The lymphocyte adhesion molecule CD44 recognizes a non-hyaluronate proteoglycan, gp600, secreted by mouse T cell line CTLL2. We now demonstrate that gp600 is identical to serglycin, a member of the small proteoglycan family stored in intracellular secretory granules of lymphoid, myeloid, and some tumor cells. Purified gp600 has the ability to bind specifically to CD44, and the binding is dependent on activation of CD44. The CD44-binding elements on gp600 or serglycin are glycosaminoglycans consisting of chondroitin 4-sulfate. Serglycin is readily exocytosed, and its interaction with active form CD44 augments the CD3-dependent degranulation of CD44 positive CTL clones. We conclude that the serglycin secreted from secretory granules of hematopoietic cells is a novel ligand for CD44, and could regulate lymphoid cell adherence and activation.
A Novel Ligand for CD44 Is Serglycin, a Hematopoietic Cell Lineage-specific Proteoglycan
N. Toyama-Sorimachi,H. Sorimachi,Yoshimi Tobita,F. Kitamura,H. Yagita,Koichi Suzuki,M. Miyasaka
Published 1995 in Journal of Biological Chemistry
ABSTRACT
PUBLICATION RECORD
- Publication year
1995
- Venue
Journal of Biological Chemistry
- Publication date
1995-03-31
- Fields of study
Biology, Medicine
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-49 of 49 references · Page 1 of 1