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INTRODUCTION856casesofseveretrachomaweretreatedfromMay1984byfreez-ingcombinedwithdrugs,theeffectsweresatisfying.MATERIALSANDMETHODSMaterials856patientswithtrachomatreatedfromMay1984toFebruary2001wereinvestigatedincluding368malesand488femalesaged6-53(mean:21.3)yearswiththoseat10-20yearsconsistingthemost.Accordingto1979secondnationalophthalmologyconferencediagnosisstandards,189caseswerediagnosedasI;504caseswerediagnosedasI;1…  相似文献   

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Partial D and weak D: can they be distinguished?   总被引:3,自引:0,他引:3  
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One popular strategy to improve the acceptance and efficacy of oral liquid supplements in long-term care is dispensing them during the medication pass, although few studies support its effectiveness. This study evaluated the impact of a supplement medication pass program on energy and nutrient consumption and weight in nursing home residents. Findings indicate that residents maintained their prestudy weight and had a 29% decrease in supplement energy intake, a 19% increase in food energy intake, and a 17% decrease in net energy intake (supplement plus food). Supplement and food protein intake remained stable. Over longer periods, this reduced energy consumption could lead to weight loss, so routine monitoring and periodic evaluations of resident intake (both food and supplement) are recommended to ensure residents are receiving and consuming adequate amounts of daily energy and nutrients.  相似文献   

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Objective. Measurement of urinary free tetrahydrocortisol and tetrahydrocortisone ratio (allo‐THF+THF)/THE is clinically important in the diagnosis of hypertension caused by congenital absence of 11β‐hydroxysteroid dehydrogenase type 2 (apparent mineralocorticoid excess, AME) or inhibition of the enzyme after licorice ingestion. Although gas chromatography‐mass spectrometry (GC‐MS) provides reliable results, it requires derivatization and is lengthy and time‐consuming. The purpose of this study was to demonstrate that detection by liquid chromatography‐mass spectrometry (LC‐MS) is a potentially superior method. Material and methods. The analysis utilizes 1 mL urine. The samples were extracted with solid‐phase extraction (SPE) using ethyl acetate as eluent. The extract was evaporated to dryness, and allo‐tetrahydrocortisol (allo‐THF), THF and THE concentrations were analyzed by LC‐MS/MS operating in the negative mode after separation on a reversed‐phase column. The calibration curves exhibited consistent linearity and reproducibility in the range of 7.5–120 nmol/L. Interassay CVs were 7.0–10 % at mean ratios of (allo‐THF+THF)/THE of 0.54–1.9. The detection limit of the analytes was 0.4–0.8 nmol/L (signal‐to‐noise ratio = 3). The mean recovery of the three analytes ranged from 88 to 95 %. The regression equation for the free ratio using the LC‐MS/MS (x) method and the total ratio using the GC‐MS (y) method was: y = 0.30x+0.91 (r = 0.61; n = 25). Conclusions. The sensitivity and specificity of the LC‐MS/MS method offer an advantage over GC‐MS by eliminating derivatization. The high costs of equipment are balanced by higher through‐put, owing also to shorter chromatographic run times.  相似文献   

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Background: Multiplex ligation‐dependent probe amplification (MLPA) has been used to detect deletions and mutations of the α‐globin gene for diagnosis of α‐thalassemia. MLPA reaction products are usually separated and analyzed by high‐voltage capillary gel electrophoresis (CGE). The goal of this study was to find and use a cost‐effective method to separate and analyze MLPA products. Methods: Blood samples were collected from China. DNA was extracted and amplified by PCR using fluorescently labeled primers. In this study, denaturing high‐performance liquid chromatography (DHPLC) was used to separate and analyze the reaction products. And the optimal separation conditions were determined using nondenaturing columntemperature. Results: The DHPLC conditions were optimized and have been applied to separate MLPA products and 27 of the MLPA products from 50 to 320 bp were well separated. DHPLC was able to separate up to 37 reaction products that differed by 4–12 base pairs and detected target gene deletions by differences in peak size. Compared with CGE, both the specificity and sensitivity of DHPLC for the 107 DNA samples were 100%. Conclusions: DHPLC could be used to test routinely for α‐globin gene mutations and deletions. Combined with MLPA, DHPLC is a low‐cost, simple to use, accurate technique with practical value. J. Clin. Lab. Anal. 25:426–431, 2011. © 2011 Wiley Periodicals, Inc.  相似文献   

