Torsion of Previously Normal Tube and Ovary in Children

Lr, Schultz; Wa, Newton; Hw, Clatworthy

doi:10.1056/nejm196302142680703

Cited by 50 publications

(19 citation statements)

References 12 publications

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“…Analysis of secreted proteins was performed by using antisera raised against HrpZ Psph or YopE, respectively. SIL), which allow measurement of protein binding to membranes (31). Because the lipid molecules are not covalently linked to the support and are separated by an ultrathin layer of water molecules, this material has characteristics reminiscent of the lipid bilayer of biological membranes (38).…”

Section: Resultsmentioning

confidence: 99%

“…In control experiments, PBS (pH 7.1) without liposomes was added to the bacteria to ensure that hrp gene induction was unaffected. Protein binding to silica beads coated with single lipid bilayers (TRANSIL, NIMBUS Biotechnology, Leipzig, Germany) was performed as described (31). Assays involved incubation of 5 l of TRANSIL beads and 1 M of purified recombinant protein for 1 h (room temperature; 10 mM Tris⅐HCl, pH 7.4, 150 mM NaCl, protein:lipid ratio 1:500͞1,000).…”

Section: Methodsmentioning

confidence: 99%

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HrpZPsph from the plant pathogen Pseudomonas syringae pv. phaseolicola binds to lipid bilayers and forms an ion-conducting pore invitro

Lee

Klüsener²,

Tsiamis³

et al. 2000

Proceedings of the National Academy of Sciences

120

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The hrp gene clusters of plant pathogenic bacteria control pathogenicity on their host plants and ability to elicit the hypersensitive reaction in resistant plants. Some hrp gene products constitute elements of the type III secretion system, by which effector proteins are exported and delivered into plant cells. Here, we show that the hrpZ gene product from the bean halo-blight pathogen, Pseudomonas syringae pv. phaseolicola (HrpZPsph), is secreted in an hrp-dependent manner in P. syringae pv. phaseolicola and exported by the type III secretion system in the mammalian pathogen Yersinia enterocolitica. HrpZPsph was found to associate stably with liposomes and synthetic bilayer membranes. Under symmetric ionic conditions, addition of 2 nM of purified recombinant HrpZ Psph to the cis compartment of planar lipid bilayers provoked an ion current with a large unitary conductivity of 207 pS. HrpZPsphrelated proteins from P. syringae pv. tomato or syringae triggered ion currents similar to those stimulated by HrpZPsph. The HrpZPsphmediated ion-conducting pore was permeable for cations but did not mediate fluxes of Cl ؊ . Such pore-forming activity may allow nutrient release and͞or delivery of virulence factors during bacterial colonization of host plants.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

HrpZPsph from the plant pathogen Pseudomonas syringae pv. phaseolicola binds to lipid bilayers and forms an ion-conducting pore invitro

Lee

Klüsener²,

Tsiamis³

et al. 2000

Proceedings of the National Academy of Sciences

120

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“…The plasmid pBB131NMT was a generous gift from Jeffrey Gordon (Washington University School of Medicine, St Louis, MO). The plasmid pET3dMRPHis has been described elsewhere (15). All oligonucleotides were synthesized by Microsynth (Balgach, Switzerland).…”

Section: Methodsmentioning

confidence: 99%

“…Colonies grown in the presence of 50 g͞ml ampicillin and 50 g͞ml kanamycin were tested for overexpression of recombinant protein after induction with IPTG. Large-scale cultures for protein production were grown from individual colonies and induced by IPTG as described (12,15). Cells were harvested, lysed, and the recombinant protein isolated by chromatography on Ni 2ϩ columns and phenylsepharose columns as described (15).…”

Section: Methodsmentioning

confidence: 99%

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Mapping the interface between calmodulin and MARCKS-related protein by fluorescence spectroscopy

