메뉴 건너뛰기




Volumn 29, Issue 2, 2014, Pages 405-422

Endovascular laser-tissue interactions and biological responses in relation to endovenous laser therapy

Author keywords

Cytokines and chemokines; Damage associated molecular patterns; Endovenous laser ablation; Fibrosis; Great saphenous vein; Inflammation; Innate immune response; Phagocytosis; Tissue remodeling; Varicose veins; Venous thrombus organization

Indexed keywords

ANTICOAGULANT AGENT; COLLAGEN; FIBROBLAST GROWTH FACTOR; HEAT SHOCK PROTEIN; HEPARANASE; INTERCELLULAR ADHESION MOLECULE 1; PHOSPHATIDYLSERINE; PLATELET DERIVED GROWTH FACTOR; SCLEROPROTEIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 84897083156     PISSN: 02688921     EISSN: 1435604X     Source Type: Journal    
DOI: 10.1007/s10103-013-1490-3     Document Type: Review
Times cited : (28)

References (210)
  • 3
    • 61349102649 scopus 로고    scopus 로고
    • Endovenous laser ablation-induced complications: Review of the literature and new cases
    • van den Bos RR, Neumann M, De Roos KP, Nijsten T (2009) Endovenous laser ablation-induced complications: review of the literature and new cases. Dermatol Surg 35:1206-1214
    • (2009) Dermatol Surg , vol.35 , pp. 1206-1214
    • Van Den Bos, R.R.1    Neumann, M.2    De Roos, K.P.3    Nijsten, T.4
  • 4
    • 33748305517 scopus 로고    scopus 로고
    • Treatment of varicose veins by endovenous laser therapy: Assessment of results by ultrasound surveillance
    • Myers K, Fris R, Jolley D (2006) Treatment of varicose veins by endovenous laser therapy: assessment of results by ultrasound surveillance. Med J Aust 185:199-202 (Pubitemid 44322781)
    • (2006) Medical Journal of Australia , vol.185 , Issue.4 , pp. 199-202
    • Myers, K.1    Fris, R.2    Jolley, D.3
  • 5
    • 55949128254 scopus 로고    scopus 로고
    • Endovenous laser ablation: Mechanism of action
    • Fan CM, Rox-Anderson R (2008) Endovenous laser ablation: mechanism of action. Phlebology 23:206-213
    • (2008) Phlebology , vol.23 , pp. 206-213
    • Fan, C.M.1    Rox-Anderson, R.2
  • 6
    • 84858438829 scopus 로고    scopus 로고
    • Endovenous laser ablation: A review of mechanisms of action
    • Vuylsteke ME, Mordon SR (2012) Endovenous laser ablation: a review of mechanisms of action. Ann Vasc Surg 26:424-433
    • (2012) Ann Vasc Surg , vol.26 , pp. 424-433
    • Vuylsteke, M.E.1    Mordon, S.R.2
  • 10
    • 0036316195 scopus 로고    scopus 로고
    • Thermal damage of the inner vein wall during endovenous laser treatment: Key role of energy absorption by intravascular blood
    • DOI 10.1046/j.1524-4725.2002.01309.x
    • Proebstle TM, Sandhofer M, Kargl A, Gul D, Rother W, Knop J, Lehr HA (2002) Thermal damage of the inner vein wall during endovenous laser treatment: key role of energy absorption by intravascular blood. Dermatol Surg 28:596-600 (Pubitemid 34816041)
    • (2002) Dermatologic Surgery , vol.28 , Issue.7 , pp. 596-600
    • Proebstle, T.M.1    Sandhofer, M.2    Kargl, A.3    Gul, D.4    Rother, W.5    Knop, J.6    Lehr, H.A.7
  • 11
    • 0036546892 scopus 로고    scopus 로고
    • Endovenous treatment of the greater saphenous vein with a 940-nm diode laser: Thrombotic occlusion after endoluminal thermal damage by laser-generated steam bubbles
    • Proebstle TM, Lehr HA, Kargl A, Espinola-Klein C, Rother W, Bethge S, Knop J (2002) Endovenous treatment of the greater saphenous vein with a 940-nm diode laser: thrombotic occlusion after endoluminal thermal damage by laser-generated steam bubbles. J Vasc Surg 35:729-736
    • (2002) J Vasc Surg , vol.35 , pp. 729-736
    • Proebstle, T.M.1    Lehr, H.A.2    Kargl, A.3    Espinola-Klein, C.4    Rother, W.5    Bethge, S.6    Knop, J.7
  • 13
    • 84897085009 scopus 로고    scopus 로고
    • Thrombosis versus thermal coagulum formation as a result of endovenous laser therapy: Biochemistry versus photophysics
    • Heger M (2013) Thrombosis versus thermal coagulum formation as a result of endovenous laser therapy: biochemistry versus photophysics, Phlebology
    • (2013) Phlebology
    • Heger, M.1
  • 14
    • 57749102725 scopus 로고    scopus 로고
    • Histological changes occurring after endoluminal ablation with two diode lasers (940 and 1319 nm) from acute changes to 4 months
    • Bush RG, Shamma HN, Hammond K (2008) Histological changes occurring after endoluminal ablation with two diode lasers (940 and 1319 nm) from acute changes to 4 months. Lasers Surg Med 40:676-679
    • (2008) Lasers Surg Med , vol.40 , pp. 676-679
    • Bush, R.G.1    Shamma, H.N.2    Hammond, K.3
  • 15
    • 0141724518 scopus 로고    scopus 로고
    • Infrequent early recanalization of greater saphenous vein after endovenous laser treatment
    • DOI 10.1016/S0741-5214(03)00420-8
    • Proebstle TM, Gul D, Lehr HA, Kargl A, Knop J (2003) Infrequent early recanalization of greater saphenous vein after endovenous laser treatment. J Vasc Surg 38:511-516 (Pubitemid 41123217)
    • (2003) Journal of Vascular Surgery , vol.38 , Issue.3 , pp. 511-516
    • Proebstle, T.M.1    Gul, D.2    Lehr, H.A.3    Kargl, A.4    Knop, J.5
  • 16
    • 67749127774 scopus 로고    scopus 로고
    • Endovenous laser treatment: A morphological study in an animal model
    • Vuylsteke M, Van DJ, Roelens J, De BT, Mordon S (2009) Endovenous laser treatment: a morphological study in an animal model. Phlebology 24:166-175
    • (2009) Phlebology , vol.24 , pp. 166-175
    • Vuylsteke, M.1    Van, D.J.2    Roelens, J.3    De, B.T.4    Mordon, S.5
  • 18
    • 0242626143 scopus 로고    scopus 로고
    • Endovenous laser surgery of the incompetent greater saphenous vein with a 980-nm diode laser
    • Oh CK, Jung DS, Jang HS, Kwon KS (2003) Endovenous laser surgery of the incompetent greater saphenous vein with a 980-nm diode laser. Dermatol Surg 29:1135-1140
    • (2003) Dermatol Surg , vol.29 , pp. 1135-1140
    • Oh, C.K.1    Jung, D.S.2    Jang, H.S.3    Kwon, K.S.4
  • 19
    • 33748956910 scopus 로고    scopus 로고
    • Reduced recanalization rates of the great saphenous vein after endovenous laser treatment with increased energy dosing: Definition of a threshold for the endovenous fluence equivalent
    • DOI 10.1016/j.jvs.2006.05.052, PII S0741521406010159
    • Proebstle TM, Moehler T, Herdemann S (2006) Reduced recanalization rates of the great saphenous vein after endovenous laser treatment with increased energy dosing: definition of a threshold for the endovenous fluence equivalent. J Vasc Surg 44:834-839 (Pubitemid 44441762)
    • (2006) Journal of Vascular Surgery , vol.44 , Issue.4 , pp. 834-839
    • Proebstle, T.M.1    Moehler, T.2    Herdemann, S.3
  • 20
    • 20444476641 scopus 로고    scopus 로고
    • The immediate effects of endovenous diode 808-nm laser in the greater saphenous vein: Morphologic study and clinical implications
    • DOI 10.1016/j.jvs.2005.03.002, PII S0741521405003319
    • Corcos L, Dini S, De AD, Marangoni O, Ferlaino E, Procacci T, Spina T, Dini M (2005) The immediate effects of endovenous diode 808-nm laser in the greater saphenous vein: morphologic study and clinical implications. J Vasc Surg 41:1018-1024 (Pubitemid 40813032)
    • (2005) Journal of Vascular Surgery , vol.41 , Issue.6 , pp. 1018-1024
    • Corcos, L.1    Dini, S.2    De Anna, D.3    Marangoni, O.4    Ferlaino, E.5    Procacci, T.6    Spina, T.7    Dini, M.8
  • 26
    • 0036152537 scopus 로고    scopus 로고
    • Comparison of endovenous radiofrequency versus 810 nm diode laser occlusion of large veins in an animal model
    • Weiss RA (2002) Comparison of endovenous radiofrequency versus 810 nm diode laser occlusion of large veins in an animal model. Dermatol Surg 28:56-61
    • (2002) Dermatol Surg , vol.28 , pp. 56-61
    • Weiss, R.A.1
  • 27
    • 34848850786 scopus 로고    scopus 로고
    • Endovenous laser treatment for varicose veins in patients with active ulcers: Measurement of intravenous and perivenous temperatures during the procedure
    • Viarengo LM, Poterio-Filho J, Poterio GM, Menezes FH, Meirelles GV(2007) Endovenous laser treatment for varicose veins in patients with active ulcers: measurement of intravenous and perivenous temperatures during the procedure. Dermatol Surg 33:1234-1242
    • (2007) Dermatol Surg , vol.33 , pp. 1234-1242
    • Viarengo, L.M.1    Poterio-Filho, J.2    Poterio, G.M.3    Menezes, F.H.4    Meirelles, G.V.5
  • 30
    • 77958152008 scopus 로고    scopus 로고
    • Neutrophils: Cinderella of innate immune system
    • Kumar V, Sharma A (2010) Neutrophils: Cinderella of innate immune system. Int Immunopharmacol 10:1325-1334
    • (2010) Int Immunopharmacol , vol.10 , pp. 1325-1334
    • Kumar, V.1    Sharma, A.2
  • 31
    • 13844296549 scopus 로고    scopus 로고
    • Towards optimization of selective photothermolysis: Prothrombotic pharmaceutical agents as potential adjuvants in laser treatment of port wine stains. A theoretical study
    • DOI 10.1186/TH04-05-0291
