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2 edition of effect of protein kinase C regulatory domain expression in Y1 adrenal cells found in the catalog.

effect of protein kinase C regulatory domain expression in Y1 adrenal cells

Stacey Lynn Hembruff

effect of protein kinase C regulatory domain expression in Y1 adrenal cells

by Stacey Lynn Hembruff

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  • 21 Currently reading

Published by Laurentian University, Department of Biology in Sudbury, Ont .
Written in English


Edition Notes

StatementStacey L. Hembruff.
The Physical Object
Paginationvi, 48 l. :
Number of Pages48
ID Numbers
Open LibraryOL20719316M

The N-terminal regulatory portion of PKD contains a tandem repeat of zinc finger-like cysteine-rich motifs (termed the cysteine-rich domain or CRD) highly homologous to domains found in DAG/phorbol ester-sensitive PKCs and in other signaling proteins regulated by DAG, including chimerins, Ras-GRP, Munc13, and DAG kinases (see Ref. 1 for review). In cell biology, protein kinase A is a family of enzymes whose activity is dependent on cellular levels of cyclic AMP. PKA is also known as cAMP-dependent protein kinase. Protein kinase A has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.

  Further, Sampaoli C, et al. reported that HR cells have p53 mutation, the lack of exons 8 and 9, including the part of the DNA binding domain and the entire C-terminal domain . Protein kinase C (PKC) is a family of serine/threonine protein kinases that regulate various cellular functions, includingadhesion,secretion,proliferation,differentiation and apoptosis. The family is classified into three groups on the basis of the arrangement of their regulatory domains w2[1]. Conventional isoforms (cPKC; a, b, g) contain a.

  The DNA-dependent protein kinase (DNA-PK) is a nuclear serine/threonine protein kinase composed of a large catalytic subunit (DNA-PKcs) and a . Download Citation | A single cell level measurement of StAR expression and activity in adrenal cells | The Steroidogenic acute regulatory protein (StAR) directs mitochondrial cholesterol uptake.


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Effect of protein kinase C regulatory domain expression in Y1 adrenal cells by Stacey Lynn Hembruff Download PDF EPUB FB2

(C) Effect of different 8-Cl-cAMP concentrations on apoptosis in cultured Y1 cells. A significant increase in caspase-3 activity was observed after 8-Cl cAMP incubation ( μM), this effect being partially abolished by PKA blockade with PKI. No effect on caspase-3 activity was observed after incubation with 8-Br cAMP ( μM).Cited by: tein kinase C is present in the cytoskeletons of adrenocortical cells.

For this purpose we have used Y-1 mouse adrenal tu- mor cells which serve as a useful system for studies of the regulation of adrenal steroidogenesis (16). We show here that protein kinase C is present in the cytoskeletons of these cells.

Forskolin, like other agents that raise intracellular levels of cAMP, inhibits the proliferation of Y1 adrenal cells and causes the cells to round up and detach from the culture dishes in which they are grown (Schimmer and Tsao, ).The combined effects of forskolin on cell proliferation and morphology markedly reduce the plating efficiency of Y1 cells and permit the isolation and Cited by: 8.

The steroidogenic acute regulatory protein (STAR) protein expression is required for cholesterol transport into mitochondria to initiate steroidogenesis in the adrenal and gonads. STAR is synthesized as a 37 kDa precursor protein which is targeted to the mitochondria and imported and processed to an intra-mitochondrial 30 kDa protein.

Tropic hormone stimulation of the cAMP-dependent protein Cited by: 3. The contributions of protein kinase A and protein kinase C to these genome-wide effects of ACTH were evaluated in microarray experiments after treatment of Y1 cells and derivative protein kinase A.

This report summarizes the genome-wide effects of ACTH on transcript accumulation in mouse adrenal Y1 cells and the relative contributions of the cAMP- protein kinase C- and Ca 2+-dependent signaling pathways to these actions of the affected the accumulation of transcripts, a much larger number than previously appreciated.

Effects of hypoxia on classical protein kinase C (PKC) isoforms. Hep3B cells were exposed to hypoxic conditions for 20 h and lysed in hypotonic lysis buffer (see Section 2).

