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BBA - Molecular Cell Research (v.1793, #12)

Editorial Board (pp. i).

Rethinking phosphatidylinositol 3-monophosphate by Marco Falasca; Tania Maffucci (pp. 1795-1803).

A generally accepted view considers phosphatidylinositol 3-monophosphate (PtdIns3 P) as a lipid confined to the endosomal compartment where it regulates trafficking pathways and is produced constitutively and exclusively by class III phosphoinositide 3-kinase (PI3K). Recent evidence suggests that this phosphoinositide has a more complex role as a second messenger involved in different physiological and pathological events and that specific intracellular localization of kinases and/or phosphatases is critical for PtdIns3 P synthesis and PtdIns3 P-dependent intracellular functions. Here, we review the current knowledge of the regulation and function of PtdIns3 P and discuss how the view of PtdIns3 P changed in the last few years.

Keywords: Autophagy; Myotubularin; mTOR; Phosphoinositide; Phosphoinositide 3-kinase; Rab5

Decreased cofilin1 expression is important for compaction during early mouse embryo development by Minyue Ma; Lin Zhou; Xuejiang Guo; Zhuo Lv; Yang Yu; Chenhui Ding; Ping Zhang; Ye Bi; Jin Xie; Liu Wang; Min Lin; Zuomin Zhou; Ran Huo; Jiahao Sha; Qi Zhou (pp. 1804-1810).

Compaction, occurring at the eight-cell stage of mouse development, is the process of cell flattening and polarization by which cellular asymmetry is first established. During this process many molecules and organelles undergo polarized distribution, but the cytoskeletal basis for these distribution specifications remains to be explored. The present study focused on cofilin1, an actin-binding protein that depolymerizes actin filaments. We showed that cofilin1 expression decreased at the compaction stage, and that down-regulation of cofilin1 expression by siRNA microinjection accelerated compaction. Continuous observation using time-lapse video miscroscopy confirmed these findings. That is, the embryonic cells microinjected with anti-cofilin1 antibody exhibit earlier adherence properties compared to uninjected cells. Pronuclear microinjection of a site-directed mutated cofilin1 plasmid, in which cofilin1 is sustained in its active form produced embryos with blastomeres that did not adhere, suggesting that inactivation of cofilin1 is critical for cell flattening and adherence. Fluorescein-phalloidin staining indicated that decreased cofilin1 expression promoted the formation of the apical pole, which is a marker for polarity. Scanning electron microscopy results demonstrated the appearance of microvilli on the outer face of blastomeres in cofilin1 knockdown embryos. Our results suggest that cofilin1 plays an important role in cortical cytoplasmic organization during embryo compaction.

Keywords: Compaction; Polarization; Early development; Embryo; Cofilin1

Mixed lineage kinase 3 negatively regulates IKK activity and enhances etoposide-induced cell death by Eric T. Cole; Yu Zhan; Widian F. Abi Saab; Amanda C. Korchnak; Brian P. Ashburner; Deborah N. Chadee (pp. 1811-1818).

Mixed lineage kinase 3 (MLK3) is a mitogen activated protein kinase kinase kinase (MAP3K) that activates multiple MAPK signaling pathways. Nuclear factor kappa B (NF-κB) is a transcription factor that has important functions in inflammation, immunity and cell survival. We found that silencing mlk3 expression with RNA interference (RNAi) in SKOV3 human ovarian cancer epithelial cells and NIH-3T3 murine fibroblasts led to a reduction in the level of the inhibitor of kappa B alpha (IκBα) protein. In addition, we observed enhanced basal IκB kinase (IKK) activity in HEK293 cells transiently transfected with MLK3 siRNA and in NIH3T3 cells stably expressing MLK3 shRNA (shMLK3). Furthermore, the basal level of NF-κB-dependent gene transcription was elevated in shMLK3 cells. Silencing mlk3 expression conferred resistance of cells to etoposide-induced apoptotic cell death and overexpression of wild type MLK3 (MLK3-WT) or kinase-dead MLK3 (MLK3-KD) promoted apoptotic cell death and cleavage of poly (ADP-ribose) polymerase (PARP). Overexpression of MLK3-WT or MLK3-KD enhanced etoposide-induced apoptotic cell death and cleavage of PARP. These data suggest that MLK3 functions to limit IKK activity, and depleting MLK3 helps protect cells from etoposide-induced cell death through activation of IKK-dependent signaling.