    • Heger M, Beek JF, Moldovan NI, van der Horst CM, van Gemert MJ (2005) Towards optimization of selective photothermolysis: prothrombotic pharmaceutical agents as potential adjuvants in laser treatment of port wine stains. A theoretical study. Thromb Haemost 93:242-256 (Pubitemid 40253728)
    • (2005) Thrombosis and Haemostasis , vol.93 , Issue.2 , pp. 242-256
    • Heger, M.1    Beek, J.F.2    Moldovan, N.I.3    Van Der Horst, C.M.A.M.4    Van Gemert, M.J.C.5
  • 32
    • 79961025227 scopus 로고    scopus 로고
    • Laser-induced primary and secondary hemostasis dynamics and mechanisms in relation to selective photothermolysis of port wine stains
    • Heger M, Salles II, Bezemer R, Cloos MA, Mordon SR, Begu S, Deckmyn H, Beek JF (2011) Laser-induced primary and secondary hemostasis dynamics and mechanisms in relation to selective photothermolysis of port wine stains. J Dermatol Sci 63:139-147
    • (2011) J Dermatol Sci , vol.63 , pp. 139-147
    • Heger, M.1    Salles, I.I.2    Bezemer, R.3    Cloos, M.A.4    Mordon, S.R.5    Begu, S.6    Deckmyn, H.7    Beek, J.F.8
  • 33
    • 18444379927 scopus 로고    scopus 로고
    • Macrophages restrain contraction of an in vitro wound healing model
    • DOI 10.1023/B:IFLA.0000049045.41784.59
    • Newton PM, Watson JA, Wolowacz RG, Wood EJ (2004) Macrophages restrain contraction of an in vitro wound healing model. Inflammation 28:207-214 (Pubitemid 41449420)
    • (2004) Inflammation , vol.28 , Issue.4 , pp. 207-214
    • Newton, P.M.1    Watson, J.A.2    Wolowacz, R.G.3    Wood, E.J.4
  • 34
    • 0035036654 scopus 로고    scopus 로고
    • Adventitial fibroblasts: Backstage journeymen
    • Miller FJ (2001) Adventitial fibroblasts: backstage journeymen. Arterioscler Thromb Vasc Biol 21:722-723
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 722-723
    • Miller, F.J.1
  • 35
    • 0029784055 scopus 로고    scopus 로고
    • Adventitial myofibroblasts contribute to neointimal formation in injured porcine coronary arteries
    • Shi Y, O'Brien JE, Fard A, Mannion JD, Wang D, Zalewski A (1996) Adventitial myofibroblasts contribute to neointimal formation in injured porcine coronary arteries. Circulation 94:1655-1664 (Pubitemid 26320272)
    • (1996) Circulation , vol.94 , Issue.7 , pp. 1655-1664
    • Shi, Y.1    O'Brien Jr., J.E.2    Fard, A.3    Mannion, J.D.4    Wang, D.5    Zalewski, A.6
  • 36
    • 0034724268 scopus 로고    scopus 로고
    • Direct in vivo evidence demonstrating neointimal migration of adventitial fibroblasts after balloon injury of rat carotid arteries
    • Li G, Chen SJ, Oparil S, Chen YF, Thompson JA (2000) Direct in vivo evidence demonstrating neointimal migration of adventitial fibroblasts after balloon injury of rat carotid arteries. Circulation 101:1362-1365 (Pubitemid 30169855)
    • (2000) Circulation , vol.101 , Issue.12 , pp. 1362-1365
    • Li, G.1    Chen, S.-J.2    Oparil, S.3    Chen, Y.-F.4    Thompson, J.A.5
  • 37
    • 78649526394 scopus 로고    scopus 로고
    • Sterile inflammation: Sensing and reacting to damage
    • Chen GY, Nunez G (2010) Sterile inflammation: sensing and reacting to damage. Nat Rev Immunol 10:826-837
    • (2010) Nat Rev Immunol , vol.10 , pp. 826-837
    • Chen, G.Y.1    Nunez, G.2
  • 39
    • 0025850837 scopus 로고
    • Heat shock induces two distinct S6 protein kinase activities in quiescent mammalian fibroblasts
    • Jurivich DA, Chung J, Blenis J (1991) Heat shock induces two distinct S6 protein kinase activities in quiescent mammalian fibroblasts. J Cell Physiol 148:252-259 (Pubitemid 21910148)
    • (1991) Journal of Cellular Physiology , vol.148 , Issue.2 , pp. 252-259
    • Jurivich, D.A.1    Chung, J.2    Blenis, J.3
  • 40
  • 41
    • 0029934015 scopus 로고    scopus 로고
    • Identification of a potential role for the adventitia in vascular lesion formation after balloon overstretch injury of porcine coronary arteries
    • Scott NA, Cipolla GD, Ross CE, Dunn B, Martin FH, Simonet L, Wilcox JN (1996) Identification of a potential role for the adventitia in vascular lesion formation after balloon overstretch injury of porcine coronary arteries. Circulation 93:2178-2187 (Pubitemid 26187108)
    • (1996) Circulation , vol.93 , Issue.12 , pp. 2178-2187
    • Scott, N.A.1    Cipolla, G.D.2    Ross, C.E.3    Dunn, B.4    Martin, F.H.5    Simonet, L.6    Wilcox, J.N.7
  • 44
    • 84859165370 scopus 로고    scopus 로고
    • Deep vein thrombosis (DVT) after venous thermoablation techniques: Rates of endovenous heat-induced thrombosis (EHIT) and classical DVTafter radiofrequency and endovenous laser ablation in a single centre
    • Marsh P, Price BA, Holdstock J, Harrison C, Whiteley MS (2010) Deep vein thrombosis (DVT) after venous thermoablation techniques: rates of endovenous heat-induced thrombosis (EHIT) and classical DVTafter radiofrequency and endovenous laser ablation in a single centre. Eur J Vasc Endovasc Surg 40:521-527
    • (2010) Eur J Vasc Endovasc Surg , vol.40 , pp. 521-527
    • Marsh, P.1    Price, B.A.2    Holdstock, J.3    Harrison, C.4    Whiteley, M.S.5
  • 45
    • 4644220284 scopus 로고    scopus 로고
    • Chemical and structural changes in blood undergoing laser photocoagulation
    • Black JF, Barton JK (2004) Chemical and structural changes in blood undergoing laser photocoagulation. Photochem Photobiol 80:89-97
    • (2004) Photochem Photobiol , vol.80 , pp. 89-97
    • Black, J.F.1    Barton, J.K.2
  • 46
    • 14644414272 scopus 로고    scopus 로고
    • Mechanistic comparison of blood undergoing laser photocoagulation at 532 and 1,064 nm
    • DOI 10.1002/lsm.20134
    • Black JF, Wade N, Barton JK (2005) Mechanistic comparison of blood undergoing laser photocoagulation at 532 and 1,064 nm. Lasers Surg Med 36:155-165 (Pubitemid 40315489)
    • (2005) Lasers in Surgery and Medicine , vol.36 , Issue.2 , pp. 155-165
    • Black, J.F.1    Wade, N.2    Barton, J.K.3
  • 47
    • 14744282612 scopus 로고    scopus 로고
    • Darkfield orthogonal polarized spectral imaging for studying endovascular laser-tissue interactions in vivo - A preliminary study
    • DOI 10.1364/OPEX.13.000702
    • Heger M, Beek J, Stenback K, Faber D, van Gemert M, Ince C (2005) Darkfield orthogonal polarized spectral imaging for studying endovenous laser-tissue interactions in vivo - a preliminary study. Opt Express 13:702-715 (Pubitemid 40334870)
    • (2005) Optics Express , vol.13 , Issue.3 , pp. 702-715
    • Heger, M.1    Beek, J.F.2    Stenback, K.3    Faber, D.J.4    Van Gemert, M.J.C.5    Ince, C.6
  • 48
    • 77955651631 scopus 로고    scopus 로고
    • Endovenous laser-tissue interactions redefined: Shining light on novel windows of therapeutic opportunity beyond selective photothermolysis
    • Heger M, Bezemer R, Huertas-Perez JF, Dekker H, Beek JF (2010) Endovenous laser-tissue interactions redefined: shining light on novel windows of therapeutic opportunity beyond selective photothermolysis. Photomed Laser Surg 28:569-572
    • (2010) Photomed Laser Surg , vol.28 , pp. 569-572
    • Heger, M.1    Bezemer, R.2    Huertas-Perez, J.F.3    Dekker, H.4    Beek, J.F.5
  • 49
    • 34547169983 scopus 로고    scopus 로고
    • Laser-induced (endo)vascular photothermal effects studied by combined brightfield and fluorescence microscopy in hamster dorsal skin fold venules
    • DOI 10.1364/OE.15.008493
    • Bezemer R, Heger M, van den Wijngaard JP, Mordon SR, van Gemert MJ, Beek JF (2007) Laser-induced (endo)vascular photothermal effects studied by combined brightfield and fluorescence microscopy in hamster dorsal skin fold venules. Opt Express 15:8493-8506 (Pubitemid 47112460)
    • (2007) Optics Express , vol.15 , Issue.14 , pp. 8493-8506
    • Bezemer, R.1    Heger, M.2    Van Den, W.J.P.H.3    Mordon, S.R.4    Van Gemert, M.J.C.5    Beek, J.F.6
  • 51
    • 84881026932 scopus 로고    scopus 로고
    • Living and dying for inflammation: Neutrophils, eosinophils, basophils
    • Geering B, Stoeckle C, Conus S, Simon HU (2013) Living and dying for inflammation: neutrophils, eosinophils, basophils. Trends Immunol 34:398-409
    • (2013) Trends Immunol , vol.34 , pp. 398-409
    • Geering, B.1    Stoeckle, C.2    Conus, S.3    Simon, H.U.4
  • 52
    • 29944438881 scopus 로고    scopus 로고
    • Necrotic death as a cell fate
    • Zong WX, Thompson CB (2006) Necrotic death as a cell fate. Genes Dev 20:1-15
    • (2006) Genes Dev , vol.20 , pp. 1-15
    • Zong, W.X.1    Thompson, C.B.2
  • 54
    • 33745672598 scopus 로고    scopus 로고
    • Interactions of systemic immune response and local wound healing in different burn depths: An experimental study on rats
    • DOI 10.1097/01.BCR.0000216330.93056.06, PII 0125309220060500000018
    • Sakallioglu AE, Basaran O, Karakayali H, Ozdemir BH, Yucel M, Arat Z, Haberal M (2006) Interactions of systemic immune response and local wound healing in different burn depths: an experimental study on rats. J Burn Care Res 27:357-366 (Pubitemid 43970304)
    • (2006) Journal of Burn Care and Research , vol.27 , Issue.3 , pp. 357-366
    • Sakallioglu, A.E.1    Basaran, O.2    Karakayali, H.3    Ozdemir, B.H.4    Yucel, M.5    Arat, Z.6    Haberal, M.7
