scholarly journals Protein and mRNA expression of protein kinase C (PKC) in the postmortem brain of bipolar and schizophrenic subjects

2020 ◽  
Vol 130 ◽  
pp. 362-371
Author(s):  
Ghanshyam N. Pandey ◽  
Hooriyah S. Rizavi ◽  
Xinguo Ren
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Postmortem Brain ◽  
Kinase C

scholarly journals Dysregulation of protein kinase C in adult depression and suicide: evidence from postmortem brain studies

2021 ◽  
Author(s):  
Ghanshyam N Pandey ◽  
Anuradha Sharma ◽  
Hooriyah S Rizavi ◽  
Xinguo Ren
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Expression ◽  
Mrna Expression ◽  
Postmortem Brain ◽  
Cortical Region ◽  
Cytosol Fraction ◽  
Kinase C ◽  
Pkc Isozymes

Abstract Background Several lines of evidence suggest the abnormalities of protein kinase C (PKC) signaling system in mood disorders and suicide based primarily on the studies of PKC and its isozymes in the platelets and postmortem brain of depressed and suicidal subjects. In this study we examined the role of PKC isozymes in depression and suicide. Methods We determined the protein and mRNA expression of various PKC isozymes in the prefrontal cortical region [Brodmann area 9 (BA9)] in 24 normal control (NC) subjects, 24 depressed suicide (DS) subjects and 12 depressed non-suicide (DNS) subjects. The levels of mRNA in the prefrontal cortex (PFC) were determined by qRT-PCR and the protein expression was determined by Western blotting. Results We observed a significant decrease in mRNA expression of PKCα, PKCβI, PKCδ and PKCε and decreased protein expression either in the membrane or the cytosol fraction of PKC isozymes - PKCα, PKCβI, PKCβII and PKCδ in DS and DNS subjects compared with NC subjects. Conclusions The current study provides detailed evidence of specific dysregulation of certain PKC isozymes in the postmortem brain of DS and DNS subjects and further supports earlier evidence for the role of PKC in the platelets and brain of adult and teenage depressed and suicidal population. This comprehensive study may lead to further knowledge of the involvement of PKC in the pathophysiology of depression and suicide.

Regulation of arginine vasopressin mRNA in rat fetal hypothalamic cell culture. Role of protein kinases and glucocorticoids

1993 ◽  
Vol 10 (1) ◽  
pp. 51-57 ◽  
Author(s):  
S-B Hu ◽  
L A Tannahill ◽  
S L Lightman
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Protein Kinase A ◽  
Arginine Vasopressin ◽  
In Situ Hybridization Histochemistry ◽  
Kinase C ◽  
Kinase A

ABSTRACT Studies have been performed to investigate the regulation of arginine vasopressin (AVP) mRNA expression in fetal hypothalamic cultures. AVP mRNA-positive neurones were identified by in-situ hybridization histochemistry, and changes in mRNA expression were quantitated by nuclease protection assay. Both protein kinase C and protein kinase A activators increased the expression of AVP mRNA, in contrast to dexamethasone, which inhibited the responses to both protein kinase C and protein kinase A activation.

A possible role for protein kinase C in CO2/H+-induced c-fos mRNA expression in PC12 cells

1998 ◽  
Vol 111 (2) ◽  
pp. 127-135 ◽  
Author(s):  
N.T Kuo ◽  
F.H Agani ◽  
M.A Haxhiu ◽  
C.H Chang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Pc12 Cells ◽  
Kinase C

scholarly journals Coordinate changes in gene expression which mark the spinous to granular cell transition in epidermis are regulated by protein kinase C.

1993 ◽  
Vol 120 (1) ◽  
pp. 217-225 ◽  
Author(s):  
A A Dlugosz ◽  
S H Yuspa
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Granular Cell ◽  
Cell Markers ◽  
Kinase C ◽  
Coordinate Changes ◽  
Cell Transition ◽  
In Cells

The protective function of skin depends on successful completion of a tightly regulated multi-step differentiation program, during which the induction of markers for a specific stage in epidermal differentiation is coupled to repression of markers expressed at the preceding stage. We have explored the role of protein kinase C (PKC) in this process using an in vitro model system, in which cultures of primary mouse epidermal keratinocytes are induced to terminally differentiate by raising the Ca2+ concentration in the medium from 0.05 to 0.12 mM. At doses which activate PKC, 12-O-tetradecanoylphorbol-13-acetate (TPA) and 1-oleoyl-2-acetylglycerol block Ca(2+)-mediated induction of the spinous cell markers keratins K1 and K10 at both the protein and mRNA level. TPA and 1-oleoyl-2-acetylglycerol also rapidly repress K1 and K10 mRNA expression when added to differentiating keratinocyte cultures already expressing these markers. The inhibition of K1 mRNA expression by TPA is blocked in cells where PKC has been inactivated with bryostatin. TPA-mediated loss of K1 mRNA is also blocked in cells exposed to cycloheximide or actinomycin D implicating a PKC-induced protein factor in this process. The loss of K1 mRNA in TPA-treated cultures is the result of both a selective destabilization of K1 transcripts and a rapid inhibition of K1 gene transcription. In contrast to the dramatic repression of mRNAs typical for spinous cell differentiation, activation of PKC concurrently enhances expression of mRNAs and proteins for the granular cell markers loricrin and filaggrin. This response does not occur in cells pre-treated with bryostatin to inactivate PKC. Our results suggest that PKC is a fundamental regulator of the coordinate changes in keratinocyte gene expression that occur during the spinous to granular cell transition in epidermis.