Keywords: MLK3; NF-κB; Apoptosis; IKK

GDF5 and BMP2 inhibit apoptosis via activation of BMPR2 and subsequent stabilization of XIAP by Zhipei Liu; Jia Shen; Kui Pu; Hugo A. Katus; Frank Plöger; Christiane P. Tiefenbacher; Xiaobo Chen; Thomas Braun (pp. 1819-1827).

GDF5 and BMP2, members of the TGF-β superfamily of growth factors, are known to regulate apoptosis in different cell types either positively or negatively. We wanted to investigate the effects of GDF5 and BMP2 on vascular smooth muscle cells and mouse embryonic fibroblasts and disclose the mechanism by which GDF5 and BMP2 might exert anti-apoptotic effects. The effect of GDF5 and BMP2 on proliferation and/or programmed cells death was assessed in isolated human vascular smooth muscle cells and mouse embryonic fibroblasts. We demonstrate that GDF5 and BMP2 prevent apoptosis induced by serum starvation in mouse embryonic fibroblasts but not in smooth muscle cells via the BMP receptor 2 (BMPR2), which is often mutated in hereditary cases of primary pulmonary hypertension. GDF5 and BMP2 stimulate the interaction of BMPR-2 with XIAP thereby reducing the ubiquitination of XIAP, which results in enhanced protein stability. The increased concentration of XIAP counteracts apoptosis by binding and inactivating activated caspases. We conclude that the inhibition of apoptosis in mouse embryonic fibroblasts by BMP2 and GDF5 does not depend on more complex signal transduction pathways such as smad and MAPK signaling but on direct stabilization of XIAP by BMPR2.

Keywords: Apoptosis; XIAP; BMP2; GDF5; Ubiquitin; BMPR2

TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells by Misato Kikuchi; Fumihiko Okumura; Tadasuke Tsukiyama; Masashi Watanabe; Naoto Miyajima; Junji Tanaka; Masahiro Imamura; Shigetsugu Hatakeyama (pp. 1828-1836).

The androgen receptor (AR) is a ligand-dependent transcription factor that belongs to the family of nuclear receptors, and its activity is regulated by numerous AR coregulators. AR plays an important role in prostate development and cancer. In this study, we found that TRIM24/transcriptional intermediary factor 1α (TIF1α), which is known as a ligand-dependent nuclear receptor co-regulator, interacts with AR and enhances transcriptional activity of AR by dihydrotestosterone in prostate cancer cells. We showed that TRIM24 functionally interacts with TIP60, which acts as a coactivator of AR and synergizes with TIP60 in the transactivation of AR. We also showed that TRIM24 binds to bromodomain containing 7 (BRD7), which can negatively regulate cell proliferation and growth. A luciferase assay indicated that BRD7 represses the AR transactivation activity upregulated by TRIM24. These findings indicate that TRIM24 regulates AR-mediated transcription in collaboration with TIP60 and BRD7.

Keywords: TRIM24; Androgen receptor; Prostate cancer; BRD7

Inflammatory protein sPLA₂-IIA abrogates TNFα-induced apoptosis in human astroglioma cells: Crucial role of ERK by Elvira Ibeas; Lucía Fuentes; Rubén Martín; Marita Hernández; María Luisa Nieto (pp. 1837-1847).

Brain injury induces the expression of well-known cytokines, such as tumor necrosis factor-alpha (TNFα), and other, which functions are less understood, as secreted phospholipase A₂ group IIA (sPLA₂-IIA). Since in pathological processes, cytokines function coordinately in networks, to further explore the actions of sPLA₂-IIA in tumorigenesis, we investigated the effect of sPLA₂-IIA in the presence of TNFα in human 1321N1 astrocytoma cells. In these cells, TNFα activates the apoptotic programme that is accompanied of cytoskeleton changes; however, simultaneous treatment with sPLA₂-IIA prevents TNFα-mediated apoptosis and reverses the modification of the markers associated to this response. In fact, the mitogenic activity elicited by the phospholipase alone is preserved. This inhibitory effect is not found in other TNFα-mediated responses, even a functional cooperation is observed on COX-2 protein induction. The cross-talk between TNFα and sPLA₂-IIA is associated with ERK activity since its pharmacological inhibition attenuates both synergistic and inhibitory responses. We have also observed that upon sPLA₂-IIA stimulation, endogenous ERK has the capacity to bind and phosphorylate sequences present within the cytoplasmic domain of TNFR1/CD120a. These findings thus indicate that sPLA₂-IIA and TNFα transduction pathways interact to modulate inflammatory responses and provide additional insights about the capacity of sPLA₂-IIA to promote apoptosis resistance in astrocytoma cells.