  • 56
    • 53349110137 scopus 로고    scopus 로고
    • Platelet-monocyte interactions - A dangerous liaison linking thrombosis, inflammation and atherosclerosis
    • Seizer P, Gawaz M, May AE (2008) Platelet-monocyte interactions - a dangerous liaison linking thrombosis, inflammation and atherosclerosis. Curr Med Chem 15:1976-1980
    • (2008) Curr Med Chem , vol.15 , pp. 1976-1980
    • Seizer, P.1    Gawaz, M.2    May, A.E.3
  • 57
    • 0031656215 scopus 로고    scopus 로고
    • Physiology and healing dynamics of chronic cutaneous wounds
    • DOI 10.1016/S0002-9610(98)00183-4, PII S0002961098001834
    • Stadelmann WK, Digenis AG, Tobin GR (1998) Physiology and healing dynamics of chronic cutaneous wounds. Am J Surg 176:26S-38S (Pubitemid 28460655)
    • (1998) American Journal of Surgery , vol.176 , Issue.2 A
    • Stadelmann, W.K.1    Digenis, A.G.2    Tobin, G.R.3
  • 58
    • 0141996919 scopus 로고    scopus 로고
    • Platelet chemokines and chemokine receptors: Linking hemostasis, inflammation, and host defense
    • DOI 10.1038/sj.mn.7800198
    • Gear AR, Camerini D (2003) Platelet chemokines and chemokine receptors: linking hemostasis, inflammation, and host defense. Microcirculation 10:335-350 (Pubitemid 39004260)
    • (2003) Microcirculation , vol.10 , Issue.3-4 , pp. 335-350
    • Gear, A.R.L.1    Camerini, D.2
  • 59
    • 0021270227 scopus 로고
    • Stimulation of leukocyte phagocytic activity by the platelet release reaction
    • Sakamoto H, Firkin FC, Chesterman CN (1984) Stimulation of leukocyte phagocytic activity by the platelet release reaction. Pathology 16:126-130 (Pubitemid 14130865)
    • (1984) Pathology , vol.16 , Issue.2 , pp. 126-130
    • Sakamoto, H.1    Firkin, F.C.2    Chesterman, C.N.3
  • 60
    • 0026628173 scopus 로고
    • P-selectin mediates Ca(2+)-dependent adhesion of activated platelets to many different types of leukocytes: Detection by flow cytometry
    • de Bruijne-Admiraal LG, Modderman PW, Von dem Borne AE, Sonnenberg A (1992) P-selectin mediates Ca(2+)-dependent adhesion of activated platelets to many different types of leukocytes: detection by flow cytometry. Blood 80:134-142
    • (1992) Blood , vol.80 , pp. 134-142
    • De Bruijne-Admiraal, L.G.1    Modderman, P.W.2    Von Dem Borne, A.E.3    Sonnenberg, A.4
  • 63
    • 0032522957 scopus 로고    scopus 로고
    • Platelet-derived factor Va/Va(Leiden) cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C
    • Camire RM, Kalafatis M, Simioni P, Girolami A, Tracy PB (1998) Platelet-derived factor Va/Va Leiden cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C. Blood 91:2818-2829 (Pubitemid 28227532)
    • (1998) Blood , vol.91 , Issue.8 , pp. 2818-2829
    • Camire, R.M.1    Kalafatis, M.2    Simioni, P.3    Girolami, A.4    Tracy, P.B.5
  • 65
    • 0025738740 scopus 로고
    • Comparison of anticoagulant and procoagulant activities of stimulated platelets and platelet-derived microparticles
    • Tans G, Rosing J, Thomassen MC, Heeb MJ, Zwaal RF, Griffin JH (1991) Comparison of anticoagulant and procoagulant activities of stimulated platelets and platelet-derived microparticles. Blood 77:2641-2648
    • (1991) Blood , vol.77 , pp. 2641-2648
    • Tans, G.1    Rosing, J.2    Thomassen, M.C.3    Heeb, M.J.4    Zwaal, R.F.5    Griffin, J.H.6
  • 67
    • 0026752756 scopus 로고
    • Coagulation factor IXa binding to activated platelets and platelet-derived microparticles: A flow cytometric study
    • Hoffman M, Monroe DM, Roberts HR (1992) Coagulation factor IXa binding to activated platelets and platelet-derived microparticles: a flow cytometric study. Thromb Haemost 68:74-78
    • (1992) Thromb Haemost , vol.68 , pp. 74-78
    • Hoffman, M.1    Monroe, D.M.2    Roberts, H.R.3
  • 68
    • 0024253430 scopus 로고
    • Complement proteins C5b-9 cause release of membrane vesicles from the platelet surface that are enriched in the membrane receptor for coagulation factor Va and express prothrombinase activity
    • Sims PJ, Faioni EM, Wiedmer T, Shattil SJ (1988) Complement proteins C5b-9 cause release ofmembrane vesicles from the platelet surface that are enriched in the membrane receptor for coagulation factor Va and express prothrombinase activity. J Biol Chem 263: 18205-18212 (Pubitemid 19005097)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.34 , pp. 18205-18212
    • Sims, P.J.1    Faioni, E.M.2    Wiedmer, T.3    Shattil, S.J.4
  • 69
    • 0030585753 scopus 로고    scopus 로고
    • Procoagulant activity and active calpain in platelet-derived microparticles
    • DOI 10.1016/0049-3848(96)00101-6
    • Pasquet JM, Toti F, Nurden AT, Dachary-Prigent J (1996) Procoagulant activity and active calpain in platelet-derived microparticles. Thromb Res 82:509-522 (Pubitemid 26233236)
    • (1996) Thrombosis Research , vol.82 , Issue.6 , pp. 509-522
    • Pasquet, J.-M.1    Toti, F.2    Nurden, A.T.3    Dachary-Prigent, J.4
  • 70
    • 0030954420 scopus 로고    scopus 로고
    • Transcellular activation of platelets and endothelial cells by bioactive lipids in platelet microparticles
    • Barry OP, Pratico D, Lawson JA, FitzGerald GA (1997) Transcellular activation of platelets and endothelial cells by bioactive lipids in platelet microparticles. J Clin Invest 99:2118-2127 (Pubitemid 27203768)
    • (1997) Journal of Clinical Investigation , vol.99 , Issue.9 , pp. 2118-2127
    • Barry, O.P.1    Pratico, D.2    Lawson, J.A.3    FitzGerald, G.A.4
  • 71
    • 0029551715 scopus 로고
    • Platelet microparticles bind, activate and aggregate neutrophils in vitro
    • DOI 10.1006/bcmd.1995.0025
    • Jy W, Mao WW, Horstman L, Tao J, Ahn YS (1995) Platelet microparticles bind, activate and aggregate neutrophils in vitro. Blood Cells Mol Dis 21:217-231 (Pubitemid 26083518)
    • (1995) Blood Cells, Molecules, and Diseases , vol.21 , Issue.3 , pp. 217-231
    • Jy, W.1    Mao, W.-W.2    Horstman, L.L.3    Tao, J.4    Ahn, Y.S.5
  • 72
    • 33748522053 scopus 로고    scopus 로고
    • Clearance of apoptotic and necrotic cells and its immunological consequences
    • DOI 10.1007/s10495-006-9527-8
    • Krysko DV, D'Herde K, Vandenabeele P (2006) Clearance of apoptotic and necrotic cells and its immunological consequences. Apoptosis 11:1709-1726 (Pubitemid 44371047)
    • (2006) Apoptosis , vol.11 , Issue.10 , pp. 1709-1726
    • Krysko, D.V.1    D'Herde, K.2    Vandenabeele, P.3
  • 73
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok VA, Voelker DR, Campbell PA, Cohen JJ, Bratton DL, Henson PM (1992) Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J Immunol 148:2207-2216
    • (1992) J Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 74
    • 3343013154 scopus 로고    scopus 로고
    • Phosphatidylserine exposure during early primary necrosis (oncosis) in JB6 cells as evidenced by immunogold labeling technique
    • DOI 10.1023/B:APPT.0000031452.75162.75
    • Krysko O, De RL, Cornelissen M (2004) Phosphatidylserine exposure during early primary necrosis (oncosis) in JB6 cells as evidenced by immunogold labeling technique. Apoptosis 9:495-500 (Pubitemid 38987586)
    • (2004) Apoptosis , vol.9 , Issue.4 , pp. 495-500
    • Krysko, O.1    De Ridder, L.2    Cornelissen, M.3
  • 75
    • 0141893347 scopus 로고    scopus 로고
    • Rapid, noninflammatory and PS-dependent phagocytic clearance of necrotic cells
    • DOI 10.1038/sj.cdd.4401286
    • Hirt UA, Leist M (2003) Rapid, noninflammatory and PS-dependent phagocytic clearance of necrotic cells. Cell Death Differ 10:1156-1164 (Pubitemid 37258581)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.10 , pp. 1156-1164
    • Hirt, U.A.1    Leist, M.2
  • 76
    • 27444447371 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein specifically binds to necrotic cells via its amino-terminal domain and facilitates necrotic cell phagocytosis
    • DOI 10.1074/jbc.M504384200
    • Jones AL, Poon IK, Hulett MD, Parish CR (2005) Histidine-rich glycoprotein specifically binds to necrotic cells via its aminoterminal domain and facilitates necrotic cell phagocytosis. J Biol Chem 280:35733-35741 (Pubitemid 41532766)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35733-35741
    • Jones, A.L.1    Poon, I.K.H.2    Hulett, M.D.3    Parish, C.R.4
  • 77
    • 0036209630 scopus 로고    scopus 로고
    • Phagocytosis by macrophages mediated by receptors for denatured protein - Dependence on tyrosine protein kinases
    • Hespanhol MR, Mantovani B (2002) Phagocytosis bymacrophages mediated by receptors for denatured proteins - dependence on tyrosine protein kinases. Braz J Med Biol Res 35:383-389 (Pubitemid 34285513)
    • (2002) Brazilian Journal of Medical and Biological Research , vol.35 , Issue.3 , pp. 383-389
    • Hespanhol, M.R.1    Mantovani, B.2
  • 78
    • 0026736029 scopus 로고
    • The Mac-1 and p150,95 beta 2 integrins bind denatured proteins to mediate leukocyte cell-substrate adhesion
    • Davis GE (1992) The Mac-1 and p150,95 beta 2 integrins bind denatured proteins to mediate leukocyte cell-substrate adhesion. Exp Cell Res 200:242-252