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马维  张英泽 《中国临床康复》2002,6(20):3126-3127,I004
Objective By hybridization in situ and biomechanical approach of platelet-derived growth fator mRNA(PDGFmRNA) and insulin-like growth factor mRNA(IGFmRNA), we discussed the influence of the platelet conentrated liquid on the healing of rabbit ulna fracture.Method We selected 24 New Zealand rabbits,divided them into 4 groups randomly (blank group,serum-control group,group with platelet concentrated liquid and group with bone graft and platelet concentrated liquid), and then made the fracture model on the middle of ulna which was fixed by finger armor plate.Before the operation, we drew out 6 ml blood from femoral artery, performed anti-coagulation with the Sodium Citrate and centrifugated by low and the followed high speed. We purified the white blood plate and injected it into the fracture position. The rabbits were killed at 1st,2nd,5th and 6th week.Qualitative analysis by hybridization in situ of PDGFmRNA and IGFmRNA and biomechanical measurement on the yth week sample were made. Result Bone callus could be seen on the radius spectimen in various degrees when the rabbits were killed at 1st. 2nd, 4th and 6th week, particularly in the last week. The average maximum destructive load on the fracture tip is higher to the control, and there is significant difference (P&;lt;0.01). Conclusion The local application of platelet concentration on the fracture tip can accelerate its healing.  相似文献   

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Class D β-lactamase-mediated resistance to β-lactams has been increasingly reported during the last decade. Those enzymes also known as oxacillinases or OXAs are widely distributed among Gram negatives. Genes encoding class D β-lactamases are known to be intrinsic in many Gram-negative rods, including Acinetobacter baumannii and Pseudomonas aeruginosa, but play a minor role in natural resistance phenotypes. The OXAs (ca. 150 variants reported so far) are characterized by an important genetic diversity and a great heterogeneity in terms of β-lactam hydrolysis spectrum. The acquired OXAs possess either a narrow spectrum or an expanded spectrum of hydrolysis, including carbapenems in several instances. Acquired class D β-lactamase genes are mostly associated to class 1 integron or to insertion sequences.Class D β-lactamases, also known as oxacillinases or OXA-type β-lactamases (OXAs), are active-serine-site enzymes like Ambler class A and class C β-lactamases, differing from class A and C enzymes in amino acid structure, whereas class B β-lactamases are metalloenzymes with a Zn2+ ion(s) in the active site (4, 71, 78). Even though class D includes mostly enzymes with higher hydrolysis rates for cloxacillin and oxacillin than for benzylpenicillin (hence the name oxacillinases), not all class D β-lactamases have this characteristic. Most of the class D enzymes belong to group 2d of the Bush functional classification scheme for β-lactamases (23). Among the four β-lactamase molecular classes, class D β-lactamases are the most diverse enzymes (107). This diversity is observed at both the genetic and biochemical levels, with enzymes possessing either a narrow or expanded spectrum of hydrolysis. In addition, several class D β-lactamases have an expanded spectrum of activity resulting from point mutations.Although many class D β-lactamase genes are embedded into class 1 integrons, recent reports indicated that other specific genetic structures, including insertion sequences and transposons, may be associated with class D β-lactamase genes. Numerous class D β-lactamase genes have been identified as a source of acquired resistance in gram-negative bacteria, but recent studies have shown that class D β-lactamases are also naturally produced in clinically significant pathogens and environmental species (107).This review focuses on the diversity and substrate profiles of class D β-lactamases, their sources, and the genetics of acquisition of the corresponding genes. All the class D β-lactamases for which a sequence is available in the GenBank databases are listed in Table Table11.

