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12578 citation(s) found for "Ma, John".

Clinical implication of centrosome amplification in plasma cell neoplasm
Ahmann, Greg, Henderson, Kim, Santana-Dávila, Rafael , Greipp, Philip R., Lacy, Martha Q. , Dispenzieri, Angela , Kumar, Shaji , Rajkumar, S. Vincent , Lust, John A., Kyle, Robert A. , Zeldenrust, Steven R., Hayman, Suzanne R. , Fonseca, Rafaël , Chng, Wee Joo , Henderson, Kimberly J., Gertz, Morie A. , Rajkumar, S Vincent , Dispenzieri, Angela , Fonseca, Rafael

Blood | December 23, 2005 | Volume: 107 | Issue: 9 | Pages: 3669-3675

10.1182/blood-2005-09-3810 | PMID 16373658 Get It

The mechanisms underlying aneuploidy in multiple myeloma (MM) are unclear. Centrosome amplification has been implicated as the cause of chromosomal instability in a variety of tumors and is a potential mechanism causing aneuploidy in MM. Using immunofluorescent (IF) staining, centrosome amplification was detected in 67% of monoclonal gammopathies, including monoclonal gammopathy of undetermined significance (MGUS). We also investigated the gene expression of centrosome proteins. Overall, gene expression data correlated well with IF-detected centrosome amplification, allowing us to derive a gene expression-based centrosome index (CI) as a surrogate for centrosome amplification. Clinically, MM patients with high CI (> 4) are associated with poor prognostic genetic and clinical subtypes (chromosome 13 deletion, t(4; 14), t(14;16), and PCLI > 1%, P < .05) and are shown here to have short survival (11.1 months versus 39.1 months, P < .001). On multivariate regression, a high CI is an independent prognostic factor. Given that centrosome amplification is already observed in MGUS and probably integral to early chromosomal instability and myeloma genesis, and patients with more extensive centrosome amplification have shorter survival, the mechanisms leading to centrosome amplification should be investigated because these may offer new avenues for therapeutic intervention.
Rare Expression of KIT and Absence of KIT Mutations in High Grade Renal Cell Carcinoma
Sengupta, Shomik , Cheville, John C. , Corless, Christopher L. , Lohse, Christine M. , Heinrich, Michael C. , Kwon, Eugene D., Zincke, Horst, Blute, Michael L., Leibovich, Bradley C. , Heinrich, Michael C

Journal of Urology | December 22, 2005 | Volume: 175 | Issue: 1 | Pages: 53-56

10.1016/s0022-5347(05)00059-5 | PMID 16406868 Get It

Role of biomarkers in studies of presymptomatic Alzheimer's disease
Morris, John C. , Kimberly, A., Quaid, Kimberly A., Kantarci, Kejal , Kaye, Jeffrey , Reiman, Eric M. , Klunk, William E. , Siemers, Eric , Kimberly, A., Holtzman, David M. , Kantarci, Kejal , Morris, John C

Alzheimer's & Dementia | December 19, 2005 | Volume: 1 | Issue: 2 | Pages: 145-151

10.1016/j.jalz.2005.09.013 | PMID 19595847 Get It

BackgroundBiomarkers that have been developed largely for the study of patients with clinically diagnosed Alzheimer's disease (AD) can also be used in the study of cognitively normal individuals who may harbor underlying AD pathology.MethodsA meeting of invited experts on AD biomarkers was held on November 11 and 12, 2004 to review currently available data and to discuss unmet needs for biomarker research in presymptomatic AD.ResultsNeuroimaging biomarkers have been studied to some extent in subjects at risk for AD. These imaging techniques include volumetric magnetic resonance imaging and positron emission tomography using either fluorodeoxyglucose or newer ligands that bind directly to amyloid plaque. Similarly, biochemical measures from cerebrospinal fluid or other physiologic fluids are emerging as potentially useful tools. Such biomarkers may be used either as diagnostic tools or as indicators of disease severity when followed longitudinally. A clinical diagnosis of asymptomatic individuals using biomarkers and studies involving asymptomatic subjects may raise logistical and ethical concerns.ConclusionsThe technical development of biomarkers that are used for presymptomatic AD diagnosis and for longitudinally measuring disease severity is evolving rapidly. Ethical and privacy considerations must be made before such biomarkers can be applied routinely to asymptomatic populations.
Urocortin
Burnett, John C.