Keywords: Abbreviations; ERK; extracellular signal-regulated kinase; JNK; c-Jun N-terminal kinase; MAP; mitogen-activated protein; COX-2; cyclooxygenase-2; I; k; B; inhibitory; k; B protein; NF-; k; B; nuclear factor-; k; B; TNFα; tumor necrosis factor α; sPLA; ₂; -IIA; secreted phospholipase A; ₂; -IIA; TNFR; TNFα receptor; DMEM; Dulbecco's modified Eagle's medium; FBS; fetal bovine serumAstrocytoma cells; Tumor necrosis factor; Secreted phospholipase A; ₂; Protein kinases; Apoptosis; Cytokines

Mitochondrial m-calpain plays a role in the release of truncated apoptosis-inducing factor from the mitochondria by Taku Ozaki; Tetsuro Yamashita; Sei-ichi Ishiguro (pp. 1848-1859).

Calpains, calcium-dependent cysteine proteases, are involved in a variety of cellular processes. We have reported on the characteristics of mitochondrial μ-calpain and have shown that ERp57-associated mitochondrial μ-calpain cleaves the apoptosis-inducing factor (AIF) to a truncated form (tAIF). In addition, we found an unknown mitochondrial calpain. In this study, we identified and characterized this undescribed mitochondrial calpain in rat liver mitochondrial intermembrane space. The mitochondrial μ- and unknown calpains were separated by DEAE-Sepharose column chromatography. We immunoprecipitated the unknown calpain with anti-calpain small subunit and identified it as calpain 2 (m-calpain large subunit) by nanoflow-LC-MS/MS analysis and database searching. Because the identified mitochondrial calpain was stained with anti-m-calpain large subunit antibody, we named it mitochondrial m-calpain. The Ca²⁺ dependency of mitochondrial m-calpain was similar to that of cytosolic m-calpain. Immunoprecipitation analyses showed that mitochondrial m-calpain is associated with a 75-kDa glucose-regulated protein, a member of the heat shock protein 70 family. We also investigated the involvement of mitochondrial m-calpain in the release of tAIF from mitochondria. Calpain inhibitor, PD150606, an anti-voltage-dependent anion channel (VDAC), and anti-Bax antibodies prevented the release of tAIF from mitochondria. In addition, we found that mitochondrial m-calpain truncated VDAC in Ca²⁺-dependent manner. This cleavage of VDAC promotes the mitochondrial accumulation of Bax and the release of tAIF from mitochondria. The accumulated Bax in mitochondrial outer membrane was co-immunoprecipitated with VDAC. Our results demonstrated that mitochondrial m-calpain plays a role in the release of tAIF from mitochondria by cleaving VDAC, and tAIF is released through VDAC-Bax pores.

Keywords: Abbreviations; AIF; apoptosis-inducing factor; tAIF; truncated AIF; VDAC; voltage-dependent anion channel; Grp75; glucose-regulated protein 75; AK2; adenylate kinase 2; PDH; pyruvate dehydrogenase; GAPDH; glyceraldehyde phosphate dehydrogenase; OM; outer membrane; IMS; intermembrane space; IM; inner membrane; DIDS; 4,4′-diisothiocyanostilbene-2,2′-disulfonic acidCalpain; Mitochondria; Apoptosis; AIF; VDAC; Grp75

Differential regulation of human tyrosine hydroxylase isoforms 1 and 2 in situ: Isoform 2 is not phosphorylated at Ser35 by Sarah L. Gordon; Larisa Bobrovskaya; Peter R. Dunkley; Phillip W. Dickson (pp. 1860-1867).

