A Three-dimensional Collagen Lattice Induces Protein Kinase C-ζ Activity: Role in α2 Integrin and Collagenase mRNA Expression

Xu, Jiahua; Clark, Richard A.F.

doi:10.1083/jcb.136.2.473

Cited by 95 publications

(82 citation statements)

References 70 publications

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“…However, it cannot be excluded that TPA-independent PKC isoforms, not inhibited by BIM at this concentration, are involved in the up-regulation of the MMPs in RCG. Xu and Clark (1997) have indeed shown that PKC-ζ is activated in RCG and participates in the up-regulation of the MMP-1. Other authors (Sudbeck et al, 1994;Vincenti et al, 1996) and ourselves (Lambert et al, 1998) have also demonstrated that TPA-induced expression of MMP-1 is inhibited by tyrosine kinase inhibitors, suggesting that PKC may act upstream of Src in the upregulation of the MMPs by phorbol esters and CD, and possibly also in RCG.…”

Section: Discussionmentioning

confidence: 99%

Distinct pathways in the over-expression of matrix metalloproteinases in human fibroblasts by relaxation of mechanical tension

et al. 2001

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The aim of the work was to analyze, on a comparative basis, the signaling pathways operating in the regulation of a panel of matrix metalloproteinases (MMP) expressed by human dermal fibroblasts submitted to mechanical stress relaxation by cytochalasin D (CD) and in a retracting collagen gel (RCG). The mRNA steady-state level of MMPs was measured by a quantitative RT-PCR procedure using a synthetic RNA as internal standard. In monolayer, most MMPs were barely detected, except MMP-2. Disruption of the actin stress fibers by CD induced a moderate increase of MMP-2 mRNA and a much larger stimulation of MMP-3, -9, -13 and -14 mRNAs. In RCG, a significant up-regulation of these MMPs was also observed although to a lower extent than in CD-treated monolayers. Among the investigated MMPs, the MMP-8 and -11 were not reproducibly detected. MMP-2 was processed to its active form both by CD and in RCG. The CD-induced up-regulation of gene expression was largely repressed by blocking protein synthesis by cycloheximide for all the MMPs, by inhibiting the tyrosine-kinases of the src family by herbimycin A for all MMPs, except MMP-2, and by inhibiting the TPAinducible PKC isoforms by bisindoyl maleimide for all MMPs, except MMP-14. The up-regulation induced by stress relaxation in RCG was protein synthesis-dependent for MMP-2 and MMP-13, tyrosine kinases-dependent for MMP-3 and MMP-13, as previously described for MMP-1. Inhibiting TPA-inducible PKC did not affect any MMP in RCG except MMP-13, which was strongly induced. The processing of MMP-2 was tyrosine kinasesdependent but PKC-independent. Inhibitors of the ERK1,2 and p38 MAP kinases pathways diversely affected the MMPs expression. Inhibiting the Rho-kinase activity by Y-27632 was inactive. These results point to the potent regulation operated by the status of the cytoskeleton on the cell phenotype, and to distinct regulatory pathways involved in the control of different MMPs expression.

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Section: Discussionmentioning

confidence: 99%

Distinct pathways in the over-expression of matrix metalloproteinases in human fibroblasts by relaxation of mechanical tension

et al. 2001

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“…Error bars show SE values. (Ivaska et al, 1999;Ravanti et al, 1999), the isoform of PKC (PKC ; Xu and Clark, 1997), and protein phosphatase 2A (PP2A; Ivaska et al, 2002a). Here, PKC␣ activity was needed for the internalization of ␣2␤1 integrin in caveolae.…”

Section: Discussionmentioning

confidence: 99%

Clustering Induces a Lateral Redistribution of α2β1 Integrin from Membrane Rafts to Caveolae and Subsequent Protein Kinase C-dependent Internalization