    • (1992) Exp Cell Res , vol.200 , pp. 242-252
    • Davis, G.E.1
  • 79
    • 0024793675 scopus 로고
    • Human mononuclear cells contain an endoglycosidase specific for heparan sulphate glycosaminoglycan demonstrable with the use of a specific solid-phase metabolically radiolabelled substrate
    • Sewell RF, Brenchley PE, Mallick NP (1989) Human mononuclear cells contain an endoglycosidase specific for heparan sulphate glycosaminoglycan demonstrable with the use of a specific solid-phase metabolically radiolabelled substrate. Biochem J 264:777-783 (Pubitemid 20023449)
    • (1989) Biochemical Journal , vol.264 , Issue.3 , pp. 777-783
    • Sewell, R.F.1    Brenchley, P.E.C.2    Mallick, N.P.3
  • 80
    • 0025501812 scopus 로고
    • Heparanase activity expressed by platelets, neutrophils, and lymphoma cells releases active fibroblast growth factor from extracellular matrix
    • Ishai-Michaeli R, Eldor A, Vlodavsky I (1990) Heparanase activity expressed by platelets, neutrophils, and lymphoma cells releases active fibroblast growth factor from extracellular matrix. Cell Regul 1:833-842
    • (1990) Cell Regul , vol.1 , pp. 833-842
    • Ishai-Michaeli, R.1    Eldor, A.2    Vlodavsky, I.3
  • 82
    • 0031966911 scopus 로고    scopus 로고
    • Regulation of platelet heparanase during inflammation: Role of pH and proteinases
    • DOI 10.1002/(SICI)1097-4652(199806)175:3<255::AID-
    • Ihrcke NS, Parker W, Reissner KJ, Platt JL (1998) Regulation of platelet heparanase during inflammation: role of pH and proteinases. J Cell Physiol 175:255-267 (Pubitemid 28198205)
    • (1998) Journal of Cellular Physiology , vol.175 , Issue.3 , pp. 255-267
    • Ihrcke, N.S.1    Parker, W.2    Reissner, K.J.3    Platt, J.L.4
  • 84
    • 0034937208 scopus 로고    scopus 로고
    • Heparanases: Endoglycosidases that degrade heparan sulfate proteoglycans
    • Bame KJ (2001) Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans. Glycobiology 11:91R-98R
    • (2001) Glycobiology , vol.11
    • Bame, K.J.1
  • 85
    • 0017695457 scopus 로고
    • Adsorbed proteins mask negatively charged sites of the erythrocyte
    • Geyer G, Linss W, Stibenz D (1977) Adsorbed proteins mask negatively charged sites of the erythrocyte glycocalyx. Acta Histochem 60:312-316 (Pubitemid 8247829)
    • (1977) Acta Histochemica , vol.60 , Issue.2 , pp. 312-316
    • Geyer, G.1    Linss, W.2    Stibenz, D.3
  • 86
    • 0017178739 scopus 로고
    • Platelet glycocalicin. I. Orientation of glycoproteins of the human platelet surface
    • Okumura T, Jamieson GA (1976) Platelet glycocalicin. I. Orientation of glycoproteins of the human platelet surface, J. Biol Chem 251:5944-5949
    • (1976) J. Biol Chem , vol.251 , pp. 5944-5949
    • Okumura, T.1    Jamieson, G.A.2
  • 87
    • 0028806512 scopus 로고
    • Ultrastructural demonstration of endothelial glycocalyx disruption in the reperfused rat heart. Involvement of oxygen free radicals
    • Czarnowska E, Karwatowska-Prokopczuk E (1995) Ultrastructural demonstration of endothelial glycocalyx disruption in the reperfused rat heart. Involvement of oxygen free radicals. Basic Res Cardiol 90:357-364
    • (1995) Basic Res Cardiol , vol.90 , pp. 357-364
    • Czarnowska, E.1    Karwatowska-Prokopczuk, E.2
  • 88
    • 84859008844 scopus 로고    scopus 로고
    • Mechanistic overview of reactive species-induced degradation of the endothelial glycocalyx during hepatic ischemia/reperfusion injury
    • van Golen RF, van Gulik TM, Heger M (2012) Mechanistic overview of reactive species-induced degradation of the endothelial glycocalyx during hepatic ischemia/reperfusion injury. Free Radic Biol Med 52:1382-1402
    • (2012) Free Radic Biol Med , vol.52 , pp. 1382-1402
    • Van Golen, R.F.1    Van Gulik, T.M.2    Heger, M.3
  • 90
    • 27744543102 scopus 로고    scopus 로고
    • Inflammatory cells during wound repair: The good, the bad and the ugly
    • DOI 10.1016/j.tcb.2005.09.002, PII S0962892405002278
    • Martin P, Leibovich SJ (2005) Inflammatory cells during wound repair: the good, the bad and the ugly. Trends Cell Biol 15:599-607 (Pubitemid 41619424)
    • (2005) Trends in Cell Biology , vol.15 , Issue.11 , pp. 599-607
    • Martin, P.1    Leibovich, S.J.2
  • 95
    • 84880616430 scopus 로고    scopus 로고
    • Crossroads of coagulation and innate immunity: The case of deep vein thrombosis
    • Schulz C, Engelmann B, Massberg S (2013) Crossroads of coagulation and innate immunity: the case of deep vein thrombosis. J Thromb Haemost 11(Suppl 1):233-241
    • (2013) J Thromb Haemost , vol.11 , Issue.SUPPL. 1 , pp. 233-241
    • Schulz, C.1    Engelmann, B.2    Massberg, S.3
  • 96
    • 0025090039 scopus 로고
    • GMP-140 mediates adhesion of stimulated platelets to neutrophils
    • Hamburger SA, McEver RP (1990) GMP-140 mediates adhesion of stimulated platelets to neutrophils. Blood 75:550-554 (Pubitemid 20069190)
    • (1990) Blood , vol.75 , Issue.3 , pp. 550-554
    • Hamburger, S.A.1    McEver, R.P.2
  • 97
    • 0024357563 scopus 로고
    • PADGEM protein: A receptor that mediates the interaction of activated platelets with neutrophils and monocytes
    • DOI 10.1016/0092-8674(89)90292-4
    • Larsen E, Celi A, Gilbert GE, Furie BC, Erban JK, Bonfanti R, Wagner DD, Furie B (1989) PADGEM protein: a receptor that mediates the interaction of activated platelets with neutrophils and monocytes. Cell 59:305-312 (Pubitemid 19264376)
    • (1989) Cell , vol.59 , Issue.2 , pp. 305-312
    • Larsen, E.1    Celi, A.2    Gilbert, G.E.3    Furie, B.C.4    Erban, J.K.5    Bonfanti, R.6    Wagner, D.D.7    Furie, B.8
  • 99
    • 0028086420 scopus 로고
    • Structural requirements of platelet chemokines for neutrophil activation
    • Yan Z, Zhang J, Holt JC, Stewart GJ, Niewiarowski S, Poncz M (1994) Structural requirements of platelet chemokines for neutrophil activation. Blood 84:2329-2339 (Pubitemid 24296396)
    • (1994) Blood , vol.84 , Issue.7 , pp. 2329-2339
    • Yan, Z.1    Zhang, J.2    Holt, J.C.3    Stewart, G.J.4    Niewiarowski, S.5    Poncz, M.6
  • 100
    • 84883729969 scopus 로고    scopus 로고
    • Neutrophil cell surface receptors and their intracellular signal transduction pathways
    • Futosi K, Fodor S, Mocsai A (2013) Neutrophil cell surface receptors and their intracellular signal transduction pathways. Int Immunopharmacol 17:638-650
    • (2013) Int Immunopharmacol , vol.17 , pp. 638-650
    • Futosi, K.1    Fodor, S.2    Mocsai, A.3
  • 104
    • 0027484754 scopus 로고
    • Inhibition of apoptosis and prolongation of neutrophil functional longevity by inflammatory mediators
    • Lee A, Whyte MK, Haslett C (1993) Inhibition of apoptosis and prolongation of neutrophil functional longevity by inflammatory mediators. J Leukoc Biol 54:283-288 (Pubitemid 23317694)
    • (1993) Journal of Leukocyte Biology , vol.54 , Issue.4 , pp. 283-288
    • Lee, A.1    Whyte, M.K.B.2    Haslett, C.3
  • 106
    • 84937092509 scopus 로고
    • Wound healing: The role of the macrophage and other immune cells
    • DiPietro LA (1995)Wound healing: the role of the macrophage and other immune cells. Shock 4:233-240
    • (1995) Shock , vol.4 , pp. 233-240
    • DiPietro, L.A.1
  • 107
    • 27144476793 scopus 로고    scopus 로고
    • Activated platelets induce Weibel-Palade-body secretion and leukocyte rolling in vivo: Role of P-selectin
    • DOI 10.1182/blood-2005-04-1530
    • Dole VS, Bergmeier W, Mitchell HA, Eichenberger SC, Wagner DD (2005) Activated platelets induce Weibel-Palade-body secretion and leukocyte rolling in vivo: role of P-selectin. Blood 106:2334-2339 (Pubitemid 41510804)
    • (2005) Blood , vol.106 , Issue.7 , pp. 2334-2339
    • Dole, V.S.1    Bergmeier, W.2    Mitchell, H.A.3    Eichenberger, S.C.4    Wagner, D.D.5
  • 108
    • 0032484987 scopus 로고    scopus 로고
    • CD40 ligand on activated platelets triggers an inflammatory reaction of endothelial cells
    • DOI 10.1038/35393
    • Henn V, Slupsky JR, Grafe M, Anagnostopoulos I, Forster R, Muller-Berghaus G, Kroczek RA (1998) CD40 ligand on activated platelets triggers an inflammatory reaction of endothelial cells. Nature 391:591-594 (Pubitemid 28157601)
    • (1998) Nature , vol.391 , Issue.6667 , pp. 591-594
    • Henn, V.1    Slupsky, J.R.2    Grafe, M.3    Anagnostopoulos, I.4    Forster, R.5    Muller-Berghaus, G.6    Kroczek, R.A.7
  • 110
    • 0036433010 scopus 로고    scopus 로고
    • Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals
    • DOI 10.1046/j.1365-2567.2002.01469.x
    • Boehme MW, Galle P, Stremmel W (2002) Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals. Immunology 107:340-349 (Pubitemid 35356954)
    • (2002) Immunology , vol.107 , Issue.3 , pp. 340-349
    • Boehme, M.W.J.1    Galle, P.2    Stremmel, W.3
  • 112
    • 0035949524 scopus 로고    scopus 로고
    • Circulating monocyte-platelet aggregates are a more sensitive marker of in vivo platelet activation than platelet surface P-selectin: Studies in baboons, human coronary intervention, and human acute myocardial infarction
