Abstract

The mechanisms underlying the role of extracellular materials and cell surface components in the development of organ form during development will be investigated by (1) using an abundant source to isolate, purify and molecularly characterize the previously described neutral hyaluronidase, (2) determining whether the neutral hyaluronidase is an extracellular enzyme, (3) establishing the generality of the correlation between neutral hyaluronidase activity and morphogenetic events, and (4) investigating potential inhibitors of the neutral hyaluronidase in an attempt to define its function during development.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Research Project (R01)
Project #
5R01HD006763-14
Application #
3310582
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1976-05-01
Project End
1987-11-30
Budget Start
1985-07-01
Budget End
1987-11-30
Support Year
14
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Stanford University
Department
Type
Schools of Medicine
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305

  Publications

Reizes, Ofer; Goldberger, Olga; Smith, April C et al. (2006) Insulin promotes shedding of syndecan ectodomains from 3T3-L1 adipocytes: a proposed mechanism for stabilization of extracellular lipoprotein lipase. Biochemistry 45:5703-11
Ueno, M; Yamada, S; Zako, M et al. (2001) Structural characterization of heparan sulfate and chondroitin sulfate of syndecan-1 purified from normal murine mammary gland epithelial cells. Common phosphorylation of xylose and differential sulfation of galactose in the protein linkage region tetrasa J Biol Chem 276:29134-40
Reizes, O; Lincecum, J; Wang, Z et al. (2001) Transgenic expression of syndecan-1 uncovers a physiological control of feeding behavior by syndecan-3. Cell 106:105-16
Park, P W; Reizes, O; Bernfield, M (2000) Cell surface heparan sulfate proteoglycans: selective regulators of ligand-receptor encounters. J Biol Chem 275:29923-6
Sun, D; Mcalmon, K R; Davies, J A et al. (1998) Simultaneous loss of expression of syndecan-1 and E-cadherin in the embryonic palate during epithelial-mesenchymal transformation. Int J Dev Biol 42:733-6
Kato, M; Wang, H; Kainulainen, V et al. (1998) Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2. Nat Med 4:691-7
Cook, D M; Hinkes, M T; Bernfield, M et al. (1996) Transcriptional activation of the syndecan-1 promoter by the Wilms' tumor protein WT1. Oncogene 13:1789-99
Spring, J; Goldberger, O A; Jenkins, N A et al. (1994) Mapping of the syndecan genes in the mouse: linkage with members of the myc gene family. Genomics 21:597-601
Kokenyesi, R; Bernfield, M (1994) Core protein structure and sequence determine the site and presence of heparan sulfate and chondroitin sulfate on syndecan-1. J Biol Chem 269:12304-9
Spring, J; Paine-Saunders, S E; Hynes, R O et al. (1994) Drosophila syndecan: conservation of a cell-surface heparan sulfate proteoglycan. Proc Natl Acad Sci U S A 91:3334-8

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