The major human tyrosine hydroxylase isoforms (hTH1 and 2) differ in their ability to be phosphorylated in vitro. hTH1 is phosphorylated at Ser31 by extracellular signal-regulated kinase (ERK). This kinase is not capable of phosphorylating hTH2 at Ser35 (the residue that corresponds to Ser31 in hTH1). We have stably transfected SH-SY5Y cells with hTH1 or hTH2 to determine if hTH2 can be phosphorylated at Ser35 in situ. Forskolin increased the phosphorylation of Ser40 in hTH1 and Ser44 in hTH2. Muscarine increased the phosphorylation of both Ser19 and Ser40/44 in both hTH1 and hTH2. EGF increased the phosphorylation of Ser31 in hTH1. Phosphorylation of Ser35 in hTH2 was not detected under any of the conditions tested. Inhibition of ERK by UO126 decreased the phosphorylation of Ser31 and this lead to a 50% decrease in the basal level of phosphorylation of Ser40 in hTH1. The basal level of Ser44 phosphorylation in hTH2 was not altered by treatment with UO126. Therefore, phosphorylation of Ser31 contributes to the phosphorylation of Ser40 in hTH1 in situ; however, this effect is absent in hTH2. This represents a major difference between the two human TH isoforms, and has implications for the regulation of catecholamine synthesis in vivo.

Keywords: Abbreviations; TH; tyrosine hydroxylase; Ser; serine; hTH; human TH; BH; ₄; tetrahydrobiopterin; ERK; extracellular signal-regulated protein kinase; CaMKII; calcium/calmodulin-dependent protein kinase II; DMEM; Dulbecco's Modified Eagle MediumTyrosine hydroxylase; Human isoform; Phosphorylation; Ser31; SH-SY5Y cell

Adenosine A₁ receptors selectively target protein kinase C isoforms to the caveolin-rich plasma membrane in cardiac myocytes by Zhaogang Yang; Wei Sun; Keli Hu (pp. 1868-1875).

Adenosine is a naturally occurring nucleoside that has been shown to regulate a variety of functions in the cardiovascular system. However, the mechanisms in adenosine receptor signaling are not completely understood. Given that adenosine receptors have been linked to protein kinase C (PKC) in cardioprotection and caveolae is critical for receptor signaling, we sought to determine whether activation of adenosine A1 receptors induces selective translocation of PKC isoforms to the membrane from the cytosol and whether activated PKC is targeted to the caveolin-rich plasma membrane microdomains. The freshly isolated adult rat cardiac myocytes were used to examine PKC isoforms including PKCα, PKCβ, PKCɛ, PKCδ and PKCζ. Immunoblot analysis revealed that the immunoreactivity for PKCɛ or PKCδ but not for PKCα, PKCβ or PKCζ increased significantly in the membrane fractions from cells pretreated with the selective adenosine A1 receptor agonist 2-chloro-N(6)-cyclopentyladenosine(CCPA, 100 nM) when compared with non-stimulated cells. The effect of CCPA on PKCɛ or PKCδ translocation was blocked by adenosine A1 receptor antagonist 8-cyclopentyl-1,3-dipropylxanthine (DPCPX, 100 nM). When Western blot was performed from the caveolin-enriched plasma membrane fractions, the immunoreactivity for PKCɛ or PKCδ but not PKCα, PKCβ or PKCζ was enhanced significantly by CCPA. Furthermore, PKCɛ and PKCδ were detected in the anti-caveolin-3 immunoprecipitates but not in the samples without primary antibody. Immunofluorescence staining further indicates increased colocalization of PKCɛ or PKCδ with caveolin-3 at cell peripheral region and T-tubular-like structures in response to adenosine A1 receptor activation. In conclusion, we demonstrate that activation of adenosine A1 receptors promotes the selective translocation of PKCɛ and PKCδ to the caveolin-enriched plasma membrane microdomains in cardiac myocytes.

Keywords: Adenosine receptor; Protein kinase c; Caveolae; Caveolin-3; Cardiac myocyte

NOA36/ZNF330 is a conserved cystein-rich protein with proapoptotic activity in human cells by Ivan S. de Melo; Concepción Iglesias; Alicia Benítez-Rondán; Francisco Medina; Juan Pedro Martínez-Barberá; Jorge Bolívar (pp. 1876-1885).

