Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1999-2-5
pubmed:abstractText
Very late antigen-4 (VLA-4)/vascular cell adhesion molecule-1 (VCAM-1) are a pair of adhesion molecules mediating cell-cell interaction. The binding activity of each depends on its surface expression, yet integrin activity can also be modulated through inside-out signaling. However, the specific intracellular molecules involved in modulating integrin VLA-4 activation via inside-out signaling or in regulating VCAM-1 expression are poorly understood. We show here that constitutive coexpression of cyclin C and c-Myc in hematopoietic BAF-B03 cells induces homotypic cell adhesion, which results from enhanced VLA-4 ligand-binding activity and induced expression of VCAM-1. Furthermore, regulation of cell adhesion appears to be a feature unique to cyclin C, but not other G1 cyclins, E and D3, and its regulatory function is independent of CDK8 kinase activity. Our results provide a novel role for cyclin C and c-Myc in the regulation of cell adhesion through distinct mechanisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Blocking, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29, http://linkedlifedata.com/resource/pubmed/chemical/CCNC protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CDK8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ccnc protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin C, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 8, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha4, http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha4beta1, http://linkedlifedata.com/resource/pubmed/chemical/Integrins, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Very Late Antigen, http://linkedlifedata.com/resource/pubmed/chemical/Vascular Cell Adhesion Molecule-1
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4700-11
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9845536-Animals, pubmed-meshheading:9845536-Antibodies, Blocking, pubmed-meshheading:9845536-Antigens, CD, pubmed-meshheading:9845536-Antigens, CD29, pubmed-meshheading:9845536-Cell Adhesion, pubmed-meshheading:9845536-Cell Adhesion Molecules, pubmed-meshheading:9845536-Cell Cycle, pubmed-meshheading:9845536-Cell Division, pubmed-meshheading:9845536-Cell Line, pubmed-meshheading:9845536-Cyclin C, pubmed-meshheading:9845536-Cyclin-Dependent Kinase 8, pubmed-meshheading:9845536-Cyclin-Dependent Kinases, pubmed-meshheading:9845536-Cyclins, pubmed-meshheading:9845536-Enzyme Activation, pubmed-meshheading:9845536-Hematopoietic Stem Cells, pubmed-meshheading:9845536-Humans, pubmed-meshheading:9845536-Integrin alpha4, pubmed-meshheading:9845536-Integrin alpha4beta1, pubmed-meshheading:9845536-Integrins, pubmed-meshheading:9845536-Mice, pubmed-meshheading:9845536-Protein-Serine-Threonine Kinases, pubmed-meshheading:9845536-Proto-Oncogene Proteins c-myc, pubmed-meshheading:9845536-Receptors, Lymphocyte Homing, pubmed-meshheading:9845536-Receptors, Very Late Antigen, pubmed-meshheading:9845536-Transfection, pubmed-meshheading:9845536-Vascular Cell Adhesion Molecule-1
pubmed:year
1998
pubmed:articleTitle
Functional cooperation of cyclin C and c-Myc in mediating homotypic cell adhesion via very late antigen-4 activation and vascular cell adhesion molecule-1 induction.
pubmed:affiliation
Department of Biochemistry and of Laboratory Medicine, Kobe University, School of Medicine, Kobe, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't