Receptors for fibroblast growth factors

  title={Receptors for fibroblast growth factors},
  author={J. C. Coutts and John T. Gallagher},
  journal={Immunology and Cell Biology},
The recent discovery of the involvement of heparan sulfate proteoglycans (HSPG) in the activation of fibroblast growth factor receptors (FGFR) has led to an intensification of study of this field. It appears that the HSPG act as low affinity receptors to which the fibroblast growth factors (FGF) must bind in order to successfully activate the high affinity FGFR. Heparan sulfate chains consisting of alternately arranged N‐acetylated or N‐sulfated glucosamine and uronic acid disaccharide regions… 

Heparan sulfate: growth control with a restricted sequence menu.

  • J. Gallagher
  • Biology
    The Journal of clinical investigation
  • 2001
It is argued that HS polysaccharides display a versatility in conformation and orientation of functional groups that permits them to employ different modes of binding with any individual protein or protein complex, which could offset the need for the controlled synthesis of a vast repertoire of defined sequences for exclusive binding of individual proteins.

Localization of fibroblast growth factor 2 (FGF-2) protein and the receptors FGFR 1–4 in normal human seminiferous epithelium

The distribution pattern suggests that FGF-2 in spermatogonia is involved in the autocrine and paracrine regulation of the proliferation and differentiation of sperMatogonia and sper matocytes via the receptors FGFR-1,FGFR-3 and FG FR-4.

Localization of fibroblast growth factor-2 (basic FGF) and FGF receptor-1 in adult human kidney.

Potential autocrine and paracrine pathways within the FGF-2 system, particularly within the vascular walls and in the distal nephron, are suggested, to provide information for further mechanistic understanding of the role of the F GF2 system in human renal disease.

Expression of Syndecan-2, -4, and Fibroblast Growth Factor Receptor Type 1 in Human Periodontal Ligament Fibroblasts and Down-regulation of These Membrane Proteins during Maturation in Culture

Observations indicate that PDL cells express syndecan-2, -4, and FGFR1 mRNAs, and that those levels are changed with the increase in ALPase activity in culture, which may be involved in the control of growth and differentiation ofPDL cells during development and regeneration.

Fibroblast Growth Factors and Their Receptors in Parathyroid Disease

It is suggested that parathyroid tissue is potentially responsive to FGFs, and the presence of elevated levels of FGF3 expression in abnormal par Kathyroid tissue may be significant, as the F GF3 gene (int-2 proto-oncogene) is located on chromosome 11q13.3, a region already identified as being susceptible to rearrangement/mutation in parathyoid disease.

Heparan sulfate proteoglycans: A GAGgle of skeletal‐hematopoietic regulators

This review summarizes the current understanding of the presence and function of heparan sulfate proteoglycans in skeletal development and hematopoiesis and discusses how HSPGs play predominant roles in establishing and regulating niches during skeleto‐hematopoietic development by participating in distinct developmental processes such as patterning, compartmentalization, growth, differentiation, and maintenance of tissues.

Heparan sulfate of perlecan is involved in glomerular filtration.

Findings suggest that heparan sulfate chains of perlecan play an important role in glomerular filtration, especially of a large amount of protein.



Heparan sulphates as membrane receptors for the fibroblast growth factors.

  • J. Gallagher
  • Biology, Computer Science
    European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies
  • 1994
The vital importance of heparan sulphate in controlling growth factor activities has opened up a new chapter in proteoglycan research and has brought proteoglycans into the mainstream of cell biology and may suggest novel methods of controlling diseases such as cancer, atherosclerosis or fibrosis.

Isolation of an additional member of the fibroblast growth factor receptor family, FGFR-3.

The existence of an additional member of the FGFR family that is highly homologous to the previously described FGFR-3 is established by showing that human acidic and basic fibroblast growth factors activate this receptor as measured by 45Ca2+ efflux assays.

Fibroblast growth factor receptors have different signaling and mitogenic potentials

Compared the properties of BaF3 murine lymphoid cells and L6 rat myoblast cells engineered to express FGFR-1 orFGFR-4 are compared, finding that the signaling and biological responses elicited by different FGF receptors substantially differ.

The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain.

The arrangement of exons and introns in the human FGF receptor 1 (FGFR 1) gene has been mapped and three alternative exons encoding a portion of the third immunoglobulin (Ig)-like domain of the receptor are found.

An essential heparin-binding domain in the fibroblast growth factor receptor kinase.

The results indicate that the FGF receptor is a ternary complex of heparan sulfate proteoglycan, tyrosine kinase transmembrane glycoprotein, and ligand.

Fibroblast growth factor receptors display both common and distinct signaling pathways.

The results suggest that the signaling mechanism of FGFR4 differs from that ofFGFR1 and KGFR, and that the primary role of FG FR4 in myoblasts may be the maintenance of their non differentiated state.

A confined variable region confers ligand specificity on fibroblast growth factor receptors: implications for the origin of the immunoglobulin fold.

The C‐terminal half of the third immunoglobulin‐like domain of FGF receptors is identified as a major determinant for ligand binding and present a novel genetic mechanism for altering receptor‐ligand specificity and generating receptor diversity.