Association of increased intracellular free Ca2+ by platelet-derived growth factor with mitogenesis but not with proteoglycan synthesis in chondrocytes — Effect of suramin

Fukuo, Keisuke; Morimoto, Shigeto; Kaji, Koichi; Koh, Eio; Hatori, Takashi; Morita, Ryosuke; Kim, S.; Onishi, Toshio

doi:10.1016/0143-4160(89)90041-9

Cited by 21 publications

(13 citation statements)

References 16 publications

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“…It should be noted that we were not able to see a rapid, transient increase in intracellular free Ca2+ upon addition of RA to dye-loaded cells in the cuvette. This is in contrast to what has been observed with other mitogens in a number of different systems [20][21][22][23][24][25][26][27], Taken together, these data suggest that RA acts by some indirect method to bring about a lowering of Ca2+ levels in keratinocytes concomitant with its stimulation of cell growth. Since Ca2+ is a critical regulator of growth and differentiation in keratinocytes.…”

Section: Discussioncontrasting

confidence: 55%

“…Raising the Ca2+ concentration above this level triggers DNA replication and cell division [17][18][19], In many cells, factors that stim ulate proliferation cause a rapid, transient increase in intracellular free Ca2+. brought about by a release of Ca2+ from internal stores and influx of Ca2+ from the extracel lular environment [20][21][22][23][24][25][26][27], Human epidermal keratino cytes are different from fibroblasts in that they proliferate optimally when the extracellular Ca2+ concentration is below 1.0 mM. When the extracellular Ca2+ concentration is raised, proliferation decreases (though does not com pletely stop) and differentiation is induced [11][12][13], In creasing the extracellular Ca2+ concentration is known to increase intracellular Ca2+ levels [28. and this report] and recently Wilson and Tang [29] and Pillai and Bikle [28] both showed that factors such as vitamin Dj, which are pro-differentiation in keratinocytes.…”

Section: Discussionmentioning

confidence: 99%

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Modulation of Ca2+ Levels in Keratinocytes by All-Trans Retinoic Acid

Varani¹,

Inman

Gibbs³

et al. 1992

Pathobiology

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Human epidermal keratinocytes, that have been growth-arrested by removal of epidermal growth factor from the culture medium, are stimulated to proliferate by all-trans retinoic acid (RA). The same treatment inhibits the onset of differentiated features and reduces cell-substrate adhesion. In the present study we show that the same treatment results in a decrease in total cell-associated Ca²⁺ as measured by changes in the amount of ⁴⁵Ca²⁺ bound to cells at equilibrium following RA treatment and by a decrease in intracellular free Ca²⁺ levels as measured with the Ca²⁺-sensitive dye, Indo-1. The alterations in Ca²⁺ levels were evident within an hour after RA treatment, were in the range of 30-35% and occurred over the same RA concentration range that stimulated proliferation (i.e., 0.25-1.0 µg/ml). When the extracellular Ca²⁺ concentration was elevated from the normal level of 0.15-1.4 mM, intracellular free Ca²⁺ increased by a factor of 2 while total cell-associated Ca²⁺ increased approximately 6-fold. Even under conditions of high extracellular Ca²⁺, RA was able to reduce cell-associated and intracellular free Ca²⁺. These data indicate that RA has the capacity to lower Ca²⁺ levels in keratinocytes concomitantly with its effects on biological behavior.

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Section: Discussioncontrasting

confidence: 55%

Section: Discussionmentioning

confidence: 99%

Modulation of Ca2+ Levels in Keratinocytes by All-Trans Retinoic Acid

Varani¹,

Inman

Gibbs³

et al. 1992

Pathobiology

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“…The number of disc cells is greater in disc hemiations than in normal discs (unpublished data). This could suggest that PDGF also regulates the function of disc cells and that in DHT PDGF stimulates extracellular matrix component production as has been observed for cartilage tissue [9,23,24]. PDGF may also be stimulative for disc cell proliferation.…”

Section: Discussionmentioning

confidence: 68%

“…In cartilage it has been demonstrated to increase the level of intracellular free calcium ions in chondrocytes [9]. Furthermore, it stimulates DNA and proteoglycan synthesis in cartilage tissue [9] and chondrocyte proliferation [13].…”

Section: Introductionmentioning

confidence: 99%

Platelet-derived growth factor and vascular endothelial growth factor expression in disc herniation tissue: an immunohistochemical study

et al. 1997

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“…The filters were washed four times with 1 ml ice-cold buffer, placed in counting tubes, and 1 ml 1% Triton X-100 in 10% aqueous glycerol was added. In some of the experiments the cells were pretreated (30 min, 4°C) with 70 or 350 qM suramin to displace any bound PDGF [14,15] prior to the addition of the radiolabeled PDGF. The suramin was removed by washing the cells once.…”

Section: Epo and Edn Releasementioning

confidence: 99%

Activation of Human Eosinophils by Platelet-Derived Growth Factor

Bach

Brashler²,

Stout³

et al. 1992

Int Arch Allergy Immunol

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Activated eosinophils are believed to be major contributors to the chronic inflammatory sequelae of asthma, but the details of the mechanism of eosinophil activation in vivo are unknown. In our search for physiologically important modes of eosinophil activation, we studied the effects of recombinant human platelet-derived growth factor (PDGF) on human peripheral blood eosinophils. We compared two activation end-points: secretion of granule contents, exemplified by the release of eosinophil peroxidase (EPO), and eosinophil-derived neurotoxin (EDN), and the generation of active oxygen metabolites (O₂^–– production). PDGF_c-sis dose dependently stimulated the secretion of large amounts of EPO and EDN from eosinophils. Higher concentrations of PDGF induced a dose-dependent O₂^–– production, especially if the cells were first primed with low concentrations of phorbol ester. These activities were not seen with the AA homodimer of PDGF, suggesting that the activation was receptor dependent. However, several attempts to directly demonstrate the existence of such receptors were unsuccessful. The magnitude of the secretory response to PDGF, and the realization that eosinophils could be easily exposed to this substance as they travel towards the lung, suggests the possibility that this growth factor may be a physiologically important activator of eosinophils in the pulmonary inflammation which is associated with asthma.

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Association of increased intracellular free Ca2+ by platelet-derived growth factor with mitogenesis but not with proteoglycan synthesis in chondrocytes — Effect of suramin

Cited by 21 publications

References 16 publications

Modulation of Ca2+ Levels in Keratinocytes by All-Trans Retinoic Acid

Modulation of Ca2+ Levels in Keratinocytes by All-Trans Retinoic Acid

Platelet-derived growth factor and vascular endothelial growth factor expression in disc herniation tissue: an immunohistochemical study

Activation of Human Eosinophils by Platelet-Derived Growth Factor

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