    • Michelson AD, Barnard MR, Krueger LA, Valeri CR, Furman MI (2001) Circulating monocyte-platelet aggregates are a more sensitive marker of in vivo platelet activation than platelet surface P-selectin: studies in baboons, human coronary intervention, and human acute myocardial infarction. Circulation 104:1533-1537 (Pubitemid 32917347)
    • (2001) Circulation , vol.104 , Issue.13 , pp. 1533-1537
    • Michelson, A.D.1    Barnard, M.R.2    Krueger, L.A.3    Valeri, C.R.4    Furman, M.I.5
  • 113
    • 35048896893 scopus 로고    scopus 로고
    • PSGL-1 regulates platelet P-selectin-mediated endothelial activation and shedding of P-selectin from activated platelets
    • DOI 10.1160/TH07-03-0207
    • Dole VS, Bergmeier W, Patten IS, Hirahashi J, Mayadas TN, Wagner DD (2007) PSGL-1 regulates platelet P-selectin-mediated endothelial activation and shedding of P-selectin from activated platelets. Thromb Haemost 98:806-812 (Pubitemid 47555073)
    • (2007) Thrombosis and Haemostasis , vol.98 , Issue.4 , pp. 806-812
    • Dole, V.S.1    Bergmeier, W.2    Patten, I.S.3    Hirahashi, J.4    Mayadas, T.N.5    Wagner, D.D.6
  • 114
    • 66549108876 scopus 로고    scopus 로고
    • P-selectin cross-links PSGL-1 and enhances neutrophil adhesion to fibrinogen and ICAM-1 in a Src kinase-dependent, but GPCR-independent mechanism
    • Xu T, Zhang L, Geng ZH, Wang HB, Wang JT, Chen M, Geng JG (2007) P-selectin cross-links PSGL-1 and enhances neutrophil adhesion to fibrinogen and ICAM-1 in a Src kinase-dependent, but GPCR-independent mechanism. Cell Adhes Migr 1:115-123
    • (2007) Cell Adhes Migr , vol.1 , pp. 115-123
    • Xu, T.1    Zhang, L.2    Geng, Z.H.3    Wang, H.B.4    Wang, J.T.5    Chen, M.6    Geng, J.G.7
  • 115
    • 4944222601 scopus 로고    scopus 로고
    • P-selectin binding to P-selectin glycoprotein ligand-1 induces an intermediate state of alphaMbeta2 activation and acts cooperatively with extracellular stimuli to support maximal adhesion of human neutrophils
    • DOI 10.1182/blood-2004-03-1108
    • Ma YQ, Plow EF, Geng JG (2004) P-selectin binding to P-selectin glycoprotein ligand-1 induces an intermediate state of alphaMbeta2 activation and acts cooperatively with extracellular stimuli to support maximal adhesion of human neutrophils. Blood 104:2549-2556 (Pubitemid 39331860)
    • (2004) Blood , vol.104 , Issue.8 , pp. 2549-2556
    • Ma, Y.-Q.1    Plow, E.F.2    Geng, J.-G.3
  • 116
    • 12444303861 scopus 로고    scopus 로고
    • Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P-selectin glycoprotein ligand 1 and platelet P-selectin
    • DOI 10.1084/jem.20021868
    • Falati S, Liu Q, Gross P, Merrill-Skoloff G, Chou J, Vandendries E, Celi A, Croce K, Furie BC, Furie B (2003) Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P-selectin glycoprotein ligand 1 and platelet P-selectin. J Exp Med 197:1585-1598 (Pubitemid 36682554)
    • (2003) Journal of Experimental Medicine , vol.197 , Issue.11 , pp. 1585-1598
    • Falati, S.1    Liu, Q.2    Gross, P.3    Merrill-Skoloff, G.4    Chou, J.5    Vandendries, E.6    Celi, A.7    Croce, K.8    Furie, B.C.9    Furie, B.10
  • 117
    • 29244449299 scopus 로고    scopus 로고
    • Neutrophil P-selectin-glycoprotein-ligand-I binding to platelet P-selectin enhances metalloproteinase 2 secretion and platelet-neutrophil aggregation
    • DOI 10.1160/TH05-05-0344
    • Abou-Saleh H, Theoret JF, Yacoub D, Merhi Y (2005) Neutrophil P-selectin-glycoprotein-ligand-1 binding to platelet P-selectin enhances metalloproteinase 2 secretion and platelet-neutrophil aggregation. Thromb Haemost 94:1230-1235 (Pubitemid 41819621)
    • (2005) Thrombosis and Haemostasis , vol.94 , Issue.6 , pp. 1230-1235
    • Abou-Saleh, H.1    Theoret, J.-F.2    Yacoub, D.3    Merhi, Y.4
  • 119
    • 0036464689 scopus 로고    scopus 로고
    • Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo
    • DOI 10.1182/blood.V99.3.1053
    • Szaba FM, Smiley ST (2002) Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. Blood 99:1053-1059 (Pubitemid 34525570)
    • (2002) Blood , vol.99 , Issue.3 , pp. 1053-1059
    • Szaba, F.M.1    Smiley, S.T.2
  • 121
    • 0030836224 scopus 로고    scopus 로고
    • Fibrin regulation of interleukin-8 gene expression in human vascular endothelial cells
    • Qi J, Goralnick S, Kreutzer DL (1997) Fibrin regulation of interleukin-8 gene expression in human vascular endothelial cells. Blood 90:3595-3602 (Pubitemid 27473429)
    • (1997) Blood , vol.90 , Issue.9 , pp. 3595-3602
    • Qi, J.1    Goralnick, S.2    Kreutzer, D.L.3
  • 123
    • 62249113519 scopus 로고    scopus 로고
    • Thrombus resolution and vein wall injury: Dependence on chemokines and leukocytes
    • Henke PK, Wakefield TW (2009) Thrombus resolution and vein wall injury: dependence on chemokines and leukocytes. Thromb Res 123(Suppl 4):S72-S78
    • (2009) Thromb Res , vol.123 , Issue.SUPPL. 4
    • Henke, P.K.1    Wakefield, T.W.2
  • 130
  • 131
    • 0026766903 scopus 로고
    • Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils
    • Kameyoshi Y, Dorschner A, Mallet AI, Christophers E, Schroder JM (1992) Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils. J Exp Med 176:587-592
    • (1992) J Exp Med , vol.176 , pp. 587-592
    • Kameyoshi, Y.1    Dorschner, A.2    Mallet, A.I.3    Christophers, E.4    Schroder, J.M.5
  • 132
    • 0028913968 scopus 로고
    • Monocyte tethering by P-selectin regulates monocyte chemotactic protein-1 and tumor necrosis factor-alpha secretion. Signal integration and NF-kappa B translocation
    • Weyrich AS, McIntyre TM, McEver RP, Prescott SM, Zimmerman GA (1995) Monocyte tethering by P-selectin regulates monocyte chemotactic protein-1 and tumor necrosis factor-alpha secretion. Signal integration and NF-kappa B translocation. J Clin Invest 95:2297-2303
    • (1995) J Clin Invest , vol.95 , pp. 2297-2303
    • Weyrich, A.S.1    McIntyre, T.M.2    McEver, R.P.3    Prescott, S.M.4    Zimmerman, G.A.5
  • 133
    • 0023689904 scopus 로고
    • Differentiation of mononuclear blood cells into macrophages, fibroblasts and endothelial cells in thrombus organization
    • Leu HJ, Feigl W, Susani M, Odermatt B (1988) Differentiation of mononuclear blood cells into macrophages, fibroblasts and endothelial cells in thrombus organization. Exp Cell Biol 56:201-210 (Pubitemid 18260945)
    • (1988) Experimental Cell Biology , vol.56 , Issue.4 , pp. 201-210
    • Leu, H.J.1    Feigl, W.2    Susani, M.3    Odermatt, B.4
  • 135
    • 0035009039 scopus 로고    scopus 로고
    • Polymorphonuclear leucocytes mediate endogenous thrombus lysis via a u-PA-dependent mechanism
    • DOI 10.1046/j.1365-2141.2001.02696.x
    • Moir E, Booth NA, Bennett B, Robbie LA (2001) Polymorphonuclear leucocytes mediate endogenous thrombus lysis via a u-PA-dependent mechanism. Br J Haematol 113:72-80 (Pubitemid 32423305)
    • (2001) British Journal of Haematology , vol.113 , Issue.1 , pp. 72-80
    • Moir, E.1    Booth, N.A.2    Bennett, B.3    Robbie, L.A.4
  • 136
    • 0037448801 scopus 로고    scopus 로고
    • Failure of thrombus to resolve in urokinase-type plasminogen activator gene-knockout mice: Rescue by normal bone marrow-derived cells
    • DOI 10.1161/01.CIR.0000050149.22928.39
    • Singh I, Burnand KG, Collins M, Luttun A, Collen D, Boelhouwer B, Smith A (2003) Failure of thrombus to resolve in urokinase-type plasminogen activator gene-knockout mice: rescue by normal bone marrow-derived cells. Circulation 107:869-875 (Pubitemid 36241046)
    • (2003) Circulation , vol.107 , Issue.6 , pp. 869-875
    • Singh, I.1    Burnand, K.G.2    Collins, M.3    Luttun, A.4    Collen, D.5    Boelhouwer, B.6    Smith, A.7
  • 138
    • 0023940734 scopus 로고
    • Oxidative inactivation of purified human alpha-2-antiplasmin, antithrombin III, and C1-inhibitor
    • Stief TW, Aab A, Heimburger N (1988) Oxidative inactivation of purified human alpha-2-antiplasmin, antithrombin III, and C1-inhibitor. Thromb Res 49:581-589
    • (1988) Thromb Res , vol.49 , pp. 581-589
    • Stief, T.W.1    Aab, A.2    Heimburger, N.3
  • 139
    • 0029134020 scopus 로고
    • The cleavage and inactivation of plasminogen activator inhibitor type 1 by neutrophil elastase: The evaluation of its physiologic relevance in fibrinolysis
    • Wu K, Urano T, Ihara H, Takada Y, Fujie M, Shikimori M, Hashimoto K, Takada A (1995) The cleavage and inactivation of plasminogen activator inhibitor type 1 by neutrophil elastase: the evaluation of its physiologic relevance in fibrinolysis. Blood 86:1056-1061
    • (1995) Blood , vol.86 , pp. 1056-1061
    • Wu, K.1    Urano, T.2    Ihara, H.3    Takada, Y.4    Fujie, M.5    Shikimori, M.6    Hashimoto, K.7    Takada, A.8
  • 140
    • 0000200197 scopus 로고
    • Leukokinetic studies. IV. The total blood, circulating and marginal granulocyte pools and the granulocyte turnover rate in normal subjects
