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Journal articles on the topic 'Soluble factor'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Carli, A. "Lipid-soluble cardiodepressant factor vs. water-soluble myocardial depressant factor-like substances in shock." American Journal of Physiology-Heart and Circulatory Physiology 261, no. 6 (December 1, 1991): H2100—H2102. http://dx.doi.org/10.1152/ajpheart.1991.261.6.h2100.

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2

Dale, B. "Sperm-induced calcium oscillations: Soluble factor, factors or receptors?" Molecular Human Reproduction 5, no. 1 (January 1, 1999): 1–4. http://dx.doi.org/10.1093/molehr/5.1.1.

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3

Godfried, Mieke H., Tom van der Poll, Jaap Jansen, Johannes A. Romijin, Jan K. M. Eeftinck Schattenkerk, Erik Endert, Sander J. H. van Deventer, and Hans P. Sauerwein. "Soluble receptors for tumour necrosis factor." AIDS 7, no. 1 (January 1993): 33–36. http://dx.doi.org/10.1097/00002030-199301000-00005.

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4

Ott, Ilka. "Soluble Tissue Factor Emerges From Inflammation." Circulation Research 96, no. 12 (June 24, 2005): 1217–18. http://dx.doi.org/10.1161/01.res.0000172745.09928.87.

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5

Reibnegger, Gilbert, Antonio Diez-Ruiz, Dietmar Fuchs, and Helmut Wachter. "Soluble tumour necrosis factor receptors as prognostic factors in cancer." Lancet 344, no. 8923 (September 1994): 681–82. http://dx.doi.org/10.1016/s0140-6736(94)92115-6.

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6

SOEJIMA, Kenji, Jun MIZUGUCHI, and Sadaaki IWANAGA. "Crystal Structures of Soluble Tissue Factor and Factor VIIa-Tissue Factor Complex." Japanese Journal of Thrombosis and Hemostasis 10, no. 2/3 (1999): 204–11. http://dx.doi.org/10.2491/jjsth.10.204.

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7

Rosen, E. M., A. Joseph, L. Jin, S. Rockwell, J. A. Elias, J. Knesel, J. Wines, J. McClellan, M. J. Kluger, and I. D. Goldberg. "Regulation of scatter factor production via a soluble inducing factor." Journal of Cell Biology 127, no. 1 (October 1, 1994): 225–34. http://dx.doi.org/10.1083/jcb.127.1.225.

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Scatter factor (SF) (also known as hepatocyte growth factor [HGF]) is a fibroblast-derived cytokine that stimulates motility, proliferation, and morphogenesis of epithelia. SF may play major roles in development, repair, and carcinogenesis. However, the physiologic signals that regulate its production are not well delineated. We found that various human tumor cell lines that do not produce SF secrete factors that stimulate SF production by fibroblasts, suggesting a paracrine mechanism for regulation of SF production. Conditioned medium from these cell lines contained two distinct scatter factor-inducing factor SF-IF activities: a high molecular weight (> 30 kD), heat sensitive activity and a low molecular weight (< 30 kD) heat stable activity. Further studies revealed that SF-producing fibroblasts also secrete factors that stimulate their own SF production. We characterized the < 30-kD SF-IF activity from ras-3T3 (clone D4), a mouse cell line that overproduces both SF and SF-IF. The < 30-kD filtrate from ras-3T3 conditioned medium induced four- to sixfold increases in expression of SF biologic activity, immunoreactive protein, and mRNA by multiple SF-producing fibroblast lines. Ras-3T3 SF-IF activity was stable to boiling, extremes of pH, and reductive alkylation, but was destroyed by proteases. We purified ras-3T3 SF-IF about 10,000-fold from serum-free conditioned medium by a combination of ultrafiltration, cation exchange chromatography, and reverse phase chromatography. The purified protein exhibited electrophoretic mobility of about 12 kD (reduced) and 14 kD (nonreduced) by SDS-PAGE. The identity of the protein was verified by elution of biologic activity from gel slices. Purified SF-IF stimulated SF production in a physiologic concentration range (about 20-400 pM). Its properties and activities were distinct from those of IL-1 and TNF, two known inducers of SF production. We suggest that SF-IF is a physiologic regulator of SF production.

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8

LANGKOPF, F. "Soluble tumour necrosis factor receptors as prognostic factors in cancer patients." Lancet 344, no. 8914 (July 1994): 57–58. http://dx.doi.org/10.1016/s0140-6736(94)91078-2.

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9

Langley, KE, LG Bennett, J. Wypych, SA Yancik, XD Liu, KR Westcott, DG Chang, KA Smith, and KM Zsebo. "Soluble stem cell factor in human serum." Blood 81, no. 3 (February 1, 1993): 656–60. http://dx.doi.org/10.1182/blood.v81.3.656.656.

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Abstract Stem cell factor (SCF) is a recently described factor active in the early stages of hematopoiesis. It can exist in membrane-bound form and in proteolytically released soluble form. The levels and nature of SCF in human serum are described. As determined by an enzyme-linked immunosorbent assay performed for 257 samples, SCF level in serum averaged 3.3 +/- 1.1 ng/mL. The serum SCF was partially purified by immunoaffinity chromatography and analyzed by glycosidase treatments in conjunction with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting. The results show that the SCF has N- linked and O-linked carbohydrate and corresponds to the soluble form, at or about 165 amino acids in length. The findings suggest functional importance for soluble SCF in humans.

