K-glypican: a novel GPI-anchored heparan sulfate proteoglycan that is highly expressed in developing brain and kidney

نویسندگان

  • K Watanabe
  • H Yamada
  • Y Yamaguchi
چکیده

Glypicans are a family of glycosylphosphatidylinositol (GPI)-anchored cell surface heparan sulfate proteoglycans (HSPGs). The glypican family, which currently includes glypican, the developmentally regulated rat intestinal transcript OCI-5, and cerebroglycan, is characterized by a similar core protein size and almost complete conservation of cysteine residues. By RT-PCR using degenerate oligonucleotide primers based on the sequence homologies, we isolated mouse cDNA encoding a novel member of the glypican family as well as mouse homologues of glypican and OCI-5. The novel molecule, named K-glypican, has a predicted molecular mass of 57.5 kD and potential attachment sites for heparan sulfate chains and a GPI anchor in its COOH-terminal region, like other members of the glypican family. Transfection of an epitope-tagged full-length K-glypican cDNA into MDCK cells demonstrated that K-glypican is indeed expressed as a GPI-anchored HSPG. Northern blot analyses with K-glypican, glypican, and OCI-5 probes demonstrated that kidney and developing brain, and that these three molecules show remarkable patterns of cell type- and developmental stage-specific expression. In situ hybridization revealed that the major sites of K-glypican expression in developing embryo are tubular epithelial cells in the kidney and proliferating neuroepithelial cells in the brain. These results indicate that K-glypican is a novel GPI-anchored HSPG involved in embryonic development.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Glypican-4 is an FGF2-binding heparan sulfate proteoglycan expressed in neural precursor cells.

FGF2 is a crucial mitogen for neural precursor cells in the developing cerebral cortex. Heparan sulfate proteoglycans (HSPGs) are thought to play a role in cortical neurogenesis by regulating the action of FGF2 on neural precursor cells. In this article, we present data indicating that glypican-4 (K-glypican), a GPI-anchored cell surface HSPG, is involved in these processes. In the developing m...

متن کامل

Heparan sulfate expression in polarized epithelial cells: the apical sorting of glypican (GPI-anchored proteoglycan) is inversely related to its heparan sulfate content

Several processes that occur in the luminal compartments of the tissues are modulated by heparin-like polysaccharides. To identify proteins responsible for the expression of heparan sulfate at the apex of polarized cells, we investigated the polarity of the expression of the cell surface heparan sulfate proteoglycans in CaCo-2 cells. Domain-specific biotinylation of the apical and basolateral m...

متن کامل

Cerebroglycan: an integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation

Heparan sulfate proteoglycans (HSPGs) are found on the surface of all adherent cells and participate in the binding of growth factors, extracellular matrix glycoproteins, cell adhesion molecules, and proteases and antiproteases. We report here the cloning and pattern of expression of cerebroglycan, a glycosylphosphatidylinositol (GPI)-anchored HSPG that is found in the developing rat brain (pre...

متن کامل

Mammalian Notum induces the release of glypicans and other GPI-anchored proteins from the cell surface.

Glypicans are heparan sulfate proteoglycans that are attached to the cell surface by a GPI (glycosylphosphatidylinositol)anchor. Glypicans regulate the activity of Wnts, Hedgehogs,bone morphogenetic proteins and fibroblast growth factors. In the particular case of Wnts, it has been proposed that GPI-anchored glypicans stimulate Wnt signalling by facilitating and/or stabilizing the interaction b...

متن کامل

Glypican-1 Mediates Both Prion Protein Lipid Raft Association and Disease Isoform Formation

In prion diseases, the cellular form of the prion protein, PrP(C), undergoes a conformational conversion to the infectious isoform, PrP(Sc). PrP(C) associates with lipid rafts through its glycosyl-phosphatidylinositol (GPI) anchor and a region in its N-terminal domain which also binds to heparan sulfate proteoglycans (HSPGs). We show that heparin displaces PrP(C) from rafts and promotes its end...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • The Journal of Cell Biology

دوره 130  شماره 

صفحات  -

تاریخ انتشار 1995