    • Athens JW, Haab OP, Raab SO, Mauer AM, Ashenbrucker H, Cartwright GE, Wintrobe MM (1961) Leukokinetic studies. IV. The total blood, circulating and marginal granulocyte pools and the granulocyte turnover rate in normal subjects. J Clin Invest 40:989-995
    • (1961) J Clin Invest , vol.40 , pp. 989-995
    • Athens, J.W.1    Haab, O.P.2    Raab, S.O.3    Mauer, A.M.4    Ashenbrucker, H.5    Cartwright, G.E.6    Wintrobe, M.M.7
  • 143
    • 0014359229 scopus 로고
    • Leukocyte labeling with 51-chromium. I. Technique and results in normal subjects
    • McMillan R, Scott JL (1968) Leukocyte labeling with 51-chromium. I. Technique and results in normal subjects. Blood 32:738-754
    • (1968) Blood , vol.32 , pp. 738-754
    • McMillan, R.1    Scott, J.L.2
  • 144
    • 61449208877 scopus 로고    scopus 로고
    • Induction of caspase- and reactive oxygen species-independent phosphatidylserine externalization in primary human neutrophils: Role in macrophage recognition and engulfment
    • Jitkaew S, Witasp E, Zhang S, Kagan VE, Fadeel B (2009) Induction of caspase- and reactive oxygen species-independent phosphatidylserine externalization in primary human neutrophils: role in macrophage recognition and engulfment. J Leukoc Biol 85:427-437
    • (2009) J Leukoc Biol , vol.85 , pp. 427-437
    • Jitkaew, S.1    Witasp, E.2    Zhang, S.3    Kagan, V.E.4    Fadeel, B.5
  • 145
    • 33750463432 scopus 로고    scopus 로고
    • Matrix metalloproteinases, their production by monocytes and macrophages and their potential role in HIV-related diseases
    • DOI 10.1189/jlb.0306152
    • Webster NL, Crowe SM (2006) Matrix metalloproteinases, their production by monocytes and macrophages and their potential role in HIV-related diseases. J Leukoc Biol 80:1052-1066 (Pubitemid 44646311)
    • (2006) Journal of Leukocyte Biology , vol.80 , Issue.5 , pp. 1052-1066
    • Webster, N.L.1    Crowe, S.M.2
  • 146
    • 0034693163 scopus 로고    scopus 로고
    • Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII
    • Hiller O, Lichte A, Oberpichler A, Kocourek A, Tschesche H (2000) Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of
    • (2000) J Biol Chem , vol.275 , pp. 33008-33013
    • Hiller, O.1    Lichte, A.2    Oberpichler, A.3    Kocourek, A.4    Tschesche, H.5
  • 147
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    • DOI 10.1016/S0092-8674(00)81768-7
    • Hiraoka N, Allen E, Apel IJ, Gyetko MR, Weiss SJ (1998) Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins. Cell 95:365-377 (Pubitemid 28507325)
    • (1998) Cell , vol.95 , Issue.3 , pp. 365-377
    • Hiraoka, N.1    Allen, E.2    Apel, I.J.3    Gyetko, M.R.4    Weiss, S.J.5
  • 148
    • 0031860311 scopus 로고    scopus 로고
    • Binding of latent matrix metalloproteinase 9 to fibrin: Activation via a plasmin-dependent pathway
    • DOI 10.1023/A:1022300216202
    • Makowski GS, Ramsby ML (1998) Binding of latent matrix metalloproteinase 9 to fibrin: activation via a plasmin-dependent pathway. Inflammation 22:287-305 (Pubitemid 28234157)
    • (1998) Inflammation , vol.22 , Issue.3 , pp. 287-305
    • Makowski, G.S.1    Ramsby, M.L.2
  • 149
    • 79251479406 scopus 로고    scopus 로고
    • Wound macrophages as key regulators of repair: Origin, phenotype, and function
    • Brancato SK, Albina JE (2011) Wound macrophages as key regulators of repair: origin, phenotype, and function. Am J Pathol 178:19-25
    • (2011) Am J Pathol , vol.178 , pp. 19-25
    • Brancato, S.K.1    Albina, J.E.2
  • 150
    • 0023104031 scopus 로고
    • Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
    • Postlethwaite AE, Keski-Oja J, Moses HL, Kang AH (1987) Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta. J Exp Med 165:251-256 (Pubitemid 17223686)
    • (1987) Journal of Experimental Medicine , vol.165 , Issue.1 , pp. 251-256
    • Postlethwaite, A.E.1    Keski-Oja, J.2    Moses, H.L.3    Kang, A.H.4
  • 151
    • 0025347812 scopus 로고
    • Bifunctional effects of transforming growth factor-beta on migration of cultured rat aortic smooth muscle cells
    • DOI 10.1016/0006-291X(90)90391-Y
    • Koyama N, Koshikawa T, Morisaki N, Saito Y, Yoshida S (1990) Bifunctional effects of transforming growth factor-beta onmigration of cultured rat aortic smooth muscle cells. Biochem Biophys Res Commun 169:725-729 (Pubitemid 20216168)
    • (1990) Biochemical and Biophysical Research Communications , vol.169 , Issue.2 , pp. 725-729
    • Koyama, N.1    Koshikawa, T.2    Morisaki, N.3    Saito, Y.4    Yoshida, S.5
  • 152
    • 0025222517 scopus 로고
    • The transforming growth factor-beta family
    • Massague J (1990) The transforming growth factor-beta family. Annu Rev Cell Biol 6:597-641
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 597-641
    • Massague, J.1
  • 153
    • 0035907240 scopus 로고    scopus 로고
    • Identification of novel TGF-beta /Smad gene targets in dermal fibroblasts using a combined cDNA microarray/promoter transactivation approach
    • Verrecchia F, Chu ML, Mauviel A (2001) Identification of novel TGF-beta /Smad gene targets in dermal fibroblasts using a combined cDNA microarray/promoter transactivation approach. J Biol Chem 276:17058-17062
    • (2001) J Biol Chem , vol.276 , pp. 17058-17062
    • Verrecchia, F.1    Chu, M.L.2    Mauviel, A.3
  • 155
    • 0029029807 scopus 로고
    • Release and activation of platelet latent TGF-beta in blood clots during dissolution with plasmin
    • Grainger DJ, Wakefield L, Bethell HW, Farndale RW, Metcalfe JC (1995) Release and activation of platelet latent TGF-beta in blood clots during dissolution with plasmin. Nat Med 1:932-937
    • (1995) Nat Med , vol.1 , pp. 932-937
    • Grainger, D.J.1    Wakefield, L.2    Bethell, H.W.3    Farndale, R.W.4    Metcalfe, J.C.5
  • 156
    • 0035877019 scopus 로고    scopus 로고
    • Peripheral blood fibrocytes: Differentiation pathway and migration to wound sites
    • Abe R, Donnelly SC, Peng T, Bucala R, Metz CN (2001) Peripheral blood fibrocytes: differentiation pathway and migration to wound sites. J Immunol 166:7556-7562 (Pubitemid 32525636)
    • (2001) Journal of Immunology , vol.166 , Issue.12 , pp. 7556-7562
    • Abe, R.1    Donnelly, S.C.2    Peng, T.3    Bucala, R.4    Metz, C.N.5
  • 158
    • 84865727895 scopus 로고    scopus 로고
    • Vasa vasorum quantification in human varicose great and small saphenous veins
    • Tonar Z, Kural T Jr, Kochova P, Nedorost L, Witter K (2012) Vasa vasorum quantification in human varicose great and small saphenous veins. Ann Anat 194:473-481
    • (2012) Ann Anat , vol.194 , pp. 473-481
    • Tonar, Z.1    Kural Jr., T.2    Kochova, P.3    Nedorost, L.4    Witter, K.5
  • 162
    • 24944455016 scopus 로고    scopus 로고
    • Phosphatidylserine-specific receptor contributes to TGF-beta production in macrophages through a MAP kinase, ERK
    • DOI 10.1248/bpb.28.1707
    • Otsuka M, Goto K, Tsuchiya S, Aramaki Y (2005) Phosphatidylserine- specific receptor contributes to TGF-beta production in macrophages through a MAP kinase, ERK. Biol Pharm Bull 28:1707-1710 (Pubitemid 41324137)
    • (2005) Biological and Pharmaceutical Bulletin , vol.28 , Issue.9 , pp. 1707-1710
    • Otsuka, M.1    Goto, K.2    Tsuchiya, S.3    Aramaki, Y.4
  • 163
    • 33746731651 scopus 로고    scopus 로고
    • HMGB1 signals through toll-like receptor (TLR) 4 and TLR2
    • DOI 10.1097/01.shk.0000225404.51320.82, PII 0002438220060800000011
    • Yu M, Wang HC, Ding AH, Golenbock DT, Latz E, Czura CJ, Fenton MJ, Tracey KJ, Yang H (2006) HMGB1 signals through toll-like receptor (TLR) 4 and TLR2. Shock 26:174-179 (Pubitemid 44162504)
    • (2006) Shock , vol.26 , Issue.2 , pp. 174-179
    • Yu, M.1    Wang, H.2    Ding, A.3    Golenbock, D.T.4    Latz, E.5    Czura, C.J.6    Fenton, M.J.7    Tracey, K.J.8    Yang, H.9
  • 165
    • 23844482773 scopus 로고    scopus 로고
    • Heat shock proteins as endogenous adjuvants in sterile and septic inflammation
    • Quintana FJ, Cohen IR (2005) Heat shock proteins as endogenous adjuvants in sterile and septic inflammation. J Immunol 175:2777-2782 (Pubitemid 41170492)
    • (2005) Journal of Immunology , vol.175 , Issue.5 , pp. 2777-2782
    • Quintana, F.J.1    Cohen, I.R.2
  • 166
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s Use Toll-like Receptor 2 (TLR2) and TLR4 to Activate the Toll/Interleukin-1 Receptor Signaling Pathway in Innate Immune Cells
    • DOI 10.1074/jbc.M103217200
    • Vabulas RM, Ahmad-Nejad P, da Costa C, Miethke T, Kirschning CJ, Hacker H, Wagner H (2001) Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells. J Biol Chem 276:31332-31339 (Pubitemid 37385004)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.33 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    Da, C.C.3    Miethke, T.4    Kirschning, C.J.5    Hacker, H.6    Wagner, H.7
  • 167
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • DOI 10.1016/S1074-7613(01)00111-X
    • Basu S, Binder RJ, Ramalingam T, Srivastava PK (2001) CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14:303-313 (Pubitemid 32289294)