Circulation | December 5, 2005 | Volume: 112 | Issue: 23 | Pages: 3544-3546

10.1161/circulationaha.105.584441 | PMID 16330694 Get It

Sensitive Spectrophotometric Assay for Plasma Oxalate
Ladwig, Paula M. , Liedtke, Robert R., Larson, Timothy S., Lieske, John C.

Clinical Chemistry | November 24, 2005 | Volume: 51 | Issue: 12 | Pages: 2377-2380

10.1373/clinchem.2005.054353 | PMID 16306102 Get It

Restriction of Feline Immunodeficiency Virus by Ref1, Lv1, and Primate TRIM5α Proteins
Saenz, Dyana T. , Teo, Wulin , Olsen, John C., Poeschla, Eric M.

Journal of Virology | November 23, 2005 | Volume: 79 | Issue: 24 | Pages: 15175-15188

10.1128/jvi.79.24.15175-15188.2005 | PMID 16306589 Get It

ABSTRACT The Ref1 and Lv1 postentry restrictions in human and monkey cells have been analyzed for lentiviruses in the primate and ungulate groups, but no data exist for the third (feline) group. We compared feline immunodeficiency virus (FIV) to other restricted (human immunodeficiency virus type 1 [HIV-1], equine infectious anemia virus [EIAV]) and unrestricted (NB-tropic murine leukemia virus [NB-MLV]) retroviruses across wide ranges of viral inputs in cells from multiple primate and nonprimate species. We also characterized restrictions conferred to permissive feline and canine cells engineered to express rhesus and human TRIM5α proteins and performed RNA interference (RNAi) against endogenous TRIM5α. We find that expression of rhesus or human TRIM5α proteins in feline cells restricts FIV, impairing pseudotyped vector transduction and viral replication, but rhesus TRIM5α is more restricting than human TRIM5α. Notably, however, canine cells did not support restriction by human TRIM5α and supported minimal restriction by rhesus TRIM5α, suggesting that these proteins may not function autonomously or that a canine factor interferes. Stable RNAi knockdown of endogenous rhesus TRIM5α resulted in marked increases in FIV and HIV-1 infectivities while having no effect on NB-MLV. A panel of nonprimate cell lines varied widely in susceptibility to lentiviral vector transduction, but normalized FIV and HIV-1 vectors varied concordantly. In contrast, in human and monkey cells, relative restriction of FIV compared to HIV-1 varied from none to substantial, with the greatest relative infectivity deficit for FIV vectors observed in human T-cell lines. Endogenous and introduced TRIM5α restrictions of FIV could be titrated by coinfections with FIV, HIV-1, or EIAV virus-like particles. Arsenic trioxide had complex and TRIM5α-independent enhancing effects on lentiviral but not NB-MLV infection. Implications for human gene therapy are discussed.
Quantitative mass spectral evidence for the absence of circulating brain natriuretic peptide (BNP-32) in severe human heart failure
Hawkridge, Adam M. , Heublein, Denise M., Bergen, H. Robert, Cataliotti, Alessandro , Burnett, John C. , Muddiman, David C.

Proceedings of the National Academy of Sciences | November 17, 2005 | Volume: 102 | Issue: 48 | Pages: 17442-17447

