Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previously we reported that, in vitro, lens cells proliferate, migrate or differentiate in response to low, medium and high concentrations of FGF respectively. To examine further the role of FGF in lens development we used immunohistochemistry to study the distribution of aFGF and bFGF in the eye of the 20 day rat foetus. Strong aFGF-like reactivity was localised in a band of cells near the lens equator which included the germinative zone where most cell proliferation occurs and the transitional zone where epithelial cells differentiate into fibres. The closely apposed inner epithelial layer of the ciliary and iridial retina also reacted strongly. Reactivity for aFGF was also found in the epidermis and in the corneal and conjunctival epithelia. In the neural retina, reactivity was found in the nerve fibre layer and in isolated cells of the inner plexiform layer. bFGF-like reactivity was found in the retinal ganglion cell layer, extra-ocular muscles and associated with endothelial cells of the hyaloid, lenticular and choroid vasculatures. Pre-digestion of sections with hyaluronidase caused loss of cell-associated reactivity but revealed strong bFGF-like reactivity in ocular basement membranes, in particular, the lens capsule. The sensitivity of this capsular bFGF localisation to heparinase indicates that bFGF in the extracellular matrix is complexed with heparan sulphate proteoglycans. The results of this study are consistent with the hypothesis that FGF plays an important role in lens development via both autocrine and paracrine mechanisms.
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PMID:Distribution of acidic and basic fibroblast growth factors (FGF) in the foetal rat eye: implications for lens development. 137 41

Basic fibroblast growth factor (FGF-2) can enhance biological potentials of periodontal ligament cells and its topical application induces considerable periodontal tissue regeneration in vivo. In this study, we examined the effect of FGF-2 on the production of hyaluronan (HA), an extracellular matrix playing important roles in homeostasis and inflammatory/wound healing responses, by human periodontal ligament (HPDL) cells. An inhibition binding-protein assay revealed that FGF-2 significantly increased HA production by HPDL cells in a dose dependent manner. Analysis by HPLC revealed that in conditioned medium of FGF-2-treated HPDL cells HA had a higher molecular mass, compared to that of untreated HPDL cells. RT-PCR analysis revealed the enhancement of mRNA expression of hyaluronan synthase (HAS) 1 and HAS 2, both of which contribute to the production of HA with a high molecular mass, but not HAS 3 in the FGF-2-treated HPDL cells. In contrast, three isoforms of hyaluronidase (HYAL) transcript were unchanged in the FGF-2-treated HPDL cells. These results provide new evidence for the possible involvement of FGF-2 in the regulation of HA production and its appreciable roles in not only homeostasis but also regeneration of periodontal tissues.
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PMID:Fibroblast growth factor-2 regulates the synthesis of hyaluronan by human periodontal ligament cells. 1557 76

Our earlier paper has reported that Wharton's jelly is a reservoir of several peptide growth factors, including acidic and basic fibroblast growth factors (aFGF and bFGF, respectively). Both can be extracted by buffered salts solutions in the form of high molecular mass complexes, probably with a component(s) of the extracellular matrix. Both aFGF and bFGF from such extracts hardly penetrate 10% polyacrylamide gels during electrophoresis. Pre-treatment of Wharton's jelly with hyaluronidase slightly increased the extractability of aFGF, but did not affect the extractability of bFGF. In contrast, the pre-treatment of tissue homogenate with bacterial collagenase (2000 U/ml, 37 degrees C, 18 h) increased the extractability of bFGF. The presence of beta-mercaptoethanol in the extracting solutions increased the extractability of both FGFs, but did not release FGFs in their free form, despite reducing the molecular mass of the FGF-containing complexes. We conclude that both aFGF and bFGF are bound through disulphide bonds to a protein component of Wharton's jelly. We propose that ground substance composed mainly of collagen fibrils and hyaluronate molecules, which surrounds the cells of Wharton's jelly, prevents the access of the extracting solution to aFGF and bFGF. Although hyaluronate and collagen do not bind aFGF or bFGF directly, they may constitute a barrier which prevents the dispersion of FGFs in Wharton's jelly. Thus, the high concentration of FGFs around the cells of Wharton's jelly may facilitate the interaction of these factors with membrane receptors, thereby resulting in stimulation of cell division and differentiation, as well as of the synthesis of extracellular matrix components.
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PMID:FGF binding by extracellular matrix components of Wharton's jelly. 1756 91