    • (2001) Immunity , vol.14 , Issue.3 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 168
    • 0032101585 scopus 로고    scopus 로고
    • Effect of hyperthermia on the transcription rate of heat-shock genes in the rabbit cerebellum and retina assayed by nuclear run-ons
    • DOI 10.1002/(SICI)1097-4547(19980601)52:5<538::AID
    • D'Souza CA, Rush SJ, Brown IR (1998) Effect of hyperthermia on the transcription rate of heat-shock genes in the rabbit cerebellum and retina assayed by nuclear run-ons. J Neurosci Res 52:538-548 (Pubitemid 28252735)
    • (1998) Journal of Neuroscience Research , vol.52 , Issue.5 , pp. 538-548
    • D'Souza, C.A.1    Rush, S.J.2    Brown, I.R.3
  • 169
    • 0031794722 scopus 로고    scopus 로고
    • Regulation of heat shock protein 27 expression of prostatic cells in response to heat treatment
    • DOI 10.1002/(SICI)1097-0045(19981101)37:3<174::AID
    • Madersbacher S, Grobl M, Kramer G, Dirnhofer S, Steiner GE, Marberger M (1998) Regulation of heat shock protein 27 expression of prostatic cells in response to heat treatment. Prostate 37:174-181 (Pubitemid 28487900)
    • (1998) Prostate , vol.37 , Issue.3 , pp. 174-181
    • Madersbacher, S.1    Grobl, M.2    Kramer, G.3    Dirnhofer, S.4    Steiner, G.E.5    Marberger, M.6
  • 170
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • DOI 10.1074/jbc.272.14.9086
    • Bush KT, Goldberg AL, Nigam SK (1997) Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J Biol Chem 272:9086-9092 (Pubitemid 27154911)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 171
    • 58849151813 scopus 로고    scopus 로고
    • Cutting edge: Critical role for mesothelial cells in necrosis-induced inflammation through the recognition of IL-1 alpha released from dying cells
    • Eigenbrod T, Park JH, Harder J, Iwakura Y, Nunez G (2008) Cutting edge: critical role for mesothelial cells in necrosis-induced inflammation through the recognition of IL-1 alpha released from dying cells. J Immunol 181:8194-8198
    • (2008) J Immunol , vol.181 , pp. 8194-8198
    • Eigenbrod, T.1    Park, J.H.2    Harder, J.3    Iwakura, Y.4    Nunez, G.5
  • 172
    • 34447116244 scopus 로고    scopus 로고
    • Identification of a key pathway required for the sterile inflammatory response triggered by dying cells
    • DOI 10.1038/nm1603, PII NM1603
    • Chen CJ, Kono H, Golenbock D, Reed G, Akira S, Rock KL (2007) Identification of a key pathway required for the sterile inflammatory response triggered by dying cells. Nat Med 13:851-856 (Pubitemid 47038190)
    • (2007) Nature Medicine , vol.13 , Issue.7 , pp. 851-856
    • Chen, C.-J.1    Kono, H.2    Golenbock, D.3    Reed, G.4    Akira, S.5    Rock, K.L.6
  • 173
    • 0022857822 scopus 로고
    • Inducible interleukin-1 gene expression in human vascular smooth muscle cells
    • Libby P, Ordovas JM, Birinyi LK, Auger KR, Dinarello CA (1986) Inducible interleukin-1 gene-expression in human vascular smoothmuscle cells. J Clin Investig 78:1432-1438 (Pubitemid 17219503)
    • (1986) Journal of Clinical Investigation , vol.78 , Issue.6 , pp. 1432-1438
    • Libby, P.1    Ordovas, J.M.2    Birinyi, L.K.3
  • 174
    • 53749093767 scopus 로고    scopus 로고
    • The IL-1-like cytokine IL-33 is constitutively expressed in the nucleus of endothelial cells and epithelial cells in vivo: A novel 'alarmin'?
    • Moussion C, Ortega N, Girard JP (2008) The IL-1-like cytokine IL-33 is constitutively expressed in the nucleus of endothelial cells and epithelial cells in vivo: a novel 'alarmin'? Plos One 3:e3331
    • (2008) Plos One , vol.3
    • Moussion, C.1    Ortega, N.2    Girard, J.P.3
  • 175
    • 84857484469 scopus 로고    scopus 로고
    • Interleukin 33 as a mechanically responsive cytokine secreted by living cells
    • Kakkar R, Hei H, Dobner S, Lee RT (2012) Interleukin 33 as a mechanically responsive cytokine secreted by living cells. J Biol Chem 287:6941-6948
    • (2012) J Biol Chem , vol.287 , pp. 6941-6948
    • Kakkar, R.1    Hei, H.2    Dobner, S.3    Lee, R.T.4
  • 177
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • DOI 10.1038/nature00858
    • Scaffidi P, Misteli T, Bianchi ME (2002) Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 418:191-195 (Pubitemid 34773774)
    • (2002) Nature , vol.418 , Issue.6894 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 178
    • 84897077849 scopus 로고    scopus 로고
    • Necrotic but not apoptiotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF kappa B pathway
    • Basu S, Binder RJ, Suto R, Anderson K, Srivastava PK (2000) Necrotic but not apoptiotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF kappa B pathway. Cell Stress Chaperones 5:373
    • (2000) Cell Stress Chaperones , vol.5 , pp. 373
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.4    Srivastava, P.K.5
  • 180
    • 0024575751 scopus 로고
    • Human vascular smooth muscle cells. Target for and source of tumor necrosis factor
    • Warner SJ, Libby P (1989) Human vascular smooth-muscle cells - target for and source of tumor necrosis factor. J Immunol 142:100-109 (Pubitemid 19034728)
    • (1989) Journal of Immunology , vol.142 , Issue.1 , pp. 100-109
    • Warner, S.J.C.1    Libby, P.2
  • 182
    • 0028903124 scopus 로고
    • Human fibroblast growth factor-1 gene-expression in vascular smooth-muscle cells is modulated via an alternate promoter in response to serum and phorbol ester
    • Chotani MA, Payson RA, Winkles JA, Chiu IM (1995) human fibroblast growth factor-1 gene-expression in vascular smooth-muscle cells is modulated via an alternate promoter in response to serum and phorbol ester. Nucleic Acids Res 23:434-441
    • (1995) Nucleic Acids Res , vol.23 , pp. 434-441
    • Chotani, M.A.1    Payson, R.A.2    Winkles, J.A.3    Chiu, I.M.4
  • 185
    • 0032985184 scopus 로고    scopus 로고
    • Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase
    • Kan M, Wu XC, Wang F, McKeehan WL (1999) Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase. J Biol Chem 274:15947-15952
    • (1999) J Biol Chem , vol.274 , pp. 15947-15952
    • Kan, M.1    Wu, X.C.2    Wang, F.3    McKeehan, W.L.4
  • 186
    • 0037072456 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor-1 signaling induces osteopontin expression and vascular smooth muscle cell-dependent adventitial fibroblast migration in vitro
    • Li GH, Oparil S, Kelpke SS, Chen YF, Thompson JA (2002) Fibroblast growth factor receptor-1 signaling induces osteopontin expression and vascular smooth muscle cell-dependent adventitial fibroblast migration in vitro. Circulation 106:854-859
    • (2002) Circulation , vol.106 , pp. 854-859
    • Li, G.H.1    Oparil, S.2    Kelpke, S.S.3    Chen, Y.F.4    Thompson, J.A.5
  • 188
    • 0347986644 scopus 로고    scopus 로고
    • Fibroblast Growth Factor-I Transcriptionally Induces Membrane Type-I Matrix Metalloproteinase Expression in Prostate Carcinoma Cell Line
    • DOI 10.1002/pros.10293
    • Udayakumar TS, Nagle RB, Bowden GT (2004) Fibroblast growth factor-1 transcriptionally induces membrane type-1 matrix metalloproteinase expression in prostate carcinoma cell line. Prostate 58:66-75 (Pubitemid 38057990)
    • (2004) Prostate , vol.58 , Issue.1 , pp. 66-75
    • Udayakumar, T.S.1    Nagle, R.B.2    Bowden, G.T.3
  • 189
    • 0033935549 scopus 로고    scopus 로고
    • The mitogenic activity of fibroblast growth correlates with its internalization and limited processing
    • DOI 10.1002/1097-4652(200008)184:2<171::AID-JCP4
    • Grieb TA, Burgess WH (2000) The mitogenic activity of fibroblast growth factor-1 correlates with its internalization and limited proteolytic processing. J Cell Physiol 184:171-182 (Pubitemid 30432308)
    • (2000) Journal of Cellular Physiology , vol.184 , Issue.2 , pp. 171-182
    • Grieb, T.A.1    Burgess, W.H.2
  • 190
    • 0029958894 scopus 로고    scopus 로고
    • Role of the nuclear localization sequence in fibroblast growth factor-1-stimulated mitogenic pathways
    • Lin YZ, Yao SY, Hawiger J (1996) Role of the nuclear localization sequence in fibroblast growth factor-1-stimulated mitogenic pathways. J Biol Chem 271:5305-5308
    • (1996) J Biol Chem , vol.271 , pp. 5305-5308
    • Lin, Y.Z.1    Yao, S.Y.2    Hawiger, J.3
  • 191
    • 1542378406 scopus 로고    scopus 로고
    • Nonocclusion and Early Reopening of the Great Saphenous Vein after Endovenous Laser Treatment Is Fluence Dependent
    • DOI 10.1111/j.1524-4725.2004.30051.x
    • Proebstle TM, Krummenauer F, Gul D, Knop J (2004) Nonocclusion and early reopening of the great saphenous vein after endovenous laser treatment is fluence dependent. Dermatol Surg 30:174-178 (Pubitemid 38314006)
    • (2004) Dermatologic Surgery , vol.30 , Issue.2 I , pp. 174-178
    • Proebstle, T.M.1    Krummenauer, F.2    Gul, D.3    Knop, J.4
  • 192
    • 42249115855 scopus 로고    scopus 로고
    • Endovenous laser treatment of saphenous vein reflux: How much energy do we need to prevent recanalizations?
