GO:0008426 protein kinase C inhibitor activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0008426 (protein kinase C inhibitor activity) describes a molecular function in which a protein or small molecule binds to and reduces the enzymatic activity of protein kinase C (PKC), a lipid-regulated serine/threonine kinase.
• PKC inhibition is achieved by diverse mechanisms, including competition with ATP or diacylglycerol (DAG), interference with phospholipid cofactor binding, and light-dependent paradoxical activation at high concentrations.
• Small-molecule PKC inhibitors such as calphostin C, enzastaurin, H7, and procyanidins are widely used to probe PKC-dependent signaling in cancer, pigmentation, and hair biology.
• PKC activity and its inhibition intersect with G-protein-coupled receptor signaling, including dopamine D4 receptor-mediated phospholipid methylation and adrenergic regulation of cyclic nucleotides.
• Endogenous protein regulators such as PKC-eta (PRKCH) illustrate that PKC family members are subject to novel modes of regulation beyond classical lipid cofactors.
• CRISPR-based knockout, point-mutation, knock-in, and overexpression models enable causal dissection of PKC inhibitor activity in disease-relevant cell types.
Description
Protein kinase C (PKC) is a family of lipid-dependent serine/threonine kinases that phosphorylate a wide range of protein substrates and thereby control cell proliferation, differentiation, and survival. The Gene Ontology term GO:0008426, protein kinase C inhibitor activity, defines a molecular function in which a gene product binds to and stops, prevents, or reduces PKC enzymatic activity. This function is distinct from generic kinase inhibition because it specifically targets PKC, an enzyme whose activity is tightly coupled to diacylglycerol and phospholipid cofactors. Researchers study GO:0008426 to understand how PKC signaling is buffered, how pharmacological inhibitors work, and how dysregulated PKC activity contributes to disease. Pharmacological PKC inhibitors have been instrumental in defining this activity. Calphostin C, a widely used PKC inhibitor, was shown to activate PKC in a light-dependent manner at high concentrations via production of singlet oxygen, revealing that inhibitor activity can be context-dependent. Enzastaurin, a selective PKC inhibitor, exhibits antitumor activity against uveal melanoma, linking PKC inhibitor activity to oncology. Several selective PKC inhibitors, including procyanidins, promote hair growth, indicating roles in epithelial biology. These examples show that GO:0008426 is not merely a biochemical curiosity but a functionally relevant activity with therapeutic implications. At the cellular level, PKC inhibitor activity intersects with GPCR signaling. Protein kinase C regulates dopamine D4 receptor-mediated phospholipid methylation, and PKC inhibitors can modulate this pathway. In rat pinealocytes, the protein kinase inhibitor H7 affects PKC activity and adrenergic stimulation of cAMP and cGMP, demonstrating crosstalk between PKC inhibition and cyclic nucleotide signaling. In rat osteoblastic cells, parathyroid hormone inhibits c-Jun N-terminal kinase activity by a protein kinase A-dependent pathway, illustrating the broader kinase signaling network in which PKC inhibitors are studied. Together, these findings position GO:0008426 as a key node for experimental interrogation of PKC-dependent biology.
protein kinase C inhibitor activity At A Glance
| GO ID | GO:0008426 |
|---|---|
| GO term | protein kinase C inhibitor activity |
| Ontology | molecular_function |
| Synonym | PKC inhibitor activity; diacylglycerol-activated phospholipid-dependent PKC inhibitor activity |
| Major function | Binds to and reduces the enzymatic activity of protein kinase C, a lipid-dependent serine/threonine kinase |
| Cofactor context | PKC activity depends on diacylglycerol and phospholipid cofactors, which inhibitors can antagonize |
| Representative inhibitors | Calphostin C, enzastaurin, H7, procyanidins |
| Disease relevance | Cancer (uveal melanoma), hair growth disorders, and GPCR-linked signaling |
What Is GO:0008426?
GO:0008426, protein kinase C inhibitor activity, is a molecular function defined by the Gene Ontology as binding to and stopping, preventing, or reducing the activity of protein kinase C, an enzyme that phosphorylates proteins. In practice, a gene product annotated with this term acts as a negative regulator of PKC enzymatic output, either by direct physical interaction or by interfering with the cofactors and substrates required for PKC catalysis. The term is synonymous with diacylglycerol-activated phospholipid-dependent PKC inhibitor activity and PKC inhibitor activity.