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10

Langley, KE, LG Bennett, J. Wypych, SA Yancik, XD Liu, KR Westcott, DG Chang, KA Smith, and KM Zsebo. "Soluble stem cell factor in human serum." Blood 81, no. 3 (February 1, 1993): 656–60. http://dx.doi.org/10.1182/blood.v81.3.656.bloodjournal813656.

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Stem cell factor (SCF) is a recently described factor active in the early stages of hematopoiesis. It can exist in membrane-bound form and in proteolytically released soluble form. The levels and nature of SCF in human serum are described. As determined by an enzyme-linked immunosorbent assay performed for 257 samples, SCF level in serum averaged 3.3 +/- 1.1 ng/mL. The serum SCF was partially purified by immunoaffinity chromatography and analyzed by glycosidase treatments in conjunction with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting. The results show that the SCF has N- linked and O-linked carbohydrate and corresponds to the soluble form, at or about 165 amino acids in length. The findings suggest functional importance for soluble SCF in humans.

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11

TOSCHI, V. "Soluble tissue factor and tissue factor pathway inhibitor in cardiovascular disease." Journal of Thrombosis and Haemostasis 5, no. 3 (March 2007): 472–74. http://dx.doi.org/10.1111/j.1538-7836.2007.02402.x.

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12

Laan, M. P., H. Koning, M. R. M. Baert, A. P. Oranje, W. A. Buurman, H. F. J. Savelkoul, and H. J. Neijens. "Levels of soluble intercellular adhesion molecule-1, soluble E-selectin, tumor necrosis factor-?, and soluble tumor necrosis factor receptor p55 and p75 in atopic children." Allergy 53, no. 1 (January 1998): 51–58. http://dx.doi.org/10.1111/j.1398-9995.1998.tb03773.x.

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13

TAKEMURA, TSUKASA, SATOSHI HINO, HIROAKI KUWAJIMA, HIDEHIKO YANAGIDA, MITSURU OKADA, MICHIO NAGATA, SEI SASAKI, JONATHAN BARASCH, RAYMOND C. HARRIS, and KAZUO YOSHIOKA. "Induction of Collecting Duct MorphogenesisIn Vitroby Heparin-Binding Epidermal Growth Factor-Like Growth Factor." Journal of the American Society of Nephrology 12, no. 5 (May 2001): 964–72. http://dx.doi.org/10.1681/asn.v125964.

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Abstract. Heparin-binding epidermal growth factor-like growth factor (HB-EGF), a member of the epidermal growth factor family of growth factors, is synthesized as a membrane-an-chored precursor (proHB-EGF) that is capable of stimulating adjacent cells in a juxtacrine manner. ProHB-EGF is cleaved in a protein kinase C-dependent process, to yield the soluble form. It was observed that HB-EGF acts as a morphogen for the collecting duct system in developing kidneys. HB-EGF protein was expressed in the ureteric bud of embryonic kidneys. Cultured mouse ureteric bud cells (UBC) produced HB-EGF via protein kinase C activation. After stimulation with phorbol ester (12-O-tetradecanoylphorbol-13-acetate) or recombinant soluble HB-EGF, UBC cultured in three-dimensional collagen gels formed short tubules with varied abundant branches. When proHB-EGF-transfected UBC were stimulated with 12-O-tetradecanoylphorbol-13-acetate and cultured in collagen gels, they exhibited linear growth, forming long tubular structures with few branches at the time of appearance of proHB-EGF on the cell surface. The structures exhibited a strong resemblance to the early branching ureteric bud of embryonic kidneys. When UBC were cultured in the presence of transforming growth factor-β and soluble HB-EGF, they formed long tubules and few branches, similar to the structures observed in proHB-EGF-transfected UBC. These cells exhibited apical-basolateral polarization and expression of the water channel aquaporin-2. These findings indicate that soluble HB-EGF and proHB-EGF induce branching tubulogenesis in UBC in different ways. Juxtacrine activation by proHB-EGF or the synergic action of soluble HB-EGF with transforming growth factor-β is important for well balanced morphogenesis of the collecting duct system.

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14

Mostafavi, Mohammad, Paul C. Stein, and C. Lowell Parsons. "Production of Soluble Virulence Factor by Escherichia Coli." Journal of Urology 153, no. 5 (May 1995): 1441–43. http://dx.doi.org/10.1016/s0022-5347(01)67426-3.

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15

Ivanovska, Irena L., Joe Swift, Kyle Spinler, Dave Dingal, and Dennis E. Discher. "Matrix and Soluble Factor Pathways to Lineage Specification." Biophysical Journal 110, no. 3 (February 2016): 95a. http://dx.doi.org/10.1016/j.bpj.2015.11.570.

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16

Andalas, Mohd, and Harahap Harahap. "Antagonis Soluble Fms-Like Tyrosine Kinase 1 (sFlt-1) dan Soluble Endoglin (sEng) pada Preeklamsia." Jurnal Ilmu Kedokteran 4, no. 1 (November 23, 2017): 1. http://dx.doi.org/10.26891/jik.v4i1.2010.1-9.

