Carbohydrate recognition in the peripheral nervous system: a calcium- dependent membrane binding site for HNK-1 reactive glycolipids potentially involved in Schwann cell adhesion

doi:10.1083/jcb.121.2.397

This Article

Full Text (PDF, 1723K)

Alert me when this article is cited

Citation Map

Services

Email this article

Similar articles in this journal

Similar articles in PubMed

Alert me to new content in the JCB

Download to citation manager

Citing Articles

Citing Articles via HighWire

Citing Articles via CrossRef

Citing Articles via Google Scholar

Google Scholar

Articles by Needham, L. K.

Articles by Schnaar, R. L.

Search for Related Content

PubMed

PubMed Citation

Articles by Needham, L. K.

Articles by Schnaar, R. L.

Pubmed/NCBI databases

Hazardous Substances DB
Compound via MeSH
Substance via MeSH
CALCIUM COMPOUNDS
CALCIUM, ELEMENTAL

Social Bookmarking

What's this?

ARTICLES

Carbohydrate recognition in the peripheral nervous system: a calcium- dependent membrane binding site for HNK-1 reactive glycolipids potentially involved in Schwann cell adhesion

LK Needham and RL Schnaar
Department of Pharmacology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.

The carbohydrate determinants recognized by the HNK-1 antibody are potential cell-cell recognition ligands in the peripheral nervous system (PNS). The HNK-1 reactive sulfoglucuronylneolacto (SGNL) glycolipids specifically support Schwann cell adhesion, suggesting the presence of a cell surface receptor specific for SGNL-oligosaccharides. We directly probed PNS membranes for receptors complementary to SGNL determinants using a synthetic radioligand consisting of radioiodinated serum albumin derivatized with multiple SGNL-oligosaccharides. A high- affinity, saturable, calcium-dependent binding site for this ligand was found in PNS myelin membranes. Binding activity was carbohydrate- specific (most potently inhibited by SGNL-lipids compared to other glycolipids) and PNS-specific (absent from comparable central nervous system membranes). The SGNL-specific binding activity on PNS membranes reported here may be involved in peripheral myelination or myelin stabilization.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Bouyain, S., Rushton, S., Drickamer, K. (2001). Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain. Glycobiology 11: 989-996 [Abstract] [Full Text]
Miura, R., Aspberg, A., Ethell, I. M., Hagihara, K., Schnaar, R. L., Ruoslahti, E., Yamaguchi, Y. (1999). The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion. J. Biol. Chem. 274: 11431-11438 [Abstract] [Full Text]
Yuen, C.-T., Chai, W., Loveless, R. W., Lawson, A. M., Margolis, R. U., Feizi, T. (1997). Brain Contains HNK-1 Immunoreactive O-Glycans of the Sulfoglucuronyl Lactosamine Series that Terminate in 2-Linked or 2,6-Linked Hexose (Mannose). J. Biol. Chem. 272: 8924-8931 [Abstract] [Full Text]
Voshol, H., van Zuylen, C. W.E.M., Orberger, G., Vliegenthart, J. F.G., Schachner, M. (1996). Structure of the HNK-1 Carbohydrate Epitope on Bovine Peripheral Myelin Glycoprotein P0. J. Biol. Chem. 271: 22957-22960 [Abstract] [Full Text]
Tiemeyer, M, Goodman, C. (1996). Gliolectin is a novel carbohydrate-binding protein expressed by a subset of glia in the embryonic Drosophila nervous system. Development 122: 925-936 [Abstract]
Hattori, M.-a., Horiuchi, R., Hosaka, K., Hayashi, H., Kojima, I. (1995). Sialyllactose-mediated Cell Interaction during Granulosa Cell Differentiation. J. Biol. Chem. 270: 7858-7863 [Abstract] [Full Text]