Translocations of regulator proteins from or to the mitochondria are key events in apoptosis regulation. NOA36/ZNF330 is a highly evolutionary conserved protein with a characteristic cystein-rich domain. In this work we address its mitochondrial localization and we demonstrate that a blockage of endogenous NOA36/ZNF330 expression by small-interfering RNA (siRNA) reduced apoptotic response to etoposide (ETO), camptothecin (CPT) and staurosporine (STS) but not to CH11 anti-Fas antibody or tumour-necrosis-factor-related apoptosis-inducing ligand (TRAIL) in HeLa cells. In contrast, when ectopically expressed in the cytoplasm, NOA36/ZNF330 induces apoptotic cell death. We also found that the domain responsible for this proapoptotic activity is located its cystein-rich region. We propose that NOA36/ZNF330 is translocated from the mitochondria to the cytoplasm when apoptosis is induced and that it contributes to cytochrome c release.

Keywords: Apoptosis; NOA36; ZNF330; Etoposide; Camptothecin; Mitochondria

Calcium-dependent plasma membrane repair requires m- or μ-calpain, but not calpain-3, the proteasome, or caspases by Ronald L. Mellgren; Katsuya Miyake; Irina Kramerova; Melissa J. Spencer; Nathalie Bourg; Marc Bartoli; Isabelle Richard; Peter A. Greer; Paul L. McNeil (pp. 1886-1893).

Mechanically damaged plasma membrane undergoes rapid calcium-dependent resealing that appears to depend, at least in part, on calpain-mediated cortical cytoskeletal remodeling. Cells null for Capns1, the non-catalytic small subunit present in both m- and μ-calpains, do not undergo calcium-mediated resealing. However, it is not known which of these calpains is needed for repair, or whether other major cytosolic proteinases may participate. Utilizing isozyme-selective siRNAs to decrease expression of Capn1 or Capn2, catalytic subunits of μ- and m-calpains, respectively, in a mouse embryonic fibroblast cell line, we now show that substantial loss of both activities is required to compromise calcium-mediated survival after cell scrape-damage. Using skeletal myotubes derived from Capn3-null mice, we were unable to demonstrate loss of sarcolemma resealing after needle scratch or laser damage. Isolated muscle fibers from Capn3 knockout mice also efficiently repaired laser damage. Employing either a cell line expressing a temperature sensitive E1 ubiquitin ligase, or lactacystin, a specific proteasome inhibitor, it was not possible to demonstrate an effect of the proteasome on calcium-mediated survival after injury. Moreover, several cell-permeant caspase inhibitors were incapable of significantly decreasing survival or inhibiting membrane repair. Taken together with previous studies, the results show that m- or μ-calpain can facilitate repair of damaged plasma membrane. While there was no evidence for the involvement of calpain-3, the proteasome or caspases in early events of plasma membrane repair, our studies do not rule out their participation in downstream events that may link plasma membrane repair to adaptive remodeling after injury.

Keywords: Calpain; Proteasome; Caspase; Membrane repair

Resistin is stored in neutrophil granules being released upon challenge with inflammatory stimuli by Elisabeth A. Boström; Andrej Tarkowski; Maria Bokarewa (pp. 1894-1900).

We have recently shown that resistin is a key mediator of arthritis accumulating in the inflamed joints and exerting its pro-inflammatory properties independently of TNFα. Here we evaluate neutrophils as a cellular source of resistin. Human neutrophils were subjected to subcellular fractionation where the presence of resistin was assessed using western blot, ELISA, and mass spectrometry. Presence of resistin on the neutrophil surface was visualized by flow cytometry. More than 95% of the neutrophils in circulation and in synovial fluid express resistin on their surface. Stimulation of mature neutrophils with fMLF induced release of resistin into supernatants and increased expression of resistin on the surface. Resistin is mobilized simultaneously with lactoferrin, a protein found in specific granules, and with granule-stored CR3/CD11b. Subcellular fractionation of human neutrophils demonstrated the presence of resistin in azurophilic and in specific granules. Here we show that neutrophils have two pools of resistin, the major one exists in specific granules, and the second on their cell membrane. Release of resistin from the neutrophil granules probably serves the main source of resistin at the site of inflammation.

Keywords: Neutrophils; Resistin; Granules; Inflammation

TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways by Claudio Marcelo Fader; Diego Germán Sánchez; María Belén Mestre; María Isabel Colombo (pp. 1901-1916).

