Mitochondrial heat shock protein participates in placental steroidogenesis

Olvera-Sánchez, Sofía; Espinosa-García, María Teresa; Monreal, J. A.; Flores-Herrera, Óscar; Martı́nez, Federico

doi:10.1016/j.placenta.2010.12.018

Cited by 40 publications

(16 citation statements)

References 43 publications

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“…These conserved START domains of both MLN64 and StAR can bind cholesterol, but whereas StAR acts as a cholesterol transporter in mitochondria ( 144 ), MLN64 participates in cholesterol transport from endosomes to cytoplasmic acceptor(s) ( 131 ). The mechanism of action of full-length MLN64 remains unclear, although the START domain of MLN64 is found as a cleavage protein in the placenta ( 143 ), and a recent report suggests that the START domain of MLN64 interacts with a cytoplasmic 60 kDa heat shock protein (HSP60) to stimulate steroidogenesis in placental mitochondria ( 145 ). Another recent study identifi ed MLN64 as a lutein-binding protein in the retina and, hence, potentially involved in preventing night blindness ( 146 ).…”

Section: Transport Of Cholesterol To Mitochondria: Cholesterol-bindinmentioning

confidence: 99%

“…The mechanism of StAR-independent steroidogenesis is unclear; it may occur without a triggering protein, or some other protein may exert StAR-like activity to promote cholesterol fl ux but without StAR's rapid kinetics. Some data suggest that a 30 kDa proteolytic cleavage product of MLN64 exerts StAR-like activity in the placenta and elsewhere ( 143,145 ).…”

Section: Acute Versus Chronic Regulation Ofmentioning

confidence: 99%

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Early steps in steroidogenesis: intracellular cholesterol trafficking

Miller

Bose

2011

Journal of Lipid Research

444

398

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Section: Transport Of Cholesterol To Mitochondria: Cholesterol-bindinmentioning

confidence: 99%

Section: Acute Versus Chronic Regulation Ofmentioning

confidence: 99%

Early steps in steroidogenesis: intracellular cholesterol trafficking

Miller

Bose

2011

Journal of Lipid Research

444

398

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“…Immunoblots of putative mitochondria pellets were performed using rabbit polyclonal antibody adenine nucleotide translocator proteins 1, 2, 3, and 4 (ANT1/2/3/4, Santa Cruz Biotechnology), which is a multipass membrane protein of the mitochondrial inner membrane that can be used to quantify mitochondria (Olvera-Sanchez et al 2011). Isolated mitochondria extracts were suspended in 1# phosphate-buffered saline (PBS) solution and incubated in boiling water for 5 min to break the mitochondria membrane and denature the proteins released.…”

Section: Immunocytochemistry: Western Blot Analysismentioning

confidence: 99%

High Concentrations of Ketocarotenoids in Hepatic Mitochondria ofHaemorhous mexicanus

Johnson

Cobine

et al. 2015

Physiological and Biochemical Zoology

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JSTOR is a not-for-profit service that helps scholars, researchers, and students discover, use, and build upon a wide range of content in a trusted digital archive. We use information technology and tools to increase productivity and facilitate new forms of scholarship. For more information about JSTOR, please contact support@jstor.org. ABSTRACTVertebrates cannot synthesize carotenoid pigments de novo, so to produce carotenoid-based coloration they must ingest carotenoids. Most songbirds that deposit red carotenoids in feathers, bills, eyes, or skin ingest only yellow or orange dietary pigments, which they oxidize to red pigments via a ketolation reaction. It has been hypothesized that carotenoid ketolation occurs in the liver of vertebrates, but this hypothesis remains to be confirmed. To better understand the role of hepatocytes in the production of ketolated carotenoids in songbirds, we measured the carotenoid content of subcellular components of hepatocytes from wild male house finches (Haemorhous mexicanus) that were molting red, ketocarotenoid-containing feathers (e.g., 3-hydroxy-echinenone). We homogenized freshly collected livers of house finches and isolated subcellular fractions, including mitochondria. We found the highest concentration of ketocarotenoids in the mitochondrial fraction. These observations are consistent with the hypothesis that carotenoid pigments are oxidized on or within hepatic mitochondria, esterified, and then transported to the Golgi apparatus for secretory processing.

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“…Indeed, there is evidence that STARD3 is able to mediate cholesterol egress from the endosomes to the mitochondria , partnering with NPC2 in the absence of NPC1 . Moreover, STARD3 is proposed to play a role in steroidogenic cells that do not express STAR, such as in the placenta , because STARD3 START domain fragments have been found in these cells . Moreover, the STARD3 START domain possesses approximately 75% of the steroidogenic activity as the STAR START domain .…”

Section: The Erc: Niemann–pick Type C Proteins and Stard3mentioning

confidence: 99%

Binding Domain‐Driven Intracellular Trafficking of Sterols for Synthesis of Steroid Hormones, Bile Acids and Oxysterols

Midzak

Papadopoulos

2014

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Steroid hormones, bioactive oxysterols and bile acids are all derived from the biological metabolism of lipid cholesterol. The enzymatic pathways generating these compounds have been an area of intense research for almost a century, as cholesterol and its metabolites have substantial impacts on human health. Owing to its high degree of hydrophobicity and the chemical properties that it confers to biological membranes, the distribution of cholesterol in cells is tightly controlled, with subcellular organelles exhibiting highly divergent levels of cholesterol. The manners in which cells maintain such sterol distributions are of great interest in the study of steroid and bile acid synthesis, as limiting cholesterol substrate to the enzymatic pathways is the principal mechanism by which production of steroids and bile acids is regulated. The mechanisms by which cholesterol moves within cells, however, remain poorly understood. In this review, we examine the subcellular machinery involved in cholesterol metabolism to steroid hormones and bile acid, relating it to both lipid-and protein-based mechanisms facilitating intracellular and intraorganellar cholesterol movement and delivery to these pathways. In The lipid cholesterol has generated some of the greatest research interest regarding the chemicals that make up life. Providing profoundly critical physical properties as a component of the membranes that separate the biotic from the abiotic, cholesterol exerts significant physiological effects in its own right. Moreover, cholesterol is enzymatically metabolized in cells to structurally diverse families of steroids, oxysterols and bile acids, each of which have specific and highly potent signaling capabilities. Our understanding of the ways through which cells handle cholesterol and respond to cholesterol metabolite signaling has expanded enormously over the past half century. However, the manner in which cells synthesize steroids and other cholesterol metabolites, despite the progress made, has yet to fully integrate the advances of cholesterol biophysics and cellular biology into its theoretical framework. These issues have captured the interest of researchers in the field (1), and in this review, we look to extend on this www.traffic.dk 895

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Mitochondrial heat shock protein participates in placental steroidogenesis

Cited by 40 publications

References 43 publications

Early steps in steroidogenesis: intracellular cholesterol trafficking

Early steps in steroidogenesis: intracellular cholesterol trafficking

High Concentrations of Ketocarotenoids in Hepatic Mitochondria ofHaemorhous mexicanus

Binding Domain‐Driven Intracellular Trafficking of Sterols for Synthesis of Steroid Hormones, Bile Acids and Oxysterols

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