Assignment of the human glypican gene (GPC1) to 2q35-q37 by fluorescence in situ hybridization
- Univ. of Leuven (Belgium); and others
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Two different cell surface heparan sulfate proteoglycan families can be distinguished: the syndecan-like integral membrane proteoglycans (SLIPS), with a core protein spanning the cytoplasmic membrane; and the glypican-related integral membrane proteoglycans (GRIPS), with a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol. The functions of these cell surface proteoglycans remain elusive, but because of their interactions with specific proteins, they are believed to be implicated in cell adhesion, cell growth, and control of proteolytic and lipolytic pathways. Glypican is the only human glypiated heparan sulfate proteoglycan that has so far been identified by cloning. Due to its highly conserved sequence, it has been speculated that this protein may support an essential function. Glypican is differentially expressed in different cell types and tissues. It is abundant in the adult rat brain, where it occurs in subpopulations of projection neurons. At this site, it may stabilize and activate neurotrophic polypeptide growth factors and mediate neuronal adhesion mechanisms that are essential for neuronal survival and injury responses. To learn more about glypican and to study its possible association with hereditary neuronal disorders, we have identified its chromosomal location. 6 refs., 1 fig.
- OSTI ID:
- 241105
- Journal Information:
- Genomics, Vol. 25, Issue 1; Other Information: PBD: 1 Jan 1995
- Country of Publication:
- United States
- Language:
- English
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