 | Sanford J ShattilShow email addressDepartment of Medicine, University of California, San Diego, La Jolla, California, USA | Department of Medicine, University of California, San Diego, La Jolla, California. | ... |
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Sanford J Shattil:Expert Impact
Concepts for whichSanford J Shattilhas direct influence:Alpha iib,Platelet activation,Tyrosine phosphorylation,Integrin activation,Platelet aggregation,Activated platelets,Integrin αiibβ3,Iiia complex.
Sanford J Shattil:KOL impact
Concepts related to the work of other authors for whichfor which Sanford J Shattil has influence:Platelet activation,Cell adhesion,Tyrosine phosphorylation,Signal transduction,Protein kinase,Willebrand factor,Shear stress.
KOL Resume for Sanford J Shattil
| Year | |
|---|---|
| 2021 | Department of Medicine, University of California, San Diego, La Jolla, California, USA |
| 2020 | Department of Medicine, University of California, San Diego, La Jolla, California. |
| 2019 | University of California, San Diego Department of Medicine, UCSD, La Jolla, California, USA. |
| 2018 | Department of Medicine, University of California, San Diego, La Jolla, CA; |
| 2017 | Hematology-Oncology Division, Department of Medicine, University of California San Diego, Leichtag Biomedical Research Building, 9500 Gilman Drive, 92093-0726, La Jolla, CA, USA |
| 2016 | Division of Haematology-Oncology, Department of Medicine, University of California San Diego, 9500 Gilman Drive, 92093, La Jolla, California, USA |
| 2015 | Department of Medicine, University of California-San Diego, La Jolla, CA. |
| 2014 | Division of Hematology-Oncology, Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA Department of Medicine, University of California San Diego, La Jolla, California 92093-0726. |
| 2013 | University of California at San Diego |
| 2012 | Moores UCSD Cancer Center, University of California San Diego, La Jolla, California, United States of America Department of Medicine, University of California San Diego, La Jolla, CA, USA |
| 2011 | Dept. of Medicine, University of California San Diego, La Jolla, California |
| 2010 | Department of Medicine, University of California, San Diego, 9500 Gilman Drive, MC0612, La Jolla, CA 92093, USA |
| 2009 | Division of Hematology-Oncology, Department of Medicine University of California, San Diego, La Jolla, CA 92093, USA Department of Medicine, University of California San Diego, La Jolla; and |
| 2008 | Medicine, University of California San Diego, La Jolla, CA, USA |
| 2007 | Department of Medicine, UCSD School of Medicine, La Jolla, California, USA. Medicine, University of California, San Diego, La Jolla, CA, USA |
| 2006 | Hematology-Oncology Division, Department of Medicine, University of California San Diego, La Jolla, CA Department of Medicine, University of California San Diego, La Jolla; |
| 2005 | Department of Medicine, University of California San Diego, La Jolla California 92093, USA |
| 2004 | Assistant Professor, Division of Hematology-Oncology, Department of Medicine, University of California San Diego, La Jolla, California From the Department of Cell Biology and Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA; and National Cancer Institute CRO-IRCCS, Aviano, Italy Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037 |
| 2003 | Cell Biology and |
| 2002 | Departments of Vascular Biology and Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037 |
| 2001 | Vascular Biology, and |
| 2000 | Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037 and the Graduate Program in Immunology, the Departments of Vascular Biology and Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037 |
| 1999 | Departments of Vascular Biology From COR Therapeutics, Inc, South San Francisco, CA; Scripps Research Institute, La Jolla, CA; and National Institute Medical Research, Mill Hill, London, UK. |
| 1998 | Department of Vascular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California; and, Ehime University School of Medicine, Ehime, Japan |
| 1997 | Departments of Vascular Biology, The Scripps Research Institute, La Jolla, CA, USA Department of Vascular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037; and, Becton-Dickinson Immunocytometry Systems, San Jose, California 95131 Molecular and Experimental Medicine, The Scripps Research Institute La Jolla CA UK From COR Therapeutics, South San Francisco, Calif (D.R.P., W.T., A.A., L.N.-A., A.R., R.M.S.); University of Tennessee, Memphis (M.M.W., C.L., L.K.J.); Lilly Research Laboratories, Indianapolis, Ind (J.A.J.); and Scripps Research Institute (S.J.S.). |
| Concept | World rank |
|---|---|
| intravascular migration extravasation | #1 |
| adequate understanding principles | #1 |
| αvβ3 cterminal residues | #1 |
| precise localized regulation | #1 |
| platelets relative activation | #1 |
| requirement extracellular ca2 | #1 |
| megakaryopoiesis faknull megakaryocytes | #1 |