Ulrich

Schmitz

Braun

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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MARCKS-related protein (MRP) isT he proteins of the myristoylated alanine-rich C kinase substrate (MARCKS) family are protein kinase C substrates that have been proposed to regulate the actin cytoskeleton (1). The family comprises two members: MARCKS itself is a ubiquitous 32-kDa protein, whereas MARCKS-related protein (MRP, also called MacMARCKS) is a 22-kDa protein expressed mainly in brain and reproductive tissues (2). MARCKS proteins share two conserved segments, namely the myristoylated N terminus and a central highly basic 24-to 25-residue-long segment, the effector domain, also called the ''phosphorylation site domain'' (1, 3). In vitro, MARCKS and MRP bind to calmodulin (CaM) with high affinity (K d Ϸ 5 nM) (4, 5). Although direct proof for an interaction between MARCKS proteins and CaM has so far not been obtained in cells, indirect evidence suggests that MARCKS proteins mediate crosstalk between the protein kinase C-and CaM-signal transduction pathways (for reviews, see refs. 6 and 7).Two segments in MARCKS proteins are of interest with respect to their interactions with CaM.(i) The Effector Domain. The structure of the effector domain of MARCKS proteins has been the subject of several reports. Fig. 1 shows the amino acid sequence of the effector domain of MRP. This segment is highly basic (12 residues of 24 are lysines or arginines), but it also contains most of the large hydrophobic residues present in the intact protein (four phenylalanines and two leucines of seven). Although sequence analysis has previously led to the conclusion that this segment forms an ␣-helix (1), circular dichroic studies with peptides (8) and proteins (5, 9) suggest an extended structure for this segment. In the absence of information on the tertiary structure of MARCKS proteins, three different topologies can be proposed for the effector domain. The effector domain could be completely buried in a hydrophobic core (model A), which is unlikely because of the high content of charged amino acid residues. The effector domain could be on the surface of MARCKS proteins and partially exposed to water (model B). This model fits the proposed amphipathic structure of the effector domain (basic͞hydrophobic residues). Finally, the effector domain could be completely exposed to water and either act as a hinge between the C-and N-terminal domains of MARCKS proteins (model C1) or form an exposed loop on the surface of the protein (model C2). The observation that MARCKS proteins are elongated molecules (5, 10) supports model C1. However, the presence of a proline at position 96 in the middle of the effector domain of MRP could potentially induce the formation of a kink or a turn (11), favoring model C2.(ii) The Myristoylated N Terminus. Covalent modification of proteins with lipids, such as myristoylation in the case of MARCKS proteins, allows the interactions of these proteins with membranes (12). Myristoylation could also mediate protein-protein interactions. However, most proteins modified with lipids interact with other proteins on the ...

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Torsion and Infarction of Cystic Ovaries in Children

Grossman¹,

Filtzer²,

Aliapoulios³

1974

Arch Pediatr Adolesc Med

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A 4-year-old patient had a torsion of a cystic ovary and Fallopian tube. The torsion of the ovarian cyst is discussed.Ovari an cysts or cystic altera¬ tions of the ovary are not un¬ usual lesions in the woman, increas¬ ing in incidence with age up to the menopause and declining thereafter. Ovarian cysts are said to be "respon¬ sible for most of the palpable low¬ er abdominal tumors in adolescent girls"1 and "some degree of cyst for¬ mation is a relatively common find¬ ing at operation in women who have had no apparent symptoms relative to cysts."2 Follicle maturation and cyst formation have been found to be ex¬ tensive in earliest infancy, although most of these cysts regress spontane¬ ously.' When these cysts do occur in this age group, they may present a major clinical problem not only be¬ cause of their increased likelihood to A 4-year-old healthy white girl came to the pediatrie outpatient department. She had a five-day history of intermittent ab¬ dominal pain, predominantly in the left lower quadrant. The pain extended into the right lower quadrant and seemed more intense in the early morning hours. Results of her physical examination were within normal limits. The abdomen was soft and nontender, and rectal examination showed no masses or tenderness. The patient was sent home.She returned the following morning with recurrent pain. At this time, she had an oral temperature of 37.6 C (99.7 F) and a white blood cell count (WBC) of 9,800/cu mm, with a normal differential cell count.There was tenderness and guarding in the right lower quadrant but no palpable ab¬ dominal masses. After admission to the hospital with a diagnosis of acute appendi¬ citis, her temperature rose to 39 C (102.2 F) and the WBC count rose to 11,800/cu mm.Her abdominal examination disclosed in¬ creased tenderness and guarding localized to the right lower quadrant. She was taken to the operating room and exploratory sur¬ gery was performed through a right lower Downloaded From: http://archpedi.jamanetwork.com/ by a University of Pennsylvania User on 06/18/2015

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Torsion of Previously Normal Tube and Ovary in Children

Cited by 50 publications

References 12 publications

HrpZPsph from the plant pathogen Pseudomonas syringae pv. phaseolicola binds to lipid bilayers and forms an ion-conducting pore invitro

HrpZPsph from the plant pathogen Pseudomonas syringae pv. phaseolicola binds to lipid bilayers and forms an ion-conducting pore invitro

Mapping the interface between calmodulin and MARCKS-related protein by fluorescence spectroscopy

Torsion and Infarction of Cystic Ovaries in Children

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