Degradation of protein kinase Cα and its free catalytic subunit, protein kinase M, in intact human neuroblastoma cells and under cell‐free conditions

Shea, Thomas B.; Beermann, Mary Lou; Griffin, W. R.; Leli, Ubaldo

doi:10.1016/0014-5793(94)00769-1

Cited by 47 publications

(27 citation statements)

References 30 publications

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“…However, the results gained from a number of experiments failed to reveal a particular combination of treatments whereby a catalytic fragment of Apl I or Apl II could be reliably detected by Western blotting under our conditions. Several other studies have likewise reported that endogenous generation of PKM is very difficult to detect (Shea et al, 1994), and a failure to observe PKM by immunoblotting is not uncommon (Grünbaum Figure 5. Calphostin C, a PKC inhibitor interacting with the regulatory domain, blocks the induction but not the maintenance of site-specific ITM.…”

Section: Aplysia Pkc Isoforms Are Proteolyzed By Calpainmentioning

confidence: 96%

Intermediate-Term Memory for Site-Specific Sensitization inAplysiaIs Maintained by Persistent Activation of Protein Kinase C

et al. 2004

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Recent studies of long-term synaptic plasticity and long-term memory have demonstrated that the same functional endpoint, such as long-term potentiation, can be induced through distinct signaling pathways engaged by different patterns of stimulation. A critical question raised by these studies is whether different induction pathways either converge onto a common molecular mechanism or engage different molecular cascades for the maintenance of long-term plasticity. We directly examined this issue in the context of memory for sensitization in the marine mollusk Aplysia. In this system, training with a single tail shock normally induces short-term memory (Ͻ30 min) for sensitization of tail-elicited siphon withdrawal, whereas repeated spaced shocks induce both intermediate-term memory (ITM) (Ͼ90 min) and long-term memory (Ͼ24 hr). We now show that a single tail shock can also induce ITM that is expressed selectively at the trained site (site-specific ITM). Although phenotypically similar to the form of ITM induced by repeated trials, the mechanisms by which site-specific ITM is induced and maintained are distinct. Unlike repeated-trial ITM, site-specific ITM requires neither protein synthesis nor PKA activity for induction or maintenance. Rather, the induction of site-specific ITM requires calpain-dependent proteolysis of activated PKC, yielding a persistently active PKC catalytic fragment (PKM) that also serves to maintain the memory in the intermediateterm temporal domain. Thus, two unique forms of ITM that have different induction requirements also use distinct molecular mechanisms for their maintenance.

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Section: Aplysia Pkc Isoforms Are Proteolyzed By Calpainmentioning

confidence: 96%

Intermediate-Term Memory for Site-Specific Sensitization inAplysiaIs Maintained by Persistent Activation of Protein Kinase C

et al. 2004

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“…PKC activity is also determined by its degradation. The literature indicates that the calcium-lipid-dependent protease calpain-can degrade PKC to a catalytically active PKM by cleaving off the regulatory domain (43,46,154,161). PKM may be a constitutively active enzyme that mediates long-term phosphorylation activity of PKC.…”

Section: The Basics Of Pkcmentioning

confidence: 99%

Protein kinase C modulates pulmonary endothelial permeability: a paradigm for acute lung injury

Siflinger-Birnboim

Johnson

2003

American Journal of Physiology-Lung Cellular and Molecular Phys

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The intracellular serine/threonine kinase protein kinase C (PKC) has an important role in the genesis of pulmonary edema. This review discusses the PKC-mediated mechanisms that participate in the pulmonary endothelial response to agents involved in lung injury characteristic of the respiratory distress syndrome. Thus the paradigms of PKC-induced lung injury are discussed within the context of pulmonary transvascular fluid exchange. We focus on the signal transduction pathways that are modulated by PKC and their effect on lung endothelial permeability. Specifically, α-thrombin, tumor necrosis factor (TNF)-α, and reactive oxygen species are discussed because of their well-established roles in both human and experimental lung injury. We conclude that PKC, most likely PKC-α, is a primary supporter for lung endothelial injury in response to α-thrombin, TNF-α, and reactive oxygen species.

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“…41 ± 43 Calpain cleaves activated PKC at the hinge region between the regulatory and catalytic domain and cleaved PKC is subsequently rapidly degraded by other cellular proteases. 44 This process, known as`downregulation' functions to attenuate the PKC signal, thus preventing the persistent accumulation of activated kinases. Our data indicates that activation of PKC with low doses of TPA results in a modest induction of apoptosis as indicated by DNA fragmentation and caspase-3 activation.…”

Section: Blocking Degradation Of Activated Pkc Enhances Tpa-induced Amentioning

confidence: 99%

Activation of PKC is sufficient to induce an apoptotic program in salivary gland acinar cells

et al. 2000

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Accumulating evidence suggests that specific isoforms of PKC may function to promote apoptosis. We show here that activation of the conventional and novel isoforms of PKC with 12-O-tetradecanoyl phorbol-13-ester (TPA) induces apoptosis in salivary acinar cells as indicated by DNA fragmentation and activation of caspase-3. TPA-induced DNA fragmentation, caspase-3 activation, and morphologic indicators of apoptosis, can be enhanced by pretreatment of cells with the calpain inhibitor, calpeptin, prior to the addition of TPA. Analysis of PKC isoform expression by immunoblot shows that TPAinduced downregulation of PKCa and PKCd is delayed in cells pre-treated with calpeptin, and that this correlates with an increase of these isoforms in the membrane fraction of cells. TPA-induced apoptosis is accompanied by biphasic activation of the c-jun-N-terminal kinase (JNK) pathway and inactivation of the extracellular regulated kinase (ERK) pathway. Expression of constitutively activated PKCa or PKCd, but not kinase negative mutants of these isoforms, or constitutively activated PKCe, induces apoptosis in salivary acinar cells, suggesting a role for these isoforms in TPAinduced apoptosis. These studies demonstrate that activation of PKC is sufficient for initiation of an apoptotic program in salivary acinar cells.

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Degradation of protein kinase Cα and its free catalytic subunit, protein kinase M, in intact human neuroblastoma cells and under cell‐free conditions

Cited by 47 publications

References 30 publications

Intermediate-Term Memory for Site-Specific Sensitization inAplysiaIs Maintained by Persistent Activation of Protein Kinase C

Intermediate-Term Memory for Site-Specific Sensitization inAplysiaIs Maintained by Persistent Activation of Protein Kinase C

Protein kinase C modulates pulmonary endothelial permeability: a paradigm for acute lung injury

Activation of PKC is sufficient to induce an apoptotic program in salivary gland acinar cells

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