| aα95−98 | #1 |
| iiia complex | #1 |
| c5b9 release | #1 |
| beta3 tail scaffolds | #1 |
| ap73 pac11 | #1 |
| 14cserotonin release epinephrine | #1 |
| cholesterolrich platelets | #1 |
| 50 iibiiia binding | #1 |
| integrins characterization | #1 |
| surfacebound ca2 pools | #1 |
| carbenicillin techniques penicillin | #1 |
| gfprap1b | #1 |
| pac1 murine igg | #1 |
| αiibβ3 hemostasis | #1 |
| platelets stimulates syk | #1 |
| alphaiibbeta3 murine megakaryocytes | #1 |
| msupar2 | #1 |
| primary hemostasis derive | #1 |
| plasma anticoagulated | #1 |
| platelet fak expression | #1 |
| conditional oligomerization | #1 |
| gfprap1gap | #1 |
| hcdr3 binding | #1 |
| vinculindeficient platelets αiib | #1 |
| observations calpain | #1 |
| csrc beta3 | #1 |
| cterminal residues β1 | #1 |
| hescderived megakaryocytes | #1 |
| recruitment alphaiibbeta3 | #1 |
| dynamic molecular scaffold | #1 |
| inside signaling | #1 |
| function integrin alphaiibbeta3 | #1 |
| integrin β1b | #1 |
| agonists platelet surface | #1 |
| 260 kb segment | #1 |
| 125i pac1 | #1 |
| monoclonal antibody pac1 | #1 |
| pkc 3kinases phosphotransferases | #1 |
| pac1 antibodies | #1 |
| calpain activation effects | #1 |
| shear flow vivo | #1 |
| antibody pac1 | #1 |
| cholesterols phospholipid | #1 |
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Prominent publications by Sanford J Shattil
Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1
[ PUBLICATION ]
BACKGROUND: . Integrins induce the formation of large complexes of cytoskeletal and signaling proteins, which regulate many intracellular processes. The activation and assembly of signaling complexes involving focal adhesion kinase (FAK) occurs late in integrin signaling, downstream from actin polymerization. Our previous studies indicated that integrin-mediated activation of the non-receptor tyrosine kinase Syk in hematopoietic cells is independent of FAK and actin polymerization, and ...
| Known for Kinase Syk | Integrin Signaling | Actin Polymerization | Guanine Nucleotide Exchange | Hematopoietic Cells |
Tyrosine phosphorylation of multiple platelet proteins is stimulated by thrombin and other agonists that cause platelet aggregation and secretion. The phosphorylation of a subset of these proteins, including a protein tyrosine kinase, pp125FAK, is dependent on the platelet aggregation that follows fibrinogen binding to integrin alpha IIb beta 3. In this report, we examined whether fibrinogen binding, per se, triggers a process of tyrosine phosphorylation in the absence of exogenous ...
| Known for Alpha Iib | Beta 3 | Platelet Aggregation | Tyrosine Phosphorylation | Fibrinogen Binding |
Regulation of the protein tyrosine kinase pp72syk by platelet agonists and the integrin alpha IIb beta 3.
[ PUBLICATION ]
Agonist stimulation of platelets induces multiple waves of tyrosine phosphorylation, several of which are dependent on the integrin alpha IIb beta 3. At least two classes of protein tyrosine kinases are activated during various stages of platelet activation, 1) Src family tyrosine kinases are activated during an early phase of platelet activation by an integrin-independent mechanism and 2) pp125FAK is activated during a late stage of platelet activation, and it is dependent on platelet ...
| Known for Alpha Iib | Protein Tyrosine | Beta 3 | Platelet Agonists | Kinase Pp72syk |
Coordinate interactions of Csk, Src, and Syk kinases with αIIbβ3 initiate integrin signaling to the cytoskeleton
[ PUBLICATION ]
Integrins regulate cell adhesion and motility through tyrosine kinases, but initiation of this process is poorly understood. We find here that Src associates constitutively with integrin alphaIIbbeta3 in platelets. Platelet adhesion to fibrinogen caused a rapid increase in alphaIIbbeta3-associated Src activity, and active Src localized to filopodia and cell edges. Csk, which negatively regulates Src by phosphorylating Tyr-529, was also constitutively associated with alphaIIbbeta3. ...
| Known for Syk Kinase | Integrin Signaling | Src Csk | Fibrinogen Binding | Vav1 Vav3 |
Tyrosine phosphorylation of pp125FAK in platelets requires coordinated signaling through integrin and agonist receptors.
[ PUBLICATION ]
FAK is a focal adhesion kinase that is phosphorylated on tyrosine in activated platelets. Induction of FAK phosphorylation requires both fibrinogen binding to integrin alpha IIb beta 3 and post-occupancy events during agonist-induced platelet aggregation or platelet spreading on a fibrinogen matrix. To identify the signaling pathways necessary for tyrosine phosphorylation of FAK, we have examined the conditions that stimulate or inhibit this phosphorylation in platelets in which ...
| Known for Tyrosine Phosphorylation | Fak Platelets | Protein Kinase Pkc | Adhesion Kinase | Platelet Aggregation |
Integrin signaling: roles for the cytoplasmic tails of alpha IIb beta 3 in the tyrosine phosphorylation of pp125FAK.