Upla

Marjomäki

Kankaanpää

et al. 2004

MBoC

151

186

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Integrin ␣2␤1 mediates the binding of several epithelial and mesenchymal cell types to collagen. The composition of the surrounding plasma membrane, especially caveolin-1-and cholesterol-containing membrane structures called caveolae, may be important to integrin signaling. On cell surface ␣2␤1 integrin was located in the raft like membrane domain, rich in GPI-anchored proteins, rather than in caveolae. However, when antibodies were used to generate clusters of ␣2␤1 integrin, they started to move laterally on cell surface along actin filaments. During the lateral movement small clusters fused together. Finally ␣2␤1 integrin was found inside caveolae and subsequently internalized into caveosome-like perinuclear structures. The internalization process, unlike cluster formation or lateral redistribution, was dependent on protein kinase C␣ activity. Caveolae are known to be highly immobile structures and ␣2␤1 integrin clusters represent a previously unknown mechanism to activate endocytic trafficking via caveolae. The process was specific to ␣2␤1 integrin, because the antibody-mediated formation of ␣V integrin clusters activated their internalization in coated vesicles and early endosomes. In addition to natural ligands human echovirus-1 (EV1) gains entry into the cell by binding to ␣2␤1 and taking advantage of ␣2␤1 internalization via caveolae. INTRODUCTIONCaveolae are cave-like invaginations of the cell surface (for reviews see Kurzchalia and Parton, 1999;Parton 2003). They have been described as highly immobile and not involved in constitutive endocytic trafficking (Thomsen et al., 2002). Their internalization can be activated, for example, by the phosphatase inhibitor okadaic acid (Parton et al., 1994). In endothelial cells the interaction of albumin docking protein gp60 and caveolin-1 initiates the endocytosis of caveolae (Minshall et al., 2000). Caveolins are membrane proteins that are molecular markers of caveolae and shown to be crucial for the formation of these structures (Fra et al., 1995). Caveolins can be associated with cell surface growth factor receptors (Couet et al., 1997) and cell adhesion receptors (Wary et al., 1996(Wary et al., , 1998Wei et al., 1999) and caveolae might therefore play a role in cellular signaling. In addition, caveolae have been suggested to participate in the uptake of folate by pinocytosis, but this is still under discussion (Parton, 2003). Caveolin-deficient mice have given novel insight into the function of caveolae. Caveolin-1 gene knockout leads to pulmonary defects, vasoconstriction, or dilatation abnormalities and resistance to diet-induced obesity (Drab et al., 2001;Razani et al., 2001;Schubert et al., 2001;Sotgia et al., 2002;Razani et al., 2002). Simian virus 40 (SV40) has been shown to be internalized through caveolae and detailed studies focused on the virus entry mechanism have produced a lot of new information about the biology of caveolae (Pelkmans et al., 2001. We have recently shown that human echovirus 1 (EV1) is another virus using caveolae in its entry (Mar...

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“…The atypical PKC isoform PKC has been particularly implicated in IKK-2 activation (30) and has been shown to be inhibited by calphostin C (40). Therefore, we focussed our attention on PKC as the candidate PKC isoform mediating these effects.…”

Section: Ras and Pkc Mediate The Activation Of Nf-b By Ha Fragmentsmentioning

confidence: 99%

Ras, Protein Kinase Cζ, and IκB Kinases 1 and 2 Are Downstream Effectors of CD44 During the Activation of NF-κB by Hyaluronic Acid Fragments in T-24 Carcinoma Cells

Fitzgerald

Bowie

Skeffington

et al. 2000

The Journal of Immunology

136

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We have investigated the ability of hyaluronic acid (HA) fragments to activate the transcription factor NF-κB. HA fragments activated NF-κB in the cell lines T-24, HeLa, MCF7, and J774. Further studies in T-24 cells demonstrated that HA fragments also induced IκBα phosphorylation and degradation, κB-linked reporter gene expression, and ICAM-1 promoter activity in an NF-κB-dependent manner. The effect of HA was size dependent as neither disaccharide nor native HA were active. CD44, the principal cellular receptor for HA, was critical for the response because the anti-CD44 Ab IM7.8.1 blocked the effect on NF-κB. HA fragments activated the IκB kinase complex, and the effect on a κB-linked reporter gene was blocked in T-24 cells expressing dominant negative IκB kinases 1 or 2. Activation of protein kinase C (PKC) was required because calphostin C inhibited NF-κB activation and IκBα phosphorylation. In particular, PKCζ was required because transfection of cells with dominant negative PKCζ blocked the effect of HA fragments on κB-linked gene expression and HA fragments increased PKCζ activity. Furthermore, damnacanthal and manumycin A, two mechanistically distinct inhibitors of Ras, blocked NF-κB activation. Transfection of T-24 cells with dominant negative Ras (RasN17) blocked HA fragment-induced κB-linked reporter gene expression, and HA fragments activated Ras activity within 5 min. Taken together, these studies establish a novel signal transduction cascade eminating from CD44 to Ras, PKCζ, and IκB kinase 1 and 2.

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A Three-dimensional Collagen Lattice Induces Protein Kinase C-ζ Activity: Role in α2 Integrin and Collagenase mRNA Expression

Cited by 95 publications

References 70 publications

Distinct pathways in the over-expression of matrix metalloproteinases in human fibroblasts by relaxation of mechanical tension

Distinct pathways in the over-expression of matrix metalloproteinases in human fibroblasts by relaxation of mechanical tension

Clustering Induces a Lateral Redistribution of α2β1 Integrin from Membrane Rafts to Caveolae and Subsequent Protein Kinase C-dependent Internalization

Ras, Protein Kinase Cζ, and IκB Kinases 1 and 2 Are Downstream Effectors of CD44 During the Activation of NF-κB by Hyaluronic Acid Fragments in T-24 Carcinoma Cells

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