10.1073/pnas.0508782102 | PMID 16293687 Get It

C-terminal brain (B-type) natriuretic peptide (BNP)-32 is a widely used clinical biomarker for the diagnosis, prognosis, and treatment of heart failure (HF). The 32-aa peptide is synthesized primarily in the atrial and ventricular myocardium and constitutes the mature biologically active form of immature BNP (pro-BNP). There has been mounting evidence that suggests BNP circulates in different structural forms that impact HF diagnosis and in vivo activity. Herein, we have developed and used an immunoaffinity purification assay to isolate endogenous BNP-32 from New York Heart Association class IV patient plasma for subsequent analysis by nano-liquid chromatography (LC) electrospray ionization Fourier transform ion cyclotron resonance (FT-ICR) MS. We have introduced stable isotope-labeled BNP-32 to the assayed plasma to enable quantification of endogenous levels of BNP-32. Unlike the chemically nonspecific point-of-care tests (POCTs) and RIAs used worldwide to quantify BNP-32 from plasma, FT-ICR-MS (unprecedented mass measurement accuracy) coupled with LC (retention time) affords extraordinary molecular specificity, and when combined with the use of internal standards is able to confidently identify and quantify BNP-32. The significance of this work is despite exceedingly high circulating levels of BNP-32 in the New York Heart Association class IV patients as determined by POCTs (>290 fmol/ml) nano-LC-electrospray ionization-FT-ICR-MS data did not reveal any endogenous BNP-32. These results provide molecularly specific evidence for the absence of circulating BNP-32 in advanced-stage HF patients and suggest the existence of altered forms of BNP that are contributing to the POCT values.
SERCA Pump Inhibitors Do Not Correct Biosynthetic Arrest of ΔF508 CFTR in Cystic Fibrosis
Grubb, Barbara R. , Gabriel, Sherif E., Mengos, April, Gentzsch, Martina , Randell, Scott H. , Heeckeren, Anna M. van, Knowles, Michael R. , Drumm, Mitchell L. , Riordan, John R., Boucher, Richard C. , Boucher, Richard C

American Journal of Respiratory Cell and Molecular Biology | November 11, 2005 | Volume: 34 | Issue: 3 | Pages: 355-363

10.1165/rcmb.2005-0286oc | PMID 16284361 Get It

Abstract Deletion of phenylalanine 508 (ΔF508) accounts for nearly 70% of all mutations that occur in the cystic fibrosis transmembrane conductance regulator (CFTR). The ΔF508 mutation is a class II processing mutation that results in very little or no mature CFTR protein reaching the apical membrane and thus no cAMP-mediated Cl− conductance. Therapeutic strategies have been developed to enhance processing of the defective ΔF508 CFTR molecule so that a functional cAMP-regulated Cl− channel targets to the apical membrane. Sarcoplasmic/endoplasmic reticulum calcium (SERCA) inhibitors, curcumin and thapsigargin, have been reported to effectively correct the CF ion transport defects observed in the ΔF508 CF mice. We investigated the effect of these compounds in human airway epithelial cells to determine if they could induce ΔF508 CFTR maturation, and Cl− secretion. We also used Baby Hamster Kidney cells, heterologously expressing ΔF508 CFTR, to determine if SERCA inhibitors could interfere with the interaction between calnexin and CFTR and thereby correct the ΔF508 CFTR misfolding defect. Finally, at the whole animal level, we tested the ability of curcumin and thapsigargin to (1) induce Cl− secretion and reduce hyperabsorption of Na+ in the nasal epithelia of the ΔF508 mouse in vivo, and (2) induce Cl− secretion in intestine (jejunum and distal colon) and the gallbladder of the ΔF508 CF mouse. We conclude that curcumin and thapsigargin failed to induce maturation of ΔF508 CFTR, or induce Cl− secretion, as measured by biochemical and electrophysiologic techniques in a variety of model systems ranging from cultured cells to in vivo studies.
Deep Sylvian Fissure Chordoid Meningioma: Case Report
McIver, Jon I., Scheithauer, Bernd W., Atkinson, John L. D.

Neurosurgery | November 11, 2005 | Volume: 57 | Issue: 5 | Pages: E1064-E1064

10.1227/01.neu.0000180038.12168.ca | PMID 16284544 Get It

The family feud: turning off Sp1 by Sp1-like KLF proteins
Lomberk, Gwen , Urrutia, Raúl , Lomberk, Gwen L

Biochemical Journal | November 8, 2005 | Volume: 392 | Issue: 1 | Pages: 1-11

10.1042/bj20051234 | PMID 16266294 Get It

Sp1 is one of the best characterized transcriptional activators. The biological importance of Sp1 is underscored by the fact that several hundreds of genes are thought to be regulated by this protein. However, during the last 5 years, a more extended family of Sp1-like transcription factors has been identified and characterized by the presence of a conserved DNA-binding domain comprising three Krüppel-like zinc fingers. Each distinct family member differs in its ability to regulate transcription, and, as a consequence, to influence cellular processes. Specific activation and repression domains located within the N-terminal regions of these proteins are responsible for these differences by facilitating interactions with various co-activators and co-repressors. The present review primarily focuses on discussing the structural, biochemical and biological functions of the repressor members of this family of transcription factors. The existence of these transcriptional repressors provides a tightly regulated mechanism for silencing a large number of genes that are already known to be activated by Sp1.