TABLE 1.

Features of oxacillinases
NameaAlternate nameOXA groupTypeOriginal hostA or NbAssociated mobile element
Gene GC content (%)Isoelectric pointd
GenBank accession no.eReferencef
Transposon or insertion sequenceIntegroncExptlTheoretical
OXA-1OXA-30Narrow spectrumE. coliATn2603+34.47.47.7J02967113
OXA-2OXA-2Narrow spectrumS. TyphimuriumA+507.79.1X0726097
OXA-3OXA-2Narrow spectrumK. pneumoniaeATn1411+507.18.1L07945142
OXA-4OXA-35Narrow spectrumE. coliATn1409+7.5AY162283142
OXA-5Narrow spectrumP. aeruginosaATn1406+40.27.68.4X5827232
OXA-6Narrow spectrumP. aeruginosaA7.7UP
OXA-7OXA-10Narrow spectrumE. coliA+40.67.79.3X75562145
OXA-8
OXA-9Narrow spectrumK. pneumoniaeATn1331+49.56.97.1M55547155
LCR-1Narrow spectrumP. aeruginosaATn1412526.57.1X5680932
OXA-10Narrow spectrumP. aeruginosaATn1404+42.16.17.0U3710570
OXA-11OXA-10ES-OXAP. aeruginosaA+426.46.3Z2259060
OXA-12Narrow spectrumA. jandaeiN62.38.68.4U10251139
AmpSNarrow spectrumA. hydrophilaN637.97.1X80276165
OXA-13OXA-10Narrow spectrumP. aeruginosaA+41.28.08.7U5918399
OXA-14OXA-10ES-OXAP. aeruginosaA+42.16.26.3L3852338
OXA-15OXA-2ES-OXAP. aeruginosaA+508.79.3U6383536
OXA-16OXA-10ES-OXAP. aeruginosaA+42.16.26.3AF04310039
OXA-17OXA-10ES-OXAP. aeruginosaA+42.16.17.0AF06020637
OXA-18ES-OXAP. aeruginosaAISCR1961.25.55.9U85514118
OXA-19OXA-13ES-OXAP. aeruginosaA+41.27.68.4AF04338198
OXA-20Narrow spectrumP. aeruginosaA+45.17.49.0AF024602108
OXA-21OXA-3Narrow spectrumA. baumanniiA+50.17.08.1Y10693162
OXA-22Narrow spectrumR. pickettiiN65.57.06.4AF064820112
OXA-23CHDLA. baumanniiATn2006/Tn2007386.77.0AJ13210542
OXA-24OXA-40CHDLA. baumanniiA34.48.69.0AJ23912919
OXA-25OXA-40CHDLA. baumanniiA34.48.08.5AF2018261
OXA-26OXA-40CHDLA. baumanniiA34.47.99.0AF2018271
OXA-27OXA-23CHDLA. baumanniiA386.88.0AF2018281
OXA-28OXA-13ES-OXAP. aeruginosaA+41.28.18.7AF231133125
OXA-29Narrow spectrumL. gormaniiN36.69.09.4AJ40061949
OXA-30OXA-1Narrow spectrumE. coliA+34.47.36.8AF255921148
OXA-31OXA-1ES-OXAP. aeruginosaA+34.47.56.8AF2946539
OXA-32OXA-2ES-OXAP. aeruginosaA+507.79.0AF315351124
OXA-33OXA-40CHDLA. baumanniiA34.48.69.0AY008291
OXA-34OXA-2ES-OXAP. aeruginosaA+508.9AF350424UP
OXA-35OXA-10ES-OXAP. aeruginosaA+41.28.08.7AF3157868
OXA-36OXA-2ES-OXAP. aeruginosaA+49.49.2AF300985UP
OXA-37OXA-20Narrow spectrumA. baumanniiA+44.87.48.9AY007784109