Why Is protein kinase C inhibitor activity Important in Cell Biology?
GO:0008426 is important because PKC sits at the crossroads of lipid second-messenger signaling and phosphorylation cascades that control cell fate. Understanding how PKC inhibitor activity is exerted helps researchers interpret pharmacological experiments, design selective inhibitors, and identify endogenous regulators of PKC. Because PKC inhibitors such as enzastaurin show antitumor activity and procyanidins promote hair growth, this GO term connects directly to therapeutic development and regenerative biology. Moreover, PKC inhibitor activity modulates GPCR-driven pathways, including dopamine D4 receptor-mediated phospholipid methylation and adrenergic regulation of cyclic nucleotides, making it relevant to neurobiology and endocrinology.
• Defines a specific molecular function that negatively regulates PKC, a central lipid-dependent kinase.
• Provides a mechanistic basis for interpreting small-molecule PKC inhibitors such as calphostin C and enzastaurin.
• Links PKC inhibition to antitumor activity in uveal melanoma, supporting oncology research.
• Connects PKC inhibitor activity to hair growth promotion by selective inhibitors including procyanidins.
• Reveals context-dependent effects, such as light-dependent PKC activation by calphostin C at high concentrations.
• Intersects with GPCR signaling, including dopamine D4 receptor-mediated phospholipid methylation.
• Modulates adrenergic stimulation of cAMP and cGMP in pinealocytes via protein kinase inhibitors such as H7.
• Highlights crosstalk with other kinases, including PKA-dependent inhibition of JNK in osteoblastic cells.
• Supports development of CRISPR models to test causal roles of PKC inhibitor activity in disease.
• Enables functional annotation of genes and compounds in PKC-dependent signaling networks.
Mechanism, Genes and Research Methods
Biological Process: What Happens During protein kinase C inhibitor activity?
In simple terms: An inhibitor molecule binds to PKC and blocks its ability to add phosphate groups to target proteins.
Protein kinase C inhibitor activity occurs when a gene product or compound physically interacts with PKC and reduces its catalytic output. Because PKC is activated by diacylglycerol and phospholipids, inhibitors can act by competing with these cofactors or by binding to the kinase domain. In cells, this inhibition dampens downstream phosphorylation events that control proliferation, differentiation, and secretion. Pharmacological examples include calphostin C, which at high concentrations can paradoxically activate PKC in a light-dependent manner via singlet oxygen production, illustrating that inhibitor activity is not always monotonic. Enzastaurin exhibits antitumor activity against uveal melanoma, showing that PKC inhibition can translate into phenotypic outcomes. Procyanidins and other selective PKC inhibitors promote hair growth, linking this activity to epithelial regeneration.
Cellular Component: Structure and Composition of protein kinase C inhibitor activity
In simple terms: The inhibitor function is carried out by proteins or small molecules that dock onto PKC or its regulatory lipids.
The structural basis of PKC inhibitor activity involves the PKC holoenzyme, which comprises regulatory domains that bind diacylglycerol and phospholipids and a catalytic kinase domain. Inhibitors may be small molecules that occupy the ATP-binding site or the diacylglycerol-binding region, or proteins that sequester PKC cofactors. Calphostin C is a perylenequinone that interacts with the regulatory domain of PKC and can generate singlet oxygen under light, modifying its inhibitory profile. Enzastaurin is a bisindolylmaleimide-like inhibitor that targets PKC beta and has been tested in melanoma models. The composition of the inhibitor complex therefore includes PKC itself, the inhibitor molecule, and in some cases membrane phospholipids that modulate binding.
Molecular Function: Substrate and Catalytic Mechanism
In simple terms: PKC normally transfers phosphate from ATP to protein substrates; inhibitors interfere with this transfer.
PKC catalyzes the transfer of the gamma-phosphate of ATP to serine and threonine residues on substrate proteins, a reaction that requires diacylglycerol and phospholipid cofactors. Protein kinase C inhibitor activity reduces this catalytic rate by preventing ATP binding, blocking substrate access, or disrupting cofactor-dependent activation. The term GO:0008426 specifically captures the function of binding to and stopping, preventing, or reducing PKC activity, rather than general kinase inhibition. Because PKC is a lipid-regulated enzyme, inhibitors that mimic or deplete diacylglycerol can shift the kinase into an inactive conformation. This mechanism is exploited by compounds such as H7, which affects PKC activity and adrenergic stimulation of cAMP and cGMP in rat pinealocytes.