One hundred μg of each sample was run on a % denaturing polyacrylamide gel and blotted to PVDF membrane. The cAMP/protein kinase A (PKA) pathway is crucial for the function of the adrenal gland [13, 14] (Figure 1). Corticotropin (ACTH) binds to its G protein-coupled transmembrane receptor (MC2R), leading to the synthesis of cAMP by adenylate cyclase [15].

cAMP, acting as a secondary messenger, targets tetramer PKA. Protein kinase D2 (PKD2) belongs to the PKD family of serine/threonine kinases that is activated by phorbol esters and G protein-coupled receptors (GPCRs). Its C-terminal regulatory domain comprises two cysteine-rich domains (C1a/C1b) followed by a pleckstrin homology (PH) domain.

The cAMP-dependent protein kinase (PKA) 1 is a ubiquitous enzyme central to many physiological functions, including cell division and differentiation, cell morphology, cell vesicle formation, apoptosis, glycolysis, and neuronal plasticity.

The catalytic (C) subunits of PKA catalyze the transfer of the ATP γ-phosphate to a protein substrate. Linking protein kinase C to the cell cycle: ectopic expression of PKC eta in NIH3T3 cells alters the expression of cyclins and Cdk inhibitors and induces adipogenesis.

Oncogene 12 – [ PubMed ]. Precursor STAR Expression in Y1 Cells. Y1 cells were treated with 8Br-cAMP either in the absence or presence of the 26S proteasome inhibitors epoxomicin (Epox) or MG and phosphoSTAR (pSTAR) and total STAR (tSTAR) protein were detected by Western blot analysis of.

Protein kinases and phosphatases play pivotal roles in regulating and coordinating aspects of metabolism, gene expression, cell growth, cell motility, cell differentiation, and cell division. As a result, if cellular life is to function in an orderly manner, the switching on and off of protein kinases and phosphatases is as crucial for their function as their catalytic activity.

Consistent with our previous study, STAR expression in Kin-8 cells was detectable after 8Br-cAMP treatment with protein levels 50% of that detected in Y1 cells. Phosphorylated STAR protein was undetectable in untreated Y1 and Kin-8 cells (Figure 1 A) and 8Br-cAMP or ACTH treatment resulted in the appearance of pSTAR protein in only in the Y1 cells.

Somatic mutations in protein kinase A catalytic α subunit (PRKACA) were found to be causative for 30–40% of cortisol-producing adenomas (CPA) of the adrenal.

Adrenocorticotropin Induces Mitogen-Activated Protein Kinase Phosphatase 1 in Y1 Mouse Adrenocortical Tumor Cells Article (PDF Available) in Endocrinology (4).

In adrenocortical cells, adrenocorticotropin (ACTH) promotes the activation of several protein kinases.

The action of these kinases is linked to steroid production, mainly through steroidogenic acute regulatory protein (StAR), whose expression and activity are dependent on protein phosphorylation events at genomic and non-genomic levels. Hormone-dependent mitochondrial dynamics and cell.

Structure. Members of the protein kinase C family are a single polypeptide, comprised of an N-terminal regulatory region (approximately kDa) and a C-terminal catalytic region (approximately 45 kDa) ().Cloning of the first isozymes in the mids revealed four conserved domains: C1-C4().Each is a functional module, and many unrelated proteins have one or the other().

Protein kinase A-dependent signaling accounted for 56% of the ACTH effect; protein kinase C-dependent signaling accounted for an additional 6%. These results indicate that ACTH affects the expression profile of Y1 adrenal cells principally through cAMP- and protein kinase A.

A regulatory role for protein kinase C (PKC) and eicosanoids has been implicated in the control of breast cancer cell growth and function.

Here we report on the effects of the two PKC agonists O-tetradecanoyl-phorbolacetate (TPA) and bryostatin 1 on arachidonic acid metabolism, prostaglandin E2 (PGE2) production, and growth in MDA MB human breast cancer cells. expression in both MA Leydig and Y1 adrenocortical cells (38), in addition to SF-1 activation (26).

In addition to their role in ster oid biosynthesis, ERK1/2 is also. In the adrenal cortex, corticotropin induces the expression of several genes encoding proteins involved in the synthesis and intracellular transport of steroid hormones via the protein kinase A (PKA) signalling pathway, and this process is mediated by steroidogenic factor-1 (SF-1).

This study was designed to elucidate the influence of the PKA and PKC pathways on the expression of the SF-1. Effects of protein kinase A (PKA) and protein kinase C (PKC) stimulation on the expression of SF-1 in Y-1 cells.

Y-1 cells were incubated for 12 h with or without (control) forskolin (an activator of the PKA pathway), or with or without (control) tetradecanoyl phorbol acetate (TPA; an activator of PKC pathway).