OXA-38
OXA-39
OXA-40CHDLA. baumanniiA34.48.69.0AF50924165
OXA-41
OXA-42Narrow spectrumB. pseudomalleiN66.39.29.3AJ488302111
OXA-43Narrow spectrumB. pseudomalleiN65.99.29.3AJ488303111
OXA-44
OXA-45ES-OXAP. aeruginosaAISCR561.88.89.4AJ519683153
OXA-46Narrow spectrumP. aeruginosaA+47.17.88.7AF31751157
OXA-47OXA-1Narrow spectrumK. pneumoniaeA+34.17.46.8AY237830127
OXA-48CHDLK. pneumoniaeATn199944.57.28.0AY236073127
OXA-49OXA-23CHDLA. baumanniiA386.0AY288523UP
OXA-50Narrow spectrumP. aeruginosaN64.88.69.0AY30613054
OXA-51OXA-Ab1CHDLA. baumanniiA39.37.08.0AJ30973422
OXA-52
OXA-53OXA-2ES-OXAS. AgonaA+50.26.97.2AY289608103
OXA-54CHDLS. oneidensisN46.66.86.7AY500137126
OXA-55CHDLS. algaeN53.88.68.6AY34349368
OXA-56Narrow spectrumP. aeruginosaA+40.76.58.7AY44508025
OXA-57Narrow spectrumB. pseudomalleiN669.3AJ63196673
OXA-58CHDLA. baumanniiA37.47.27.2AY665723130
OXA-59Narrow spectrumB. pseudomalleiN65.99.3AJ63224973
OXA-60Narrow spectrumR. pickettiiN64.95.15.4AF52530355
OXA-61Narrow spectrumC. jejuniN27.49.1AY5879562
OXA-62CHDLP. pnomenusaN65.3>9.09.5AY423074144
OXA-63Narrow spectrumB. pilosicoliN24.96.0AY61900394
OXA-64OXA-Ab2OXA-51CHDLA. baumanniiN39.68.0AY75090721
OXA-65OXA-Ab3OXA-51CHDLA. baumanniiN39.28.8AY75090821
OXA-66OXA-Ab4OXA-51CHDLA. baumanniiN39.49.0AY75090921
OXA-67OXA-Ab5OXA-51CHDLA. baumanniiN398.0DQ491200UP
OXA-68OXA-Ab6OXA-51CHDLA. baumanniiN397.1AY75091021
OXA-69OXA-Ab7OXA-51CHDLA. baumanniiN39.38.48.6AY75091166
OXA-70OXA-Ab8OXA-51CHDLA. baumanniiN39.39.0AY75091221
OXA-71OXA-Ab9OXA-51CHDLA. baumanniiN39.78.0AY75091321
OXA-72OXA-40CHDLA. baumanniiA36.48.8EF534256166
OXA-73OXA-23CHDLK. pneumoniaeA37.68.0AY762325UP
OXA-74OXA-10UnknownP. aeruginosaA41.96.57.0AJ85418246
OXA-75OXA-Ab10OXA-51CHDLA. baumanniiN38.78.6AY85952966
OXA-76OXA-Ab11OXA-51CHDLA. baumanniiN39.39.2AY94920366
OXA-77OXA-Ab12OXA-51CHDLA. baumanniiN39.28.6AY94920266
OXA-78OXA-Ab13OXA-51CHDLA. baumanniiN39.28.9AY862132UP
OXA-79OXA-Ab14OXA-51CHDLA. baumanniiN39.59.0EU01953447
OXA-80OXA-Ab15OXA-51CHDLA. baumanniiN39.39.0EU01953547
OXA-81
OXA-82OXA-Ab16OXA-51CHDLA. baumanniiN39.49.0EU019536158
OXA-83OXA-Ab17OXA-51CHDLA. baumanniiN39.59.0DQ309277158
OXA-84OXA-Ab18OXA-51CHDLA. baumanniiN39.49.0DQ309276158
OXA-85Narrow spectrumF. nucleatumN24.65.36.1AY227054164
OXA-86OXA-Ab19OXA-51CHDLA. baumanniiN38.88.0DQ149247159