Regulation of PKC Inhibitor Activity
In simple terms: The ability to inhibit PKC can itself be turned up or down by light, lipids, and other signaling inputs.
PKC inhibitor activity is regulated by the same inputs that control PKC: lipid cofactors, calcium, and phosphorylation. Calphostin C illustrates a striking regulatory twist, as its inhibitory versus activating effects depend on light exposure and concentration, with high concentrations producing singlet oxygen that activates PKC. Endogenous regulation of PKC family members can also occur through novel mechanisms, as shown for PKC-eta, which is subject to distinct regulatory control. In rat osteoblastic cells, parathyroid hormone inhibits JNK activity via a PKA-dependent pathway, demonstrating that PKC-related signaling is embedded in a broader kinase regulatory network. These examples show that PKC inhibitor activity is not a static property but a dynamically regulated function.
Crosstalk with GPCR and Cyclic Nucleotide Signaling
In simple terms: PKC inhibitors can change how cells respond to hormones and neurotransmitters.
PKC inhibitor activity intersects with G-protein-coupled receptor signaling. Protein kinase C regulates dopamine D4 receptor-mediated phospholipid methylation, and modulating PKC activity alters this pathway. In rat pinealocytes, the protein kinase inhibitor H7 affects PKC activity and adrenergic stimulation of cAMP and cGMP, revealing crosstalk between PKC inhibition and cyclic nucleotide second messengers. These findings indicate that GO:0008426 is relevant to neuroendocrine and neurotransmitter signaling contexts. Such crosstalk also provides experimental handles: measuring cAMP, cGMP, or phospholipid methylation can report on PKC inhibitor activity in cells.
Key Genes Involved in GO:0008426 protein kinase C inhibitor activity
The following genes and proteins are central to the study of protein kinase C inhibitor activity, either as PKC family members, direct inhibitors, or signaling partners.
| Gene | Major Role | Research Relevance |
|---|---|---|
| PRKCA | PKC alpha isoform, a diacylglycerol- and phospholipid-dependent kinase | Target of inhibitor activity; widely studied in cancer and signaling |
| PRKCB | PKC beta isoform | Target of enzastaurin in uveal melanoma models |
| PRKCH | PKC eta isoform with novel regulation | Illustrates non-classical PKC regulation relevant to inhibitor studies |
| PRKCG | PKC gamma isoform | PKC family member subject to lipid-dependent regulation |
| PRKCD | PKC delta isoform | PKC family member implicated in diverse signaling pathways |
| PRKCE | PKC epsilon isoform | PKC family member studied in lipid-regulated signaling |
| DRD4 | Dopamine D4 receptor | PKC regulates DRD4-mediated phospholipid methylation |
| JNK (MAPK8/9/10) | Stress-activated kinase | PTH inhibits JNK via PKA-dependent pathway, showing kinase crosstalk |
| PKA (PRKACA/B) | cAMP-dependent protein kinase | Mediates PTH-dependent JNK inhibition in osteoblastic cells |
| Calphostin C target (PKC) | Small-molecule PKC inhibitor | Light-dependent activation at high concentrations via singlet oxygen |
| Enzastaurin target (PKC beta) | Selective PKC inhibitor | Antitumor activity in uveal melanoma |
| Procyanidin target (PKC) | Selective PKC inhibitor | Promotes hair growth in skin pharmacology studies |
| H7 target (PKC) | Protein kinase inhibitor | Affects PKC and adrenergic cAMP/cGMP in pinealocytes |
| Diacylglycerol (DAG) | Lipid cofactor | Required for PKC activation; inhibitors can antagonize DAG binding |
| Phospholipids | Membrane cofactors | Support PKC activation and are targeted by inhibitor mechanisms |
| ATP | Phosphate donor | Competitive inhibitors block ATP binding to PKC |
How Is protein kinase C inhibitor activity Regulated?