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Proangiogenic factor signal transduction like vascular endothelial growth factor (VEGF), placental growth factor(PlGF) and tissue growth factor â-1 (TGFâ-1) are important to angiogenesis and vascular health in pregnancy. Inpreeclampsia (PE) concentration of fms-like tyrosine kinase-1 (sFlt-1) and soluble endoglin (sEng) are increasesignificantly. Base on analysis from resent research shown that sFlt-1 and sEng inhibit angiogenic factor signaltransduction by competition - in result angiogenic factor can‘t bind to their receptor. sFlt-1 and sEng are potential usedas preeclampsia therapy because sFlt-1 and sEng have main role in PE pathogenesis. We suggest that the research tofind out effective sFlt-1 and sEng antagonist have to conduct in the next time.

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17

Perucci, Luiza O., Karina B. Gomes, Letícia G. Freitas, Lara C. Godoi, Patrícia N. Alpoim, Melina B. Pinheiro, Aline S. Miranda, Antônio L. Teixeira, Luci M. Dusse, and Lirlândia P. Sousa. "Soluble Endoglin, Transforming Growth Factor-Beta 1 and Soluble Tumor Necrosis Factor Alpha Receptors in Different Clinical Manifestations of Preeclampsia." PLoS ONE 9, no. 5 (May 22, 2014): e97632. http://dx.doi.org/10.1371/journal.pone.0097632.

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18

Lim, Hoong Sern, Andrew D. Blann, and Gregory Y. H. Lip. "Soluble CD40 Ligand, Soluble P-Selectin, Interleukin-6, and Tissue Factor in Diabetes Mellitus." Circulation 109, no. 21 (June 2004): 2524–28. http://dx.doi.org/10.1161/01.cir.0000129773.70647.94.

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19

Watts, RG, and TH Howard. "Mechanisms for actin reorganization in chemotactic factor-activated polymorphonuclear leukocytes." Blood 81, no. 10 (May 15, 1993): 2750–57. http://dx.doi.org/10.1182/blood.v81.10.2750.2750.

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Abstract Cytoskeletal structure in polymorphonuclear leukocytes (PMNs) is thought to reflect a simple equilibrium between two actin pools (globular [G]- and filamentous [F] actin). Recent description of two distinct F-actin pools in PMNs (Triton-insoluble [stable] and Triton- soluble [labile] F-actin pools) (Watts and Howard, Cell Motil Cytoskeleton, 21:25, 1992) suggest a tripartite equilibrium between these F-actin pools and G-actin and multiple possible mechanisms for polymerization. To study the contribution of each actin pool to actin dynamics in PMNs, changes in actin content of the Triton-soluble and - insoluble F-actin pools and G-actin in chemotactic factor (CTF)- activated PMNs were measured by NBDphallacidin binding and by gel scans of Triton-lysed PMNs. From 0 to 30 seconds after CTF activation, PMNs rapidly increase total (Triton-soluble + Triton-insoluble) F-actin content (maximum = 1.7- +/- 0.10-fold basal at 30 seconds). Concurrent measures of the actin content of individual actin pools (Triton-soluble and -insoluble F-actin and G-actin) show that at all times (0 to 30 seconds) only the Triton-insoluble F-actin pool grows (maximum = 2.81- +/- 0.73-fold basal at 30 seconds), whereas both the Triton-soluble and G-actin pools simultaneously decrease (50% decrease at 30 seconds). Concurrent growth of one F-actin pool (Triton-insoluble) and loss of another F-actin pool (Triton-soluble) emphasize the functional uniqueness of the F-actin pools and can occur only if the Triton- soluble F-actin anneals or cross-links filament-to-filament with the Triton-insoluble fraction or if the Triton-insoluble F-actin pool first depolymerizes to monomer, which is then added to the Triton-insoluble pool. Because from 0 to 30 seconds after FMLP activation G-actin never increases, but, like the Triton-soluble F-actin progressively decreases, the results suggest that F-actin growth results from simultaneous new filament growth by monomer addition to the Triton- insoluble F-actin and cytoskeletal remodelling by Triton-soluble F- actin annealing or cross-linking to Triton-insoluble F-actin. These findings offer important new insights into the mechanism(s) of actin polymerization in CTF-activated human PMNs.

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20

Watts, RG, and TH Howard. "Mechanisms for actin reorganization in chemotactic factor-activated polymorphonuclear leukocytes." Blood 81, no. 10 (May 15, 1993): 2750–57. http://dx.doi.org/10.1182/blood.v81.10.2750.bloodjournal81102750.

