Abstract

Preliminary data are presented which demonstrate the attachment of lymphoma cells to attachment-promoting molecules such as fibronectin and serum spreading factor. Data are also discussed which indicate that normal lymphocytes from the thymus interact with at least one of these molecules--serum spreading factor. It is proposed here to study the interactions of lymphoid cells with known adhesion molecules. A plan is also presented for the identification of novel molecules involved in mediating the attachment of normal lymphocytes. The fact that normal bone marrow cells attach to a monolayer of thymic epithelium indicates that such molecules exist. These molecules will be examined for structure, function, and tissue distribution. The hypothesis is that the selective attachment of immature lymphocytes to molecules within the thymus probably modulates their differentiation, path of migration, and response to external stimuli. Understanding these interactions will give insight into the behavior and development of lymphocytes as well as possibly provide a better understanding of the behavior of lymphoid tumors. New methods which involve the study of cell attachment to electrophoretically separated proteins are proposed for studying this problem. (LB)

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
2R01CA038352-04
Application #
3176449
Study Section
Pathobiochemistry Study Section (PBC)
Project Start
1984-03-15
Project End
1990-03-31
Budget Start
1987-07-01
Budget End
1988-06-30
Support Year
4
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Sanford-Burnham Medical Research Institute
Department
Type
DUNS #
009214214
City
La Jolla
State
CA
Country
United States
Zip Code
92037

  Publications

Tomasini-Johansson, B R; Ruoslahti, E; Pierschbacher, M D (1993) A 30 kD sulfated extracellular matrix protein immunologically crossreactive with vitronectin. Matrix 13:203-14
Cardarelli, P M; Crispe, I N; Pierschbacher, M D (1988) Preferential expression of fibronectin receptors on immature thymocytes. J Cell Biol 106:2183-90
Cheresh, D A; Pytela, R; Pierschbacher, M D et al. (1987) An Arg-Gly-Asp-directed receptor on the surface of human melanoma cells exists in an divalent cation-dependent functional complex with the disialoganglioside GD2. J Cell Biol 105:1163-73
Suzuki, S; Argraves, W S; Arai, H et al. (1987) Amino acid sequence of the vitronectin receptor alpha subunit and comparative expression of adhesion receptor mRNAs. J Biol Chem 262:14080-5
Pytela, R; Pierschbacher, M D; Argraves, S et al. (1987) Arginine-glycine-aspartic acid adhesion receptors. Methods Enzymol 144:475-89
Cardarelli, P M; Pierschbacher, M D (1987) Identification of fibronectin receptors on T lymphocytes. J Cell Biol 105:499-506
Suzuki, S; Argraves, W S; Pytela, R et al. (1986) cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors. Proc Natl Acad Sci U S A 83:8614-8
Cardarelli, P M; Pierschbacher, M D (1986) T-lymphocyte differentiation and the extracellular matrix: identification of a thymocyte subset that attaches specifically to fibronectin. Proc Natl Acad Sci U S A 83:2647-51
Argraves, W S; Pytela, R; Suzuki, S et al. (1986) cDNA sequences from the alpha subunit of the fibronectin receptor predict a transmembrane domain and a short cytoplasmic peptide. J Biol Chem 261:12922-4
Pytela, R; Pierschbacher, M D; Ginsberg, M H et al. (1986) Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors. Science 231:1559-62

Showing the most recent 10 out of 15 publications