PKC inhibitor activity is regulated at multiple levels. The primary layer is lipid-dependent regulation of PKC itself, because diacylglycerol and phospholipids are required for PKC activation and inhibitors can antagonize these cofactors. A second layer is light- and concentration-dependent behavior of inhibitors such as calphostin C, which activates PKC at high concentrations via singlet oxygen production. A third layer involves endogenous regulatory mechanisms, as exemplified by novel regulation of PKC-eta. Finally, PKC inhibitor activity is embedded in kinase signaling networks, including PKA-dependent inhibition of JNK in osteoblastic cells and adrenergic modulation of cAMP and cGMP in pinealocytes. These layers mean that experimental interpretation of GO:0008426 must account for context, dose, and crosstalk.
protein kinase C inhibitor activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PRKCB | Uveal melanoma | Enzastaurin-treated melanoma cell lines and xenografts |
| PRKCA | Cancer and general PKC signaling | PKC inhibitor-treated cancer cell lines |
| PRKCH | PKC-eta regulation in disease | Knockout or overexpression models for PKC-eta |
| DRD4 | Neuropsychiatric signaling | Dopamine D4 receptor-expressing cells with PKC inhibitors |
| JNK/PKA axis | Bone and metabolic signaling | Osteoblastic cells treated with PTH and kinase inhibitors |
Cancer and Uveal Melanoma
PKC inhibitor activity has direct oncology relevance. Enzastaurin, a selective PKC inhibitor, exhibits antitumor activity against uveal melanoma, indicating that reducing PKC signaling can suppress tumor growth in this cancer type. Because PKC is a lipid-dependent kinase that drives proliferation and survival, inhibitors annotated with GO:0008426 are candidate therapeutic agents. Experimental models using enzastaurin in melanoma cell lines provide a template for testing PKC inhibitor activity in other cancers.
Hair Growth and Skin Biology
Several selective PKC inhibitors, including procyanidins, promote hair growth, linking GO:0008426 to epithelial regeneration. This suggests that PKC inhibitor activity can modulate follicular cycling and may be relevant to alopecia or skin pharmacology. The mechanism likely involves dampening PKC-dependent signaling in hair follicle cells, although the precise pathways require further study.
Neuropsychiatric and Neuroendocrine Signaling
PKC regulates dopamine D4 receptor-mediated phospholipid methylation, a pathway implicated in neurotransmission and potentially in neuropsychiatric conditions. In rat pinealocytes, protein kinase inhibitors such as H7 affect PKC activity and adrenergic stimulation of cAMP and cGMP, connecting GO:0008426 to neuroendocrine regulation. These findings suggest that PKC inhibitor activity can influence dopamine and adrenergic signaling, with implications for neurological and endocrine research.
Bone and Metabolic Signaling
Parathyroid hormone inhibits c-Jun N-terminal kinase activity in rat osteoblastic cells by a protein kinase A-dependent pathway, illustrating how kinase signaling crosstalk affects bone biology. Although this study focuses on PKA, it provides a framework for understanding how PKC inhibitor activity may intersect with bone cell signaling. PKC inhibitors are therefore useful tools for dissecting kinase networks in osteoblasts and related metabolic tissues.
From protein kinase C inhibitor activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of a candidate PKC inhibitor gene increase PKC activity? | CRISPR knockout cell line with PKC substrate phosphorylation readout |
| Does a point mutation in the inhibitor binding interface alter PKC inhibition? | CRISPR point-mutation knock-in cell line |
| Can a tagged inhibitor protein be used to measure PKC interaction? | Tagged knock-in of the inhibitor gene |
| Does overexpression of a PKC inhibitor reduce tumor growth? | Overexpression cell model in melanoma or cancer lines |
| Does PKC inhibitor activity modulate GPCR signaling? | Cells expressing DRD4 or adrenergic receptors treated with inhibitors |
| Does PKC inhibition affect hair follicle biology? | Skin or follicle organ culture with procyanidins |
How to Study the protein kinase C inhibitor activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| In vitro kinase assay | Phosphate incorporation into PKC substrates | Testing inhibitor potency and mechanism |
| Phospho-specific immunoblotting | PKC substrate phosphorylation in cells | Validating inhibitor activity in cell lines |
| cAMP/cGMP assays | Cyclic nucleotide levels | Adrenergic signaling in pinealocytes |
| Phospholipid methylation assay | Dopamine D4 receptor-mediated methylation | GPCR-PKC crosstalk studies |
| CRISPR knockout | Loss-of-function of candidate inhibitor genes | Causal testing of GO:0008426 |
| CRISPR point mutation | Specific residue effects on inhibitor function | Mapping binding interfaces |
| Tagged knock-in | Protein interaction and localization | Proteomic and imaging studies |
| Overexpression | Gain-of-function of inhibitor genes | Tumor suppression and phenotype testing |
Kinase Activity Assays
PKC inhibitor activity is classically measured using kinase assays that quantify phosphate incorporation into PKC substrates in the presence or absence of inhibitor. These assays can use purified PKC, diacylglycerol, and phospholipid cofactors to reconstitute the lipid-dependent activation state. Compounds such as calphostin C, enzastaurin, H7, and procyanidins can be tested for dose-dependent inhibition. Care must be taken with light-sensitive inhibitors like calphostin C, which can activate PKC at high concentrations via singlet oxygen.