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Cytoskeletal structure in polymorphonuclear leukocytes (PMNs) is thought to reflect a simple equilibrium between two actin pools (globular [G]- and filamentous [F] actin). Recent description of two distinct F-actin pools in PMNs (Triton-insoluble [stable] and Triton- soluble [labile] F-actin pools) (Watts and Howard, Cell Motil Cytoskeleton, 21:25, 1992) suggest a tripartite equilibrium between these F-actin pools and G-actin and multiple possible mechanisms for polymerization. To study the contribution of each actin pool to actin dynamics in PMNs, changes in actin content of the Triton-soluble and - insoluble F-actin pools and G-actin in chemotactic factor (CTF)- activated PMNs were measured by NBDphallacidin binding and by gel scans of Triton-lysed PMNs. From 0 to 30 seconds after CTF activation, PMNs rapidly increase total (Triton-soluble + Triton-insoluble) F-actin content (maximum = 1.7- +/- 0.10-fold basal at 30 seconds). Concurrent measures of the actin content of individual actin pools (Triton-soluble and -insoluble F-actin and G-actin) show that at all times (0 to 30 seconds) only the Triton-insoluble F-actin pool grows (maximum = 2.81- +/- 0.73-fold basal at 30 seconds), whereas both the Triton-soluble and G-actin pools simultaneously decrease (50% decrease at 30 seconds). Concurrent growth of one F-actin pool (Triton-insoluble) and loss of another F-actin pool (Triton-soluble) emphasize the functional uniqueness of the F-actin pools and can occur only if the Triton- soluble F-actin anneals or cross-links filament-to-filament with the Triton-insoluble fraction or if the Triton-insoluble F-actin pool first depolymerizes to monomer, which is then added to the Triton-insoluble pool. Because from 0 to 30 seconds after FMLP activation G-actin never increases, but, like the Triton-soluble F-actin progressively decreases, the results suggest that F-actin growth results from simultaneous new filament growth by monomer addition to the Triton- insoluble F-actin and cytoskeletal remodelling by Triton-soluble F- actin annealing or cross-linking to Triton-insoluble F-actin. These findings offer important new insights into the mechanism(s) of actin polymerization in CTF-activated human PMNs.

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21

Ballester-Bolinches, A., R. Esteban-Romero, and M. C. Pedraza-Aguilera. "On a Class of p-Soluble Groups." Algebra Colloquium 12, no. 02 (June 2005): 263–67. http://dx.doi.org/10.1142/s1005386705000258.

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Let p be a prime. The class of all p-soluble groups G such that every p-chief factor of G is cyclic and all p-chief factors of G are G-isomorphic is studied in this paper. Some results on T-, PT-, and PST-groups are also obtained.

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22

Ogawa, Tadashi, Koichi Takayama, Nobuyuki Takakura, Seigo Kitano, and Hikaru Ueno. "Anti-tumor angiogenesis therapy using soluble receptors: enhanced inhibition of tumor growth when soluble fibroblast growth factor receptor-1 is used with soluble vascular endothelial growth factor receptor." Cancer Gene Therapy 9, no. 8 (July 24, 2002): 633–40. http://dx.doi.org/10.1038/sj.cgt.7700478.

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23

Viac, J., C. Vincent, S. Palacio, D. Schmitt, and A. Claudy. "Tumour necrosis factor (TNF) soluble receptors in malignant melanoma: Correlation with soluble ICAM-1 level." European Journal of Cancer 32, no. 3 (March 1996): 447–49. http://dx.doi.org/10.1016/0959-8049(95)00541-2.

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24

Lee, Geoffrey F., and Robert F. Kelley. "A Novel Soluble Tissue Factor Variant with an Altered Factor VIIa Binding Interface." Journal of Biological Chemistry 273, no. 7 (February 13, 1998): 4149–54. http://dx.doi.org/10.1074/jbc.273.7.4149.

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25

Hubbard, Anthony R., and Trevor W. Barrowcliffe. "Measurement of Activated Factor VII Using Soluble Mutant Tissue Factor -Proposal for Standardization." Thrombosis and Haemostasis 72, no. 04 (1994): 649–50. http://dx.doi.org/10.1055/s-0038-1648934.

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26

Vadivel, Kanagasabai, Amy E. Schmidt, Duilio Cascio, Kaillathe Padmanabhan, Sriram Krishnaswamy, Hans Brandstetter, and S. Paul Bajaj. "Structure of human factor VIIa–soluble tissue factor with calcium, magnesium and rubidium." Acta Crystallographica Section D Structural Biology 77, no. 6 (May 14, 2021): 809–19. http://dx.doi.org/10.1107/s2059798321003922.

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Coagulation factor VIIa (FVIIa) consists of a γ-carboxyglutamic acid (GLA) domain, two epidermal growth factor-like (EGF) domains and a protease domain. FVIIa binds three Mg2+ ions and four Ca2+ ions in the GLA domain, one Ca2+ ion in the EGF1 domain and one Ca2+ ion in the protease domain. Further, FVIIa contains an Na+ site in the protease domain. Since Na+ and water share the same number of electrons, Na+ sites in proteins are difficult to distinguish from waters in X-ray structures. Here, to verify the Na+ site in FVIIa, the structure of the FVIIa–soluble tissue factor (TF) complex was solved at 1.8 Å resolution containing Mg2+, Ca2+ and Rb+ ions. In this structure, Rb+ replaced two Ca2+ sites in the GLA domain and occupied three non-metal sites in the protease domain. However, Rb+ was not detected at the expected Na+ site. In kinetic experiments, Na+ increased the amidolytic activity of FVIIa towards the synthetic substrate S-2288 (H-D-Ile-Pro-Arg-p-nitroanilide) by ∼20-fold; however, in the presence of Ca2+, Na+ had a negligible effect. Ca2+ increased the hydrolytic activity of FVIIa towards S-2288 by ∼60-fold in the absence of Na+ and by ∼82-fold in the presence of Na+. In molecular-dynamics simulations, Na+ stabilized the two Na+-binding loops (the 184-loop and 220-loop) and the TF-binding region spanning residues 163–180. Ca2+ stabilized the Ca2+-binding loop (the 70-loop) and Na+-binding loops but not the TF-binding region. Na+ and Ca2+ together stabilized both the Na+-binding and Ca2+-binding loops and the TF-binding region. Previously, Rb+ has been used to define the Na+ site in thrombin; however, it was unsuccessful in detecting the Na+ site in FVIIa. A conceivable explanation for this observation is provided.