[ PUBLICATION ]
pp125FAK (focal adhesion kinase) a protein tyrosine kinase that may mediate cellular responses to adhesion, is activated and tyrosine-phosphorylated when platelets adhere to fibrinogen via the integrin, alpha IIb beta 3. To determine whether either of the cytoplasmic tails of alpha IIb beta 3 regulates FAK phosphorylation, CHO cells were stably transfected with alpha IIb beta 3 or various cytoplasmic tail truncation mutants. Cells expressing wild-type alpha IIb beta 3 or alpha IIb beta 3 ...
| Known for Alpha Iib | Tyrosine Phosphorylation | Cytoplasmic Tail | Beta 3 | Fibrinogen Integrin |
Specific cleavage of the transmembrane molecule, CUB domain-containing protein-1 (CDCP1), by plasmin-like serine proteases induces outside–in signal transduction that facilitates early stages of spontaneous metastasis leading to tumor cell intravasation, namely cell escape from the primary tumor, stromal invasion and transendothelial migration. We identified active β1 integrin as a biochemical and functional partner of the membrane-retained 70-kDa CDCP1 fragment, newly generated from its ...
| Known for Β1 Integrin | Cleaved Cdcp1 | Serine Proteases | Fak Akt | Neoplasm Cell |
Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation.
[ PUBLICATION ]
Platelet activation is accompanied by the appearance on the platelet surface of approximately 45,000 receptor sites for fibrinogen. The binding of fibrinogen to these receptors is required for platelet aggregation. Although it is established that the fibrinogen receptor is localized to a heterodimer complex of the membrane glycoproteins, IIb and IIIa, little is known about the changes in this complex during platelet activation that result in the expression of the receptor. In the present ...
| Known for Iiia Complex | Platelet Membrane | Glycoprotein Iib | Fibrinogen Receptor | Pac1 Binding |
Mice deficient in the adaptor Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) exhibit a bleeding disorder and lack T cells. Linker for activation of T cells (LAT)-deficient mice exhibit a similar T cell phenotype, but show no signs of hemorrhage. Both SLP-76 and LAT are important for optimal platelet activation downstream of the collagen receptor, GPVI. In addition, SLP-76 is involved in signaling mediated by integrin alphaIIbbeta3. Because SLP-76 and LAT ...
| Known for Slp76 Lat | Cell Receptor | Differential Requirement | Integrin Alphaiibbeta3 | Proteins Mice |
pp72syk is essential for development and function of several hematopoietic cells, and it becomes activated through tandem SH2 interaction with ITAM motifs in immune response receptors. Since Syk is also activated through integrins, which do not contain ITAMs, a CHO cell model system was used to study Syk activation by the platelet integrin, alpha IIb beta 3. As in platelets, Syk underwent tyrosine phosphorylation and activation during CHO cell adhesion to alpha IIb beta 3 ligands, ...
| Known for Tyrosine Kinase | Platelet Integrin | Alpha Iib | Syk Activation | Cell Adhesion |
Activation of human platelets by complement proteins C5b-9 is accompanied by the release of small plasma membrane vesicles (microparticles) that are highly enriched in binding sites for coagulation factor Va and exhibit prothrombinase activity. We have now examined whether assembly of the prothrombinase enzyme complex (factors VaXa) is directly linked to the process of microparticle formation. Gel-filtered platelets were incubated without stirring with various agonists at 37 degrees C, ...
| Known for Scott Syndrome | Prothrombinase Complex | Isolated Defect | Platelets Microparticles | Platelet Plasma |
Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor.
[ PUBLICATION ]
To analyze the basis of affinity modulation of integrin function, we studied cloned stable Chinese hamster ovary cell lines expressing recombinant integrins of the beta 3 family (alpha IIb beta 3 and alpha v beta 3). Antigenic and peptide recognition specificities of the recombinant receptors resembled those of the native receptors found in platelets or endothelial cells. The alpha IIb beta 3-expressing cell line (A5) bound RGD peptides and immobilized fibrinogen (Fg) but not soluble ...
| Known for Beta 3 | Alpha Iib | Affinity Modulation | Intrinsic Property | Pac1 Platelets |
Modification of red cell membrane structure by cholesterol-rich lipid dispersions. A model for the primary spur cell defect.
[ PUBLICATION ]
Cholesterol-rich membranes are the hallmark of "spur" red cells. Spur cells accumulate cholesterol from cholesterol-rich serum lipoproteins. Previous studies suggested that this added cholesterol is responsible for both the altered morphology and the destruction of spur cells. To examine this process in the absence of other serum factors, cholesterol-lecithin dispersions with varying amounts of unesterified cholesterol (C) relative to phospholipid (P) were prepared, and their influence ...
| Known for Cell Membrane | Hdl Lipoproteins | Ldl Microscopy | Cholesterol Rich | Altered Morphology |
The platelet membrane glycoprotein IIb-IIIa complex (GPIIb-IIIa) recognizes peptides containing the amino acid sequence Arg-Gly-Asp, a sequence present at two locations in the alpha chain of fibrinogen. GPIIb-IIIa also interacts with peptides containing the carboxyl-terminal 10-15 residues of the fibrinogen gamma chain. We found that the alpha chain tetrapeptide, Arg-Gly-Asp-Ser (RGDS), and the gamma chain peptide, Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val (LGGAKQAG-DV), each inhibited ...
| Known for Gamma Chain | Binding Fibrinogen | Platelet Receptor | Gpiib Iiia | Differential Effects |
