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rdf:type |
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lifeskim:mentions |
umls-concept:C0033578,
umls-concept:C0040682,
umls-concept:C0431085,
umls-concept:C0542341,
umls-concept:C0597032,
umls-concept:C1314939,
umls-concept:C1332712,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1998811
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pubmed:issue |
3
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pubmed:dateCreated |
1998-4-30
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pubmed:abstractText |
CD44 isoforms, such as CD44s (the standard form), contain at least one ankyrin-binding site within the 70-amino acid (aa) cytoplasmic domain and several hyaluronic acid (HA)-binding sites within the extracellular domain. To study the role of CD44s-ankyrin interaction in regulating human prostate tumor cells, we have constructed several CD44s cytoplasmic deletion mutants that lack the ankyrin-binding site(s). These truncated cDNAs were stably transfected into CD44-negative human prostate tumor cells (LNCaP). Our results indicate that a critical region of 15-amino acids (aa) between aa 304 and aa 318 of CD44s is required for ankyrin binding. Biochemical analyses, using competition binding assays with a synthetic peptide containing the 15 aa between aa 304 and aa 318 (NSGNGAVEDRKPSGL), further support the conclusion that this region contains the ankyrin-binding domain of CD44s. Deletion of this 15-aa ankyrin-binding sequence from CD44s results in a drastic reduction of HA-mediated binding/cell adhesion, Src p60 kinase(s) interaction and anchorage-independent growth in soft agar. These findings suggest that the binding of cytoskeletal proteins, such as ankyrin, to the cytoplasmic domain of CD44s plays a pivotal role in regulating HA-mediated functions as well as Src kinase activity and prostate tumor cell transformation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ankyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins pp60(c-src),
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Spectrin,
http://linkedlifedata.com/resource/pubmed/chemical/fodrin
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pubmed:status |
MEDLINE
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pubmed:issn |
0886-1544
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
209-22
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9519902-Amino Acid Sequence,
pubmed-meshheading:9519902-Ankyrins,
pubmed-meshheading:9519902-Antigens, CD44,
pubmed-meshheading:9519902-Carrier Proteins,
pubmed-meshheading:9519902-Cell Adhesion,
pubmed-meshheading:9519902-Cell Division,
pubmed-meshheading:9519902-Cell Transformation, Neoplastic,
pubmed-meshheading:9519902-DNA, Complementary,
pubmed-meshheading:9519902-Humans,
pubmed-meshheading:9519902-Hyaluronic Acid,
pubmed-meshheading:9519902-Male,
pubmed-meshheading:9519902-Microfilament Proteins,
pubmed-meshheading:9519902-Molecular Sequence Data,
pubmed-meshheading:9519902-Peptides,
pubmed-meshheading:9519902-Prostatic Neoplasms,
pubmed-meshheading:9519902-Protein Binding,
pubmed-meshheading:9519902-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:9519902-Recombinant Fusion Proteins,
pubmed-meshheading:9519902-Sequence Deletion,
pubmed-meshheading:9519902-Spectrin,
pubmed-meshheading:9519902-Tumor Cells, Cultured
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pubmed:year |
1998
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pubmed:articleTitle |
The ankyrin-binding domain of CD44s is involved in regulating hyaluronic acid-mediated functions and prostate tumor cell transformation.
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pubmed:affiliation |
Department of Cell Biology and Anatomy, University of Miami Medical School, Florida 33101, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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