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27

Dalton, George, Sung-Wan An, Saif I. Al-Juboori, Nicole Nischan, Joonho Yoon, Evgenia Dobrinskikh, Donald W. Hilgemann, et al. "Soluble klotho binds monosialoganglioside to regulate membrane microdomains and growth factor signaling." Proceedings of the National Academy of Sciences 114, no. 4 (January 9, 2017): 752–57. http://dx.doi.org/10.1073/pnas.1620301114.

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Soluble klotho, the shed ectodomain of the antiaging membrane protein α-klotho, is a pleiotropic endocrine/paracrine factor with no known receptors and poorly understood mechanism of action. Soluble klotho down-regulates growth factor-driven PI3K signaling, contributing to extension of lifespan, cardioprotection, and tumor inhibition. Here we show that soluble klotho binds membrane lipid rafts. Klotho binding to rafts alters lipid organization, decreases membrane’s propensity to form large ordered domains for endocytosis, and down-regulates raft-dependent PI3K/Akt signaling. We identify α2-3-sialyllactose present in the glycan of monosialogangliosides as targets of soluble klotho. α2-3-Sialyllactose is a common motif of glycans. To explain why klotho preferentially targets lipid rafts we show that clustering of gangliosides in lipid rafts is important. In vivo, raft-dependent PI3K signaling is up-regulated in klotho-deficient mouse hearts vs. wild-type hearts. Our results identify ganglioside-enriched lipid rafts to be receptors that mediate soluble klotho regulation of PI3K signaling. Targeting sialic acids may be a general mechanism for pleiotropic actions of soluble klotho.

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28

Hisatome, Ichiro, Peili Li, Fikri Taufiq, Nani Maharani, Masanari Kuwabara, Haruaki Ninomiya, and Udin Bahrudin. "Hyperuricemia as a Risk Factor for Cardiovascular Diseases." Journal of Biomedicine and Translational Research 6, no. 3 (December 23, 2020): 101–9. http://dx.doi.org/10.14710/jbtr.v6i3.9383.

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Serum uric acid level above 7 mg/dl is defined as hyperuricemia, which gives rise to the monosodium urate (MSU), causing gout and urolithiasis. Hyperuricemia is an independent risk factor as well as a marker for hypertension, heart failure, atherosclerosis, atrial fibrillation, and chronic kidney disease. MSU crystals, soluble uric acid (UA), or oxidative stress derived from xanthine oxidoreductase (XOR) might be plausible explanations for the association of cardio-renovascular diseases with hyperuricemia. In macrophages, MSU activates the Nod-like receptor family, pyrin domain containing 3(NLRP3) inflammasome, and proteolytic processing mediated by caspase-1 with enhanced interleukin (IL)-1β and IL-18 secretion. Soluble UA accumulates intracellularly through UA transporters (UAT) in vascular and atrial myocytes, causing endothelial dysfunction ad atrial electrical remodeling. XOR generates reactive oxygen species (ROS) that lead to cardiovascular diseases. Since it remains unclear whether asymptomatic hyperuricemia could be a risk factor for cardiovascular and kidney diseases, European and American guidelines do not recommend pharmacological treatment for asymptomatic patients with cardio-renovascular diseases. The Japanese guideline, on the contrary, recommends pharmacological treatment for hyperuricemia with CKD to protect renal function, and it attaches importance of the cardio-renal interaction for the treatment of asymptomatic hyperuricemia patients with hypertension and heart failure.

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29

Rutka, James T., Jackson Hall, Jane R. Giblin, Dolores V. Dougherty, Michael S. B. Edwards, Robert Stern, and Mark L. Rosenblum. "Partial characterization of a soluble mitogenic factor from medulloblastoma." Journal of Neurosurgery 68, no. 2 (February 1988): 251–58. http://dx.doi.org/10.3171/jns.1988.68.2.0251.

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✓ To determine how medulloblastoma cells might influence the proliferation and phenotype of normal stromal cells, normal human leptomeningeal cells were treated in culture with medulloblastoma-conditioned medium; their ability to incorporate tritiated thymidine and synthesize collagen was measured. The treated leptomeningeal cells had a significantly greater uptake of tritiated thymidine and grew faster than control leptomeningeal cells. Immunofluorescence studies demonstrated a greater intensity of staining for procollagen type III in the cell layer of the treated cultures than in control cultures; diethylaminoethyl (DEAE)-cellulose chromatography of the medium showed that the treated cells synthesized predominantly type III collagen, whereas control cells synthesized type I collagen. Analysis of the medulloblastoma-conditioned medium revealed that the soluble factor responsible for these effects is an acid- and heat-stable protein. The increased proliferation and altered collagen synthesis induced in leptomeningeal cell cultures by a soluble factor from a medulloblastoma are examples of how tumor and stromal elements interact, and may be related to the process of desmoplasia often observed in medulloblastomas in vivo.

