Immunocytochemical distribution of extracellular matrix receptors in human osteoclasts: A β3 integrin is colocalized with vinculin and talin in the podosomes of osteoclastoma giant cells

Zambonin-Zallone, A; Teti, Anna; Grano, Maria; Rubinacci, Alessandro; Abbadini, Marzia; Gáboli, Mirella; Marchisio, Pier Carlo

doi:10.1016/0014-4827(89)90266-8

Cited by 195 publications

(98 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Integrins are usually observed in invadosomes in normal cells. For example, the integrin αvβ3 had been detected in the ring surrounding the invadosome cores in osteoclasts (Pfaff and Jurdic, 2001;Zambonin-Zallone et al, 1989). Moreover, ablation of β1, β2 and β3 integrins was necessary to inhibit invadosome formation in osteoclasts (Schmidt et al, 2011).…”

Section: Integrinsmentioning

confidence: 99%

The microenvironment controls invadosome plasticity

Martino

Henriet

Ezzoukhry

et al. 2016

Journal of Cell Science

View full text Add to dashboard Cite

Invadosomes are actin-based structures involved in extracellular matrix degradation. Invadosomes is a term that includes podosomes and invadopodia, which decorate normal and tumour cells, respectively. They are mainly organised into dots or rosettes, and podosomes and invadopodia are often compared and contrasted. Various internal or external stimuli have been shown to induce their formation and/or activity. In this Commentary, we address the impact of the microenvironment and the role of matrix receptors on the formation, and dynamic and degradative activities of invadosomes. In particular, we highlight recent findings regarding the role of type I collagen fibrils in inducing the formation of a new linear organisation of invadosomes. We will also discuss invadosome plasticity more generally and emphasise its physio-pathological relevance.

show abstract

Section: Integrinsmentioning

confidence: 99%

The microenvironment controls invadosome plasticity

Martino

Henriet

Ezzoukhry

et al. 2016

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…Culture conditions were the same as described above. Since podosome formation is observed in osteoclasts attached to glass similar to bone laminae ( 12), these experiments were taken as resembling the effects seen in cells attached to bone. Additionally, in subsequent experiments on polished bone surfaces a similar appearance of podosome formation was observed and regulated by retinol ( 12).…”

Section: Osteoclast Preparationmentioning

confidence: 99%

Extracellular protons acidify osteoclasts, reduce cytosolic calcium, and promote expression of cell-matrix attachment structures.

Teti¹,

Blair²,

Schlesinger³

et al. 1989

J. Clin. Invest.

139

View full text Add to dashboard Cite

Because metabolic acids stimulate bone resorption in vitro and in vivo, we focused on the cellular events produced by acidosis that might be associated with stimulation of bone remodeling. To this end, we exposed isolated chicken osteoclasts to a metabolic (butyric) acid and observed a fall in both intracellular pH and cytosolic calcium (ICa2j1i). These phenomena were recapitulated when bone resorptive cells, alkalinized by HCO3 loading, were transferred to a bicarbonate-free environment.The acid-induced decline in osteoclast ICa2"1i was blocked by either NaCN or Na3VO4, in a Na+-independent fashion, despite the failure of each inhibitor to alter stimulated intracellular acidification. Moreover, K+-induced membrane depolarization also reduced cytosolic calcium in a manner additive to the effect of protons. These findings suggest that osteoclasts adherent to bone lack functional voltage-operated Ca2" channels, and they reduce [Ca2"ii in response to protons via a membrane residing Ca-ATPase. Most importantly, acidosis enhances formation of podosomes, the contact areas of the osteoclast clear zone, indicating increased adhesion to substrate, an early step in bone resorption. Thus, extracellular acidification of osteoclasts leads to decrements in intracellular pH and calcium, and appears to promote cell-matrix attachment.

show abstract

“…Podosome cores are surrounded by a ring structure of adhesion plaque proteins such as talin or vinculin (Tarone et al, 1985;Zambonin-Zallone et al, 1989). Podosomes are highly dynamic structures with a lifetime of 2-12 minutes (Destaing et al, 2005), which suggests tight control of the turnover of both internal components and the podosome structure itself.…”

Section: Introductionmentioning

confidence: 99%

Supervillin couples myosin-dependent contractility to podosomes and enables their turnover

Bhuwania

Cornfine

Fang

et al. 2012

Journal of Cell Science

100

135

View full text Add to dashboard Cite

SummaryPodosomes are actin-rich adhesion and invasion structures. Especially in macrophages, podosomes exist in two subpopulations, large precursors at the cell periphery and smaller podosomes (successors) in the cell interior. To date, the mechanisms that differentially regulate these subpopulations are largely unknown. Here, we show that the membrane-associated protein supervillin localizes preferentially to successor podosomes and becomes enriched at precursors immediately before their dissolution. Consistently, podosome numbers are inversely correlated with supervillin protein levels. Using deletion constructs, we find that the myosin II regulatory Nterminus of supervillin ] is crucial for these effects. Phosphorylated myosin light chain (pMLC) localizes at supervillinpositive podosomes, and time-lapse analyses show that enrichment of GFP-supervillin at podosomes coincides with their coupling to contractile myosin-IIA-positive cables. We also show that supervillin binds only to activated myosin IIA, and a dysregulated N-terminal construct [SV(1-830)] enhances pMLC levels at podosomes. Thus, preferential recruitment of supervillin to podosome subpopulations might both require and induce actomyosin contractility. Using siRNA and pharmacological inhibition, we demonstrate that supervillin and myosin IIA cooperate to regulate podosome lifetime, podosomal matrix degradation and cell polarization. In sum, we show here that podosome subpopulations differ in their molecular composition and identify supervillin, in cooperation with myosin IIA, as a crucial factor in the regulation of podosome turnover and function.

show abstract

Immunocytochemical distribution of extracellular matrix receptors in human osteoclasts: A β3 integrin is colocalized with vinculin and talin in the podosomes of osteoclastoma giant cells

Cited by 195 publications

References 34 publications

The microenvironment controls invadosome plasticity

The microenvironment controls invadosome plasticity

Extracellular protons acidify osteoclasts, reduce cytosolic calcium, and promote expression of cell-matrix attachment structures.

Supervillin couples myosin-dependent contractility to podosomes and enables their turnover

Contact Info

Product

Resources

About