Phospho-Substrate and Signaling Readouts
Downstream phosphorylation events report on PKC inhibitor activity in cells. For example, PKC regulates dopamine D4 receptor-mediated phospholipid methylation, which can be measured as a functional readout. In pinealocytes, cAMP and cGMP levels reflect adrenergic stimulation and PKC inhibitor effects. In osteoblastic cells, JNK activity is a readout for PKA-dependent signaling that intersects with PKC pathways. Combining phospho-specific antibodies with inhibitor treatment provides a robust way to quantify GO:0008426 activity.
CRISPR-Based Genetic Models
CRISPR knockout, point-mutation, knock-in, and overexpression models allow causal testing of genes annotated with PKC inhibitor activity. Knockout of a candidate inhibitor should increase PKC substrate phosphorylation if the gene functions in GO:0008426. Point mutations can dissect binding interfaces, while tagged knock-ins enable interaction proteomics. Overexpression can test whether increased inhibitor levels suppress PKC-dependent phenotypes such as tumor growth. These approaches are complemented by pharmacological inhibitors like enzastaurin and procyanidins.
Phenotypic and Disease Models
Phenotypic assays link PKC inhibitor activity to disease biology. Uveal melanoma cells treated with enzastaurin show antitumor activity, providing a cancer model. Hair growth promotion by procyanidins offers a regenerative model. Neuroendocrine readouts in pinealocytes and dopamine D4 receptor signaling provide neurobiological models. Bone cell studies with PTH and kinase inhibitors offer a metabolic model. Together, these systems enable functional validation of GO:0008426 in physiologically relevant contexts.
How CRISPR Can Be Used to Study GO:0008426 protein kinase C inhibitor activity
Knockout
CRISPR knockout of a gene annotated with protein kinase C inhibitor activity removes the inhibitor and is expected to increase PKC substrate phosphorylation if the gene functions in GO:0008426. Knockout models are essential for distinguishing direct PKC inhibition from indirect effects. For example, knocking out a PKC inhibitor in melanoma cells could test whether loss of inhibition enhances tumor growth, complementing enzastaurin studies. Knockout of PKC-eta regulators can reveal novel control mechanisms.
Point Mutation
CRISPR point mutation introduces specific amino acid changes to dissect the binding interface between a PKC inhibitor and PKC. This approach can identify residues required for inhibitor activity without deleting the entire protein. Point mutations are particularly useful for separating PKC inhibitor activity from other functions of a multifunctional protein. They can also model disease-associated variants in PKC or its regulators.
Knock-in
CRISPR knock-in can add tags, reporters, or disease-relevant alleles to genes involved in PKC inhibitor activity. Tagged knock-in enables immunoprecipitation and mass spectrometry to identify PKC-inhibitor complexes. Knock-in of mutant PKC alleles can test how structural changes affect inhibitor sensitivity. This approach is valuable for studying endogenous regulation of PKC-eta and other family members.
Overexpression
CRISPR overexpression or cDNA-based overexpression of a PKC inhibitor gene tests gain-of-function phenotypes. Overexpression can suppress PKC-dependent proliferation and survival, as suggested by antitumor activity of enzastaurin. In hair follicle models, overexpression of PKC inhibitors could mimic procyanidin effects. Overexpression models are also useful for biochemical purification of inhibitor-PKC complexes.
How EDITGENE Supports protein kinase C inhibitor activity Research
Researchers studying protein kinase C inhibitor activity-related genes often need to determine whether a candidate gene is causally involved in PKC regulation or is merely correlated with pathway changes. EDITGENE provides CRISPR-based cell model services that enable precise knockout, point mutation, knock-in, and overexpression of genes in this pathway, supported by library screening and bioinformatics for functional annotation.
Contact EDITGENE today to design your custom CRISPR model for protein kinase C inhibitor activity research.