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30

Arai, Ken, Gen Hamanaka, and KellyK Chung. "Do phagocytotic mechanisms regulate soluble factor secretion in microglia?" Neural Regeneration Research 16, no. 5 (2021): 974. http://dx.doi.org/10.4103/1673-5374.297067.

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31

Matsui, Suguru, Norio Yoshimura, and Takahiro Oka. "Characterization of soluble suppressor factor from human decidual cells." Japanese Journal of Clinical Immunology 11, no. 4 (1988): 422–25. http://dx.doi.org/10.2177/jsci.11.422.

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32

Kern, P., W. V. Kern, and P. Kremsner. "Soluble Tumor Necrosis Factor Receptors in Plasmodium vivax Malaria." Journal of Infectious Diseases 168, no. 5 (November 1, 1993): 1340–41. http://dx.doi.org/10.1093/infdis/168.5.1340.

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33

Yu, Hongmei, Caroline M. Alexander, and David J. Beebe. "Understanding microchannel culture: parameters involved in soluble factor signaling." Lab on a Chip 7, no. 6 (2007): 726. http://dx.doi.org/10.1039/b618793e.

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34

Blann, Andrew D., and Malcolm A. Waite. "von Willebrand factor and soluble E-selectin in hypertension." Coronary Artery Disease 7, no. 2 (February 1996): 143–48. http://dx.doi.org/10.1097/00019501-199602000-00008.

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35

Carney, David E., Charles J. Lutz, Anthony L. Picone, Louis A. Gatto, Henry J. Schiller, Christine M. Finck, Bruce Searles, et al. "Soluble Tumor Necrosis Factor Receptor Prevents Post-pump Syndrome." Journal of Surgical Research 83, no. 2 (May 1999): 113–21. http://dx.doi.org/10.1006/jsre.1999.5576.

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36

Wines, Bruce D., Amanda Gavin, Maree S. Powell, Michael Steinitz, Russell R. C. Buchanan, and P. Mark Hogarth. "Soluble FcgammaRIIa inhibits rheumatoid factor binding to immune complexes." Immunology 109, no. 2 (June 2003): 246–54. http://dx.doi.org/10.1046/j.1365-2567.2003.01652.x.

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Sengupta, Tanusree, Rinku Majumder, and Barry R. Lentz. "The Interaction of Soluble Phospholipids with Coagulation Factor VIIa." Blood 116, no. 21 (November 19, 2010): 4421. http://dx.doi.org/10.1182/blood.v116.21.4421.4421.

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Abstract Abstract 4421 Factor VIIa (fVIIa) is one of the key proteins in the blood coagulation cascade. It activates factors IX and × on a negatively charged phospholipid surface in either a TF-dependent or TF-independent fashion (Silverberg et al, 1977; Bom et al, 1990). Monroe et al (1997) demonstrated that fVIIa binds to activated platelets independent of TF and partially restores thrombin generation in an in vitro model of hemophilia. Thus, it appears that interaction of fVIIa with platelet phospholipids plays an important role. We report that binding of 1,2-dihexanoyl-sn-glycero-3-phospholipids -L-serine (C6PS) and 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine (C6PE) to fVIIa causes changes in its activity as well as structure. Titration with C6PS led to changes in intrinsic fluorescence indicative of two or more binding sites for this lipid. Similar titrations with C6PE indicated that it probably binds to a single site on the protein. Experiments are underway to test this initial conclusion. Both lipids bind with comparable affinity (kd ~ 165 and 160 μ M) when data were analyzed using a single site model. We also examined the effect of the soluble lipids on the activity of fVIIa. Both C6PS and C6PE binding increased fVIIa proteolytic and amidolytic activity, with the effect of C6PS being more pronounced. Based on current data, it appears that both lipids bind to a single weak site, but that binding of either to this site promotes binding of C6PS to a second, tighter, and C6PS-specific site, which seems to be crucial in regulating activity. Further experiments are underway to test this hypothesis. Disclosures: No relevant conflicts of interest to declare.

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Tomida, Mikio. "Analysis of Recombinant Soluble Mouse D-Factor/LIF Receptor1." Journal of Biochemistry 117, no. 6 (June 1995): 1228–31. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a124848.

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Luttun, Aernout, and Peter Carmeliet. "Soluble VEGF receptor Flt1: the elusive preeclampsia factor discovered?" Journal of Clinical Investigation 111, no. 5 (March 1, 2003): 600–602. http://dx.doi.org/10.1172/jci18015.

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40

BARBER, Matthew D., Kenneth C. H. FEARON, and James A. ROSS. "Relationship of serum levels of interleukin-6, soluble interleukin-6 receptor and tumour necrosis factor receptors to the acute-phase protein response in advanced pancreatic cancer." Clinical Science 96, no. 1 (January 1, 1999): 83–87. http://dx.doi.org/10.1042/cs0960083.