    • DOI 10.1177/1538574407311107
    • Vuylsteke M, Liekens K, Moons P, Mordon S (2008) Endovenous laser treatment of saphenous vein reflux: how much energy do we need to prevent recanalizations? Vasc Endovasc Surg 42:141-149 (Pubitemid 351550918)
    • (2008) Vascular and Endovascular Surgery , vol.42 , Issue.2 , pp. 141-149
    • Vuylsteke, M.1    Liekens, K.2    Moons, P.3    Mordon, S.4
  • 193
    • 67650875881 scopus 로고    scopus 로고
    • Vascular extracellularmatrix and arterial mechanics
    • Wagenseil JE, Mecham RP (2009) Vascular extracellularmatrix and arterial mechanics. Physiol Rev 89:957-989
    • (2009) Physiol Rev , vol.89 , pp. 957-989
    • Wagenseil, J.E.1    Mecham, R.P.2
  • 194
    • 77950871113 scopus 로고    scopus 로고
    • Adventitial fibroblasts in vascular structure and function: The role of oxidative stress and beyond
    • Di WH, Ratsep MT, Chapman A, Boyd R (2010) Adventitial fibroblasts in vascular structure and function: the role of oxidative stress and beyond. Can J Physiol Pharmacol 88:177-186
    • (2010) Can J Physiol Pharmacol , vol.88 , pp. 177-186
    • Di, W.H.1    Ratsep, M.T.2    Chapman, A.3    Boyd, R.4
  • 195
    • 43049092274 scopus 로고    scopus 로고
    • Metalloproteinases and their inhibitors: Regulators of wound healing
    • Gill SE, Parks WC (2008) Metalloproteinases and their inhibitors: regulators of wound healing. Int J Biochem Cell Biol 40:1334-1347
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1334-1347
    • Gill, S.E.1    Parks, W.C.2
  • 196
    • 2542478053 scopus 로고    scopus 로고
    • Wound healing: An overview of acute, fibrotic and delayed healing
    • d1-504
    • Diegelmann RF, Evans MC (2004)Wound healing: an overview of acute, fibrotic and delayed healing. Front Biosci 9:283-289 (Pubitemid 38925460)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 283-289
    • Diegelmann, R.F.1    Evans, M.C.2
  • 197
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO (1992) Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69:11-25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 198
    • 0028979348 scopus 로고
    • Integrin alpha 2 beta 1 is a positive regulator of collagenase (MMP-1) and collagen alpha 1(I) gene expression
    • Riikonen T, Westermarck J, Koivisto L, Broberg A, Kahari VM, Heino J (1995) Integrin alpha 2 beta 1 is a positive regulator of collagenase (MMP-1) and collagen alpha 1(I) gene expression. J Biol Chem 270:13548-13552
    • (1995) J Biol Chem , vol.270 , pp. 13548-13552
    • Riikonen, T.1    Westermarck, J.2    Koivisto, L.3    Broberg, A.4    Kahari, V.M.5    Heino, J.6
  • 199
    • 0028156640 scopus 로고
    • The effects of heating on the mechanical properties of arterial elastin
    • Lillie MA, Chalmers GW, Gosline JM (1994) The effects of heating on the mechanical properties of arterial elastin. Connect Tissue Res 31:23-35 (Pubitemid 2159631)
    • (1994) Connective Tissue Research , vol.31 , Issue.1 , pp. 23-35
    • Lillie, M.A.1    Chalmers, G.W.G.2    Gosline, J.M.3
  • 200
    • 70350218956 scopus 로고    scopus 로고
    • Chemical and thermal unfolding of glypican-1: Protective effect of heparan sulfate against heat-induced irreversible aggregation
    • Svensson G, Linse S, Mani K (2009) Chemical and thermal unfolding of glypican-1: protective effect of heparan sulfate against heat-induced irreversible aggregation. Biochemistry 48:9994-10004
    • (2009) Biochemistry , vol.48 , pp. 9994-10004
    • Svensson, G.1    Linse, S.2    Mani, K.3
  • 201
    • 0033824335 scopus 로고    scopus 로고
    • Mechanical stress-initiated signal transductions in vascular smooth muscle cells
    • Li C, Xu Q (2000) Mechanical stress-initiated signal transductions in vascular smooth muscle cells. Cell Signal 12:435-445
    • (2000) Cell Signal , vol.12 , pp. 435-445
    • Li, C.1    Xu, Q.2
  • 202
    • 0028142253 scopus 로고
    • Cell adhesion receptors for native and denatured type I collagens and fibronectin in rabbit arterial smooth muscle cells in culture
    • DOI 10.1006/excr.1994.1256
    • Yamamoto K, Yamamoto M (1994) Cell adhesion receptors for native and denatured type I collagens and fibronectin in rabbit arterial smooth muscle cells in culture. Exp Cell Res 214:258-263 (Pubitemid 24302400)
    • (1994) Experimental Cell Research , vol.214 , Issue.1 , pp. 258-263
    • Yamamoto, K.1    Yamamoto, M.2
  • 203
    • 0029124871 scopus 로고
    • Identification of integrins involved in cell adhesion to native and denatured type I collagens and the phenotypic transition of rabbit arterial smooth muscle cells
    • Yamamoto M, Yamato M, Aoyagi M, Yamamoto K (1995) Identification of integrins involved in cell adhesion to native and denatured type I collagens and the phenotypic transition of rabbit arterial smooth muscle cells. Exp Cell Res 219:249-256
    • (1995) Exp Cell Res , vol.219 , pp. 249-256
    • Yamamoto, M.1    Yamato, M.2    Aoyagi, M.3    Yamamoto, K.4
  • 204
    • 0141885257 scopus 로고    scopus 로고
    • Collagen directly stimulates bladder smooth muscle cell growth in vitro: Regulation by extracellular regulated mitogen activated protein kinase
    • DOI 10.1097/01.ju.0000091810.33953.13
    • Herz DB, Aitken K, Bagli DJ (2003) Collagen directly stimulates bladder smooth muscle cell growth in vitro: regulation by extracellular regulated mitogen activated protein kinase. J Urol 170:2072-2076 (Pubitemid 37255011)
    • (2003) Journal of Urology , vol.170 , Issue.5 , pp. 2072-2076
    • Herz, D.B.1    Aitken, K.2    Bagli, D.J.3
  • 205
    • 66949161978 scopus 로고    scopus 로고
    • The integrin alpha2beta1 agonist, aggretin, promotes proliferation and migration of VSMC through NF-kB translocation and PDGF production
    • Chung CH, Lin KT, Chang CH, Peng HC, Huang TF (2009) The integrin alpha2beta1 agonist, aggretin, promotes proliferation and migration of VSMC through NF-kB translocation and PDGF production. Br J Pharmacol 156:846-856
    • (2009) Br J Pharmacol , vol.156 , pp. 846-856
    • Chung, C.H.1    Lin, K.T.2    Chang, C.H.3    Peng, H.C.4    Huang, T.F.5
  • 208
    • 0033951271 scopus 로고    scopus 로고
    • Selective adhesion of macrophages to denatured forms of type I collagen is mediated by scavenger receptors
    • DOI 10.1016/S0945-053X(99)00052-9, PII S0945053X99000529
    • Gowen BB, Borg TK, Ghaffar A, Mayer EP (2000) Selective adhesion of macrophages to denatured forms of type I collagen is mediated by scavenger receptors. Matrix Biol 19:61-71 (Pubitemid 30109396)
    • (2000) Matrix Biology , vol.19 , Issue.1 , pp. 61-71
    • Gowen, B.B.1    Borg, T.K.2    Ghaffar, A.3    Mayer, E.P.4
  • 209
    • 0035800775 scopus 로고    scopus 로고
    • Ligands of macrophage scavenger receptor induce cytokine expression via differential modulation of protein kinase signaling pathways
    • Hsu HY, Chiu SL, Wen MH, Chen KY, Hua KF (2001) Ligands of macrophage scavenger receptor induce cytokine expression via differential modulation of protein kinase signaling pathways. J Biol Chem 276:28719-28730
    • (2001) J Biol Chem , vol.276 , pp. 28719-28730
    • Hsu, H.Y.1    Chiu, S.L.2    Wen, M.H.3    Chen, K.Y.4    Hua, K.F.5
  • 210
    • 33847074230 scopus 로고    scopus 로고
    • Phagocytosis and remodeling of collagen matrices
    • DOI 10.1016/j.yexcr.2006.12.019, PII S0014482707000055
    • Abraham LC, Dice JF, Lee K, Kaplan DL (2007) Phagocytosis and remodeling of collagen matrices. Exp Cell Res 313:1045-1055 (Pubitemid 46273449)
    • (2007) Experimental Cell Research , vol.313 , Issue.5 , pp. 1045-1055
    • Abraham, L.C.1    Dice, J.F.2    Lee, K.3    Kaplan, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.