Frequently Asked Questions About protein kinase C inhibitor activity
What is protein kinase C inhibitor activity?
Protein kinase C inhibitor activity (GO:0008426) is a molecular function in which a gene product binds to and stops, prevents, or reduces the activity of protein kinase C, a lipid-dependent serine/threonine kinase.
What genes are involved in protein kinase C inhibitor activity?
Genes and proteins involved include PKC family members such as PRKCA, PRKCB, PRKCH, and PRKCG, as well as signaling partners like DRD4 and JNK/PKA components.
What is the GO ID for protein kinase C inhibitor activity?
The GO ID is GO:0008426, under the molecular_function ontology.
How do PKC inhibitors work?
PKC inhibitors work by competing with ATP or diacylglycerol, disrupting phospholipid cofactor binding, or otherwise preventing PKC from phosphorylating substrates. Some, like calphostin C, can paradoxically activate PKC at high concentrations via singlet oxygen.
What diseases are linked to PKC inhibitor activity?
PKC inhibitor activity is linked to cancer such as uveal melanoma, hair growth disorders, and neuropsychiatric or neuroendocrine signaling.
What is enzastaurin?
Enzastaurin is a selective PKC inhibitor that exhibits antitumor activity against uveal melanoma.
Do procyanidins inhibit PKC?
Yes, several selective PKC inhibitors including procyanidins promote hair growth, indicating PKC inhibitor activity in skin biology.
How is PKC inhibitor activity measured?
It is measured using kinase assays, phospho-substrate immunoblotting, cAMP/cGMP assays, and phospholipid methylation assays, often combined with CRISPR models.
What is the difference between PKC inhibitor activity and PKC activity?
PKC activity is the kinase function that phosphorylates substrates, while PKC inhibitor activity is the function that binds to and reduces PKC activity.
Can CRISPR be used to study protein kinase C inhibitor activity?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models enable causal testing of genes involved in PKC inhibitor activity.
Conclusion
GO:0008426, protein kinase C inhibitor activity, defines a molecular function that negatively regulates PKC, a central lipid-dependent kinase. Research using calphostin C, enzastaurin, procyanidins, and H7 has revealed diverse mechanisms and disease links, from uveal melanoma to hair growth and neuroendocrine signaling. Understanding this activity requires attention to lipid cofactors, light-dependent effects, and crosstalk with GPCR and cyclic nucleotide pathways. CRISPR-based models provide a rigorous way to test causality for genes annotated with PKC inhibitor activity. By combining knockout, point mutation, knock-in, and overexpression with functional readouts, researchers can dissect how PKC inhibition shapes cell fate and disease. EDITGENE supports these efforts with tailored cell model and screening services.
References
- 1. Ishii T et al.. 2024. Protein kinase C (PKC) inhibitor Calphostin C activates PKC in a light-dependent manner at high concentrations via the production of singlet oxygen.. Eur J Pharmacol 984:177036 PMID: 39368603
- 2. Rando RR. 1988. Regulation of protein kinase C activity by lipids.. FASEB J 2(8):2348-55 PMID: 3282960
- 3. Wu X et al.. 2012. The protein kinase C inhibitor enzastaurin exhibits antitumor activity against uveal melanoma.. PLoS One 7(1):e29622 PMID: 22253748
- 4. Takahashi T et al.. 2000. Several selective protein kinase C inhibitors including procyanidins promote hair growth.. Skin Pharmacol Appl Skin Physiol 13(3-4):133-42 PMID: 10859531
- 5. Pal D et al.. 2012. Novel regulation of protein kinase C-η.. Biochem Biophys Res Commun 425(4):836-41 PMID: 22892130
- 6. Sharma A et al.. 2001. Protein kinase C regulates dopamine D4 receptor-mediated phospholipid methylation.. Eur J Pharmacol 427(2):83-90 PMID: 11557258
- 7. Ho AK et al.. 1988. Effects of protein kinase inhibitor (1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H7) on protein kinase C activity and adrenergic stimulation of cAMP and cGMP in rat pinealocytes.. Biochem Pharmacol 37(6):1015-20 PMID: 2833269
- 8. Doggett TA et al.. 2002. Parathyroid hormone inhibits c-Jun N-terminal kinase activity in rat osteoblastic cells by a protein kinase A-dependent pathway.. Endocrinology 143(5):1880-8 PMID: 11956171