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The level of the acute-phase response is a major predictor of survival in patients with advanced pancreatic cancer. This study examines the association between the acute-phase protein response, as determined by serum C-reactive protein, and serum levels of interleukin-6, soluble interleukin-6 receptor and the soluble tumour necrosis factor receptors in patients with pancreatic cancer. Thirty-four blood samples were collected from 13 patients with advanced pancreatic cancer. Samples were also collected from six healthy subjects. Levels of C-reactive protein, interleukin-6, soluble interleukin-6 receptor and soluble tumour necrosis factor receptors 55 and 75 were measured by indirect ELISA. Serum levels of C-reactive protein, interleukin-6 and soluble tumour necrosis factor receptors 55 and 75 were significantly higher in cancer patients than in controls. Levels of serum soluble interleukin-6 receptor were not significantly different between the two groups. In cancer patients, a significant positive association was found between the level of the acute-phase protein response and serum levels of interleukin-6, soluble tumour necrosis factor receptor 55 and soluble tumour necrosis factor receptor 75. No association was found between levels of soluble interleukin-6 receptor and any other factor. There is no significant relationship between the level of soluble interleukin-6 receptor and the acute-phase protein response in vivo and the biological role of soluble interleukin-6 receptor in the chronic inflammatory component of cachexia remains unclear.

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Yu, Mao Jie, Bei Qing Huang, and Xian Fu Wei. "Research of the Factor that Influence the Glossiness of Water-Based Tipping Paper Gravure Varnish." Applied Mechanics and Materials 262 (December 2012): 426–29. http://dx.doi.org/10.4028/www.scientific.net/amm.262.426.

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In order to prepare high-gloss water-soluble gravure varnish which is used on tipping paper, different content and types of filming resin with different content of all kinds of additives added are used to prepare water-soluble gravure varnish. Test its main performance and then use IGT apparatus to proof. The effect of varnish component and content on glossiness of water-soluble varnish is discussed by measuring glossiness of proof. The results show: different content and types of water-soluble filming resin have a great influence on the glossiness of water-soluble gravure varnish which is used on tipping paper; the glossiness of water-soluble varnish film can improve by adding auxiliaries such as cosolvent, substrate wetting agent, flow agent, wax emulsion and other promoter into water-soluble varnish system.

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Visser, Wil, Ilse Beckmann, Marco A. H. Knook, and Henk C. S. Wallenburg. "Soluble tumor necrosis factor receptor II and soluble cell adhesion molecule 1 as markers of tumor necrosis factor-α release in preeclampsia." Acta Obstetricia et Gynecologica Scandinavica 81, no. 8 (January 2002): 713–19. http://dx.doi.org/10.1080/j.1600-0412.2002.810805.x.

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Lim, H., A. Blann, and G. Lip. "Soluble CD40 Ligand, soluble P-selectin, interleukin-6, and tissue factor in diabetes mellitus. Relationships to cardiovascular disease and risk factor intervention." ACC Current Journal Review 13, no. 8 (August 2004): 19–20. http://dx.doi.org/10.1016/j.accreview.2004.07.107.

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44

Visser, Wil, Ilse Beckmann, Marco A. H. Knook, and Henk C. S. Wallenburg. "Soluble tumor necrosis factor receptor II and soluble cell adhesion molecule 1 as markers of tumor necrosis factor-α release in preeclampsia." Acta Obstetricia et Gynecologica Scandinavica 81, no. 8 (August 2002): 713–19. http://dx.doi.org/10.1034/j.1600-0412.2002.810805.x.

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45

Alasztics, Bálint, Nóra Gullai, Attila Molvarec, and János Rigó Jr. "The role of angiogenic factors in preeclampsia." Orvosi Hetilap 155, no. 47 (November 2014): 1860–66. http://dx.doi.org/10.1556/oh.2014.30042.

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Preeclampsia is one of the most common and most serious complications of pregnancy and the management of this condition still challenges obstetricians. Despite intensive research the etiology of preeclampsia still remains unclear. At the beginning of the 2000s preeclampsia-related research was directed towards factors that influence angiogenesis. Most studies have been carried out on the placental growth factor and soluble fms-like tyrosine kinase-1. Most publications confirm the increased concentrations of antiangiogenic factors and decreased concentrations of proangiogenic factors in maternal blood samples in preeclampsia even before the onset of clinical symptoms. According to our current knowledge antiangiogenic proteins are responsible for the endothelial dysfunction in the symptomatic stage of the disease. Placental growth factor and soluble fms-like tyrosine kinase-1 may have important roles in the prediction and treatment of the disease. The point of care detection of placental growth factor and soluble fms-like tyrosine kinase-1 may be used to predict preeclampsia. Rapid tests are available to determine the serum levels of the two proteins. Removal of soluble fms-like tyrosine kinase-1 from maternal circulation is a potential treatment option for early onset preeclampsia. Orv. Hetil., 2014, 155(47), 1860–1866.

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Noguchi, M., N. Hiwatashi, Z. Liu, and T. Toyota. "Secretion imbalance between tumour necrosis factor and its inhibitor in inflammatory bowel disease." Gut 43, no. 2 (August 1, 1998): 203–9. http://dx.doi.org/10.1136/gut.43.2.203.

