Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Sandra L. Fitzpatrick"'
Publikováno v:
Journal of Biological Chemistry. 279:7740-7750
The annexin A2-S100A10 heterotetramer (AIIt) is a multifunctional Ca(2+)-dependent, phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 subunits and two S100A10 subunits. It was reported previously that oxidative stres
Autor:
Kenneth S. Graham, Mary K. Young, Chang-Soon Yoon, David M. Waisman, Geetha Kassam, Mijung Kwon, Sandra L. Fitzpatrick
Publikováno v:
Biochemistry. 40:13246-13253
Tumor or tumor-associated cells cleave circulating plasminogen into three or four kringle-containing antiangiogenic fragments, collectively referred to as angiostatin. Angiostatin blocks tumor growth and metastasis by preventing the growth of endothe
Autor:
David M. Waisman, Peter Louie, Carol E. Braat, Akhil Manro, Geetha Kassam, Sandra L. Fitzpatrick
Publikováno v:
Biochemistry. 39:2140-2148
Fucoidan, a sulfated fucopolysaccharide, mimics the fucosylated glycans of glycoproteins and has therefore been used as a probe for investigating the role of membrane polysaccharides in cell-cell adhesion. In the present report we have characterized
Autor:
Mijung Kwon, Sandra L. Fitzpatrick, David M. Waisman, Geetha Kassam, Hyoung-Min Kang, Kyu-Sil Choi
Publikováno v:
Trends in Cardiovascular Medicine. 9:92-102
The enzymatic cascade triggered by activation of plasminogen has been implicated in a variety of normal and pathologic events, such as fibrinolysis, wound healing, tissue remodeling, embryogenesis, and the invasion and spread of transformed tumor cel
Autor:
Kyu-Sil Choi, Jaspinder Ghuman, David M. Waisman, Hyoung-Min Kang, Sandra L. Fitzpatrick, Geetha Kassam
Publikováno v:
Biochemistry. 37:648-655
In this paper, we have characterized the regulation of plasmin activity by annexin II tetramer (AIIt). Plasmin activity was measured by a fibrin lysis assay in which a fibrin polymer was produced from purified components and the extent of polymer lys
Autor:
David M. Waisman, Peter Louie, Akhil Manro, Sandra L. Fitzpatrick, Carol E. Braat, Geetha Kassam
Publikováno v:
Journal of Biological Chemistry. 272:15093-15100
In this report, we have characterized the interaction of heparin with the Ca2+- and phospholipid-binding protein annexin II tetramer (AIIt). Analysis of the circular dichroism spectra demonstrated that the Ca2+-dependent binding of AIIt to heparin ca
Publikováno v:
Biochemistry. 36:2041-2050
Annexin II tetramer (AIIt) is a Ca2+-dependent, phosphatidylserine-binding, and F-actin-bundling phosphoprotein which is localized to both the extracellular and cytoplasmic surfaces of the plasma membrane. The tetramer is composed of two p36 heavy ch
Autor:
Ismail Hubaishy, Donald J. Fujita, David M. Waisman, C. Bellagamba, Sandra L. Fitzpatrick, Jeffrey D. Bjorge
Publikováno v:
Journal of Biological Chemistry. 272:3195-3199
In the present article we have examined if the interaction of the Ca2+-binding protein, annexin II tetramer (AIIt) with the plasma membrane phospholipids or with the submembranous cytoskeleton, effects the accessibility of the tyrosine phosphorylatio
Autor:
Peter G. Jones, Sandra L. Fitzpatrick, I. Hubaishy, C. Bellagamba, David M. Waisman, D. J. Fujita, Jeffrey D. Bjorge
Publikováno v:
Biochemistry. 34:14527-14534
Annexin II tetramer (AIIt) is a Ca(2+)-dependent phospholipid-binding phosphoprotein. In cells either expressing transforming protein tyrosine kinases or treated with growth factors such as PDGF, AIIt has been shown to contain increased levels of pho
Publikováno v:
Biochemistry. 33:8180-8187
Chromaffin granules represent a substantial and exchangeable intracellular calcium pool which is thought to be regulated by a sodium/calcium exchange protein and also by a putative inositol trisphosphate-activated calcium channel. A family of calcium