1 during inflammatory and hematopoietic recruitment in mice

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