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Background—Tumour necrosis factor (TNF) α and TNF-β are soluble ligands binding to TNF receptors with similar activities; soluble TNF receptors neutralise TNF activity by acting as inhibitors. Little is known about the cytokine/soluble receptor role in inflammatory bowel disease (IBD).Aims—To test the hypothesis that an imbalance in secretion between TNF and TNF inhibitors plays a role in gut inflammation in patients with IBD.Methods—The secretion of TNF-α, TNF-β, and soluble TNF receptors was compared in the culture supernatants of colonic biopsy specimens and isolated lamina propria mononuclear cells from patients with active colonic IBD.Results—Spontaneous secretion of TNF-α in involved IBD mucosa was higher than in normal control and self limited colitis mucosa. Secretion of TNF-β was higher in patients with Crohn’s disease than in those with ulcerative colitis. Soluble TNF receptor in IBD mucosa inhibited TNF activity. Type 2 soluble receptor release from IBD mucosa was increased in active inflammation; release from lamina propria cells was not increased. Mucosal TNF-α production correlated with severity of disease.Conclusions—Results showed enhanced secretion of TNF-α but failure to release enhanced amounts of soluble TNF receptor in lamina propria mononuclear cells of patients with IBD. An imbalance in secretion between TNF and TNF inhibitor may be implicated in the pathogenesis of IBD.

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VILCHIS-LANDEROS, M. Magdalena, José L. MONTIEL, Valentín MENDOZA, Guillermo MENDOZA-HERNÁNDEZ, and Fernando LÓPEZ-CASILLAS. "Recombinant soluble betaglycan is a potent and isoform-selective transforming growth factor-β neutralizing agent." Biochemical Journal 355, no. 1 (February 26, 2001): 215–22. http://dx.doi.org/10.1042/bj3550215.

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Betaglycan is an accessory receptor of members of the transforming growth factor-β (TGF-β) superfamily, which regulates their actions through ligand-dependent interactions with type II receptors. A natural soluble form of betaglycan is found in serum and extracellular matrices. Soluble betaglycan, prepared as a recombinant protein using the baculoviral expression system, inhibits the actions of TGF-β. Because of its potential use as an anti-TGF-β therapeutic agent, we have purified and characterized baculoviral recombinant soluble betaglycan. Baculoviral soluble betaglycan is a homodimer formed by two 110kDa monomers associated by non-covalent interactions. This protein is devoid of glycosaminoglycan chains, although it contains the serine residues, which, in vertebrate cells, are modified by these carbohydrates. On the other hand, mannose-rich carbohydrates account for approximately 20kDa of the mass of the monomer. End-terminal sequence analysis of the soluble betaglycan showed that Gly24 is the first residue of the mature protein. Similarly to the natural soluble betaglycan, baculoviral soluble betaglycan has an equilibrium dissociation constant (Kd) of 3.5nM for TGF-β1. Ligand competition assays indicate that the relative affinities of recombinant soluble betaglycan for the TGF-β isoforms are TGF-β2>TGF-β3>TGF-β1. The anti-TGF-β potency of recombinant soluble betaglycan invitro is 10-fold higher for TGF-β2 than for TGF-β1. Compared with a commercial pan-specific anti-TGF-β neutralizing antibody, recombinant soluble betaglycan is more potent against TGF-β2 and similar against TGF-β1. These results indicate that baculoviral soluble betaglycan has the biochemical and functional properties that would make it a suitable agent for the treatment of the diseases in which excess TGF-β plays a central physiopathological role.

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Brown, CB, P. Beaudry, TD Laing, S. Shoemaker, and K. Kaushansky. "In vitro characterization of the human recombinant soluble granulocyte- macrophage colony-stimulating factor receptor." Blood 85, no. 6 (March 15, 1995): 1488–95. http://dx.doi.org/10.1182/blood.v85.6.1488.bloodjournal8561488.

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We have cloned, expressed, and partially purified a naturally occurring, truncated, soluble form of the human granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor alpha subunit to investigate its biochemical and biologic properties. The soluble receptor species lacks the transmembrane and cytoplasmic domains that are presumably removed from the intact receptor cDNA by a mechanism of alternative splicing. The resulting soluble 55- to 60-kD glycosylated receptor species binds GM-CSF with a dissociation constant (kd) of 3.8 nmol/L. The soluble GM-CSF receptor successfully competes for GM-CSF binding not only with the transmembrane-anchored GM-CSF receptor alpha subunit but also with the native oligomeric high-affinity receptor complex. In addition, in human bone marrow colony-forming assays, the soluble GM-CSF receptor species can antagonize the activity of GM-CSF. Our data suggest that the soluble GM-CSF receptor may be capable of acting in vivo as a modulator of the biologic activity of GM-CSF.

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Wang, Y. I., G. Li, Y. Zhang, W. Gao, and Z. Yao. "The Expression of von Willebrand Factor, Soluble Thrombomodulin, and Soluble P-Selectin During Orthotopic Liver Transplantation." Transplantation Proceedings 39, no. 1 (January 2007): 172–75. http://dx.doi.org/10.1016/j.transproceed.2006.10.027.

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Schmidt-Lucke, Caroline, Funmi Belgore, Dirk Reinhold, Siegfried Ansorge, Helmut U. Klein, J. André Schmidt-Lucke, and Gregory Y. H. Lip. "Soluble vascular endothelial growth factor, soluble VEGF receptor Flt-1 and endothelial function in healthy smokers." International Journal of Cardiology 100, no. 2 (April 2005): 207–12. http://dx.doi.org/10.1016/j.ijcard.2004.05.046.

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