During reticulocyte maturation, some membrane proteins and organelles that are not required in the mature red cell are lost. Several of these proteins are released into the extracellular medium associated with the internal vesicles present in multivesicular bodies (MVBs). Likewise, organelles such as mitochondria and endoplasmic reticulum are wrapped into double membrane vacuoles (i.e., autophagosomes) and degraded via autophagy. Morphological, molecular, and biochemical studies have shown that autophagosomes fuse with MVBs forming the so-called amphisomes, a prelysosomal hybrid organelle. SNAREs are key molecules of the vesicle fusion machinery. TI-VAMP/VAMP7 and VAMP3/cellubrevin are two v-SNARE proteins involved in the endocytic and exocytic pathways. We have previously shown that in the human leukemic K562 cells, Rab11 decorates MVBs and it is necessary for fusion between autophagosomes with MVBs. In the present report, we present evidence indicating that VAMP3 is required for the fusion between MVBs with autophagosomes to generate the amphisome, allowing the maturation of the autophagosome, but it does not seem to be involved in the next step, i. e., fusion with the lysosome. On the other hand, we demonstrate that VAMP7 is necessary for this latter event, allowing the completion of the autophagic pathway. Furthermore, VAMP7 and ATPase NSF, a protein required for SNAREs disassembly, participate in the fusion between MVBs with the plasma membrane to release the internal vesicles (i.e., exosomes) into the extracellular medium.

Keywords: SNAREs; VAMP7; VAMP3; Multivesicular bodies; Autophagy; Autophagosome; Exosomes; LC3; Rab11; K562

Prostaglandin F_2α-F-prostanoid receptor regulates CXCL8 expression in endometrial adenocarcinoma cells via the calcium–calcineurin–NFAT pathway by Kurt J. Sales; David Maldonado-Pérez; Vivien Grant; Rob D. Catalano; Martin R. Wilson; Pamela Brown; Alistair R.W. Williams; Richard A. Anderson; E. Aubrey Thompson; Henry N. Jabbour (pp. 1917-1928).

Pro-inflammatory mediators, like prostaglandin (PG) and chemokines, promote tumourigenesis by enhancing cell proliferation, migration of immune cells and recruitment of blood vessels. Recently we showed elevated expression of the chemokine (C-X-C motif) receptor 2 (CXCR2) in endometrial adenocarcinomas localized to neutrophils and neoplastic epithelial and vascular cells. Furthermore we found that PGF_2α-F-prostanoid (FP) receptor regulates the expression of the CXCR2 ligand CXCL1, to promote neutrophil chemotaxis in endometrial adenocarcinomas. In the present study we identified another CXCR2 ligand, CXCL8 as a target for PGF_2α-FP receptor signalling which enhances epithelial cell proliferation in endometrial adenocarcinoma cells in vitro and in nude mice in vivo. We found that PGF_2α-FP receptor interaction induces CXCL8 expression in endometrial adenocarcinoma cells via the protein kinase C–calcium–calcineurin–NFAT signaling pathway. Promoter analysis revealed that CXCL8 transcriptional activation by PGF_2α signaling is mediated by cooperative interactions between the AP1 and NFAT binding sites. Furthermore, PGF_2α via the FP receptor induced the expression of the regulator of calcineurin 1 isoform 4 (RCAN1-4) via the calcineurin/NFAT pathway in a reciprocal manner to CXCL8. Using an adenovirus to overexpress RCAN1-4, we found that RCAN1-4 is a negative regulator of CXCL8 expression in endometrial adenocarcinoma cells. Taken together our data have elucidated the molecular and cellular mechanism whereby PGF_2α regulates CXCL8 expression via the FP receptor in endometrial adenocarcinomas and have highlighted RCAN1-4 as a negative regulator of CXCL8 expression which may be exploited therapeutically to inhibit CXCL8-mediated tumour development.

Keywords: PGF; _2α; FP receptor; Chemokine; Calcineurin; Prostaglandin; CXCL8

Corrigendum to “HSPB7 is a SC35 speckle resident small heat shock protein” [Biochim. Biophys. Acta 1793 (2009) 1343–1353] by Michel J. Vos; Bart Kanon; Harm H. Kampinga (pp. 1929-1930).

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BBA - Molecular Cell Research (v.1793, #12)