scholarly journals Calcitonin Induces 25-Hydroxyvitamin D31α-Hydroxylase mRNA Expression via Protein Kinase C Pathway in LLC-PK1Cells

1999 ◽  
Vol 10 (12) ◽  
pp. 2474-2479
Author(s):  
NORIKO YOSHIDA ◽  
TADASHI YOSHIDA ◽  
AKIRA NAKAMURA ◽  
TOSHIAKI MONKAWA ◽  
MATSUHIKO HAYASHI ◽  
...  
Keyword(s):  
Vitamin D ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Protein Kinase A ◽  
Mrna Levels ◽  
Hydroxyvitamin D ◽  
Kinase C ◽  
25 Hydroxyvitamin D ◽  
Kinase A

Abstract. The biosynthesis of 1α, 25-dihydroxyvitamin D3from 25-hydroxyvitamin D3is catalyzed by 25-hydroxyvitamin D31α-hydroxylase (CYP27B1) in renal proximal tubules. It was recently demonstrated that LLC-PK1cells express CYP27B1 mRNA, which is regulated by intracellular cAMP but not vitamin D3. To clarify the effect of calcitonin on vitamin D3metabolismin vitro, LLC-PK1cells were incubated with hormonal factors, and expression of CYP27B1 mRNA was measured by quantitative reverse transcription-PCR. Calcitonin at 100 nmol/L significantly increased CYP27B1 mRNA expression by 24 h (271 ± 21% of control). Incubation with calcitonin over a range of 1 μmol/L to 1 pmol/L resulted in a concentration-dependent increase in CYP27B1 mRNA levels. It is known that the calcitonin receptor has dual intracellular signaling pathways, via protein kinases A and C. Both 500 μmol/L 8-bromo-cAMP, a protein kinase A activator, and 100 nmol/L phorbol 12-myristate 13-acetate, a protein kinase C activator, increased CYP27B1 mRNA levels at 24 h (207 ± 54 and 246 ± 58% of control, respectively). However, calcitonin-induced CYP27B1 mRNA expression was only inhibited by the protein kinase C inhibitors staurosporine and calphostin C. The protein kinase A inhibitors Rp-cAMPS at 10 and 100 μmol/L and H-89 at 10 μmol/L had no effect on the action of calcitonin, in spite of cAMP-activation by calcitonin. The present data suggest that calcitonin upregulates CYP27B1 mRNA expression via the protein kinase C pathway in LLC-PK1cells.

IP-10 mRNA EXPRESSION IN CULTURED KERATINOCYTES IS SUPPRESSED BY INHIBITION OF PROTEIN KINASE-C AND TYROSINE KINASE AND ELEVATION OF cAMP

Cytokine ◽  
1999 ◽  
Vol 11 (7) ◽  
pp. 469-475 ◽  
Author(s):  
Dick M Boorsma ◽  
Jacoba Flier ◽  
Edward N van den Brink ◽  
Shakun Sampat ◽  
Hugo L Walg ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Mrna Expression ◽  
Cultured Keratinocytes ◽  
Kinase C

scholarly journals Differential Regulation of Angiotensin II-induced Expression of Connective Tissue Growth Factor by Protein Kinase C Isoforms in the Myocardium

2005 ◽  
Vol 280 (16) ◽  
pp. 15719-15726 ◽  
Author(s):  
Zhiheng He ◽  
Kerrie J. Way ◽  
Emi Arikawa ◽  
Eva Chou ◽  
Darren M. Opland ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Angiotensin Ii ◽  
Growth Factor ◽  
Protein Kinase ◽  
Connective Tissue ◽  
Mrna Expression ◽  
Tissue Growth ◽  
Dominant Negative ◽  
Wild Type ◽  
Kinase C

Protein kinase C (PKC) and angiotensin II (AngII) can regulate cardiac function in pathological conditions such as in diabetes or ischemic heart disease. We have reported that expression of connective tissue growth factor (CTGF) is increased in the myocardium of diabetic mice. Now we showed that the increase in CTGF expression in cardiac tissues of streptozotocin-induced diabetic rats was reversed by captopril and islet cell transplantation. Infusion of AngII in rats increased CTGF mRNA expression by 15-fold, which was completely inhibited by co-infusion with AT1 receptor antagonist, candesartan. Similarly, incubation of cultured cardiomyocytes with AngII increased CTGF mRNA expression by 2-fold, which was blocked by candesartan and a general PKC inhibitor, GF109203X. The role of PKC isoform-dependent action was further studied using adenoviral vector-mediated gene transfer of dominant negative (dn) PKC or wild type PKC isoforms. Expression of dnPKCα, -ϵ, and -ζ isoforms suppressed AngII-induced CTGF expression in cardiomyocytes. In contrast, expression of dominant negative PKCδ significantly increased AngII-induced CTGF expression, whereas expression of wild type PKCδ inhibited this induction. This inhibitory effect was further confirmed in the myocardium of transgenic mice with cardiomyocyte-specific overexpression of PKCδ (δTg mice). Thus, AngII can regulate CTGF expression in cardiomyocytes through a PKC activation-mediated pathway in an isoform-selective manner both in physiological and diabetic states and may contribute to the development of cardiac fibrosis in diabetic cardiomyopathy.

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