OXA-87OXA-Ab20OXA-51CHDLA. baumanniiN38.98.0DQ348075159
OXA-88OXA-Ab21OXA-51CHDLA. baumanniiN39.29.2DQ39296375
OXA-89OXA-Ab22OXA-51CHDLA. baumanniiN38.47.08.6DQ44568394
OXA-90OXA-Ab23OXA-51CHDLA. baumanniiN39.28.6EU433382UP
OXA-91OXA-Ab24OXA-51CHDLA. baumanniiN398.0DQ51908375
OXA-92OXA-Ab25OXA-51CHDLA. baumanniiN39.38.6DQ335566156
OXA-93OXA-Ab26OXA-51CHDLA. baumanniiN39.38.0DQ51908775
OXA-94OXA-Ab27OXA-51CHDLA. baumanniiN39.38.9DQ51908875
OXA-95OXA-Ab28OXA-51CHDLA. baumanniiN39.58.6DQ51908975
OXA-96OXA-58CHDLA. baumanniiA37.57.2DQ51909075
OXA-97OXA-58CHDLA. baumanniiA37.87.2EF102240129
OXA-98OXA-Ab29OXA-51CHDLA. baumanniiN39.28.6AM279652UP
OXA-99OXA-Ab30OXA-51CHDLA. baumanniiN39.48.0DQ888718UP
OXA-100
OXA-101OXA-10UnknownC. freundiiA+40.78.8AM412777UP
OXA-102OXA-23CHDLA. radioresistensN385.8Unknown123
OXA-103OXA-23CHDLA. radioresistensN385.8Unknown123
OXA-104OXA-Ab31OXA-51CHDLA. baumanniiN39.38.6EF58128547
OXA-105OXA-23CHDLA. radioresistensN387.0UnknownUP
OXA-106OXA-Ab32OXA-51CHDLA. baumanniiN39.38.9EF65003247
OXA-107OXA-Ab33OXA-51CHDLA. baumanniiN39.38.6EF65003347
OXA-108OXA-Ab34OXA-51CHDLA. baumanniiN398.5EF65003447
OXA-109OXA-Ab35OXA-51CHDLA. baumanniiN39.39.0EF65003547
OXA-110OXA-Ab36OXA-51CHDLA. baumanniiN39.38.6EF65003647
OXA-111OXA-Ab37OXA-51CHDLA. baumanniiN39.47.1EF65003747
OXA-112OXA-Ab38OXA-51CHDLA. baumanniiN39.48.6EF65003847
OXA-113OXA-Ab39OXA-51CHDLA. baumanniiN39.38.0EF653400106
OXA-114Narrow spectrumA. xylosoxidansN70.48.69.0EU18884241
OXA-115OXA-Ab40OXA-51CHDLA. baumanniiN39.39.0EU029998UP
OXA-116OXA-Ab41OXA-51A. baumanniiN39.38.6EU220744UP
OXA-117OXA-Ab42OXA-51A. baumanniiN39.28.6EU220745UP
OXA-118Narrow spectrumB. cepaciaA+49.37.3AF37196433
OXA-119Narrow spectrumUncultured bacteriumA+49.46.7AY139598150
OXA-120
OXA-121
OXA-122
OXA-123
OXA-124
OXA-125
OXA-126
OXA-127
OXA-128OXA-10CHDLA. baumanniiN+39.18.0EU37551552a
OXA-129OXA-Ab43OXA-5UnknownS. BredeneyA+39.99.1AM93266995
OXA-130OXA-Ab44OXA-51A. baumanniiN39.18.5EU547445UP
OXA-131OXA-Ab45OXA-51A. baumanniiN39.49.0EU547446UP
OXA-132OXA-Ab46OXA-51A. baumanniiN39.38.0EU547447UP
OXA-133OXA-23CHDLA. radioresistensN39.36.1EU571228123
OXA-134CHDLA. lwoffiiN46.25.3UP
OXA-135
OXA-136OXA-63Narrow spectrumB. pilosicoliN25.15.3EU08683096
OXA-137OXA-63Narrow spectrumB. pilosicoliN24.95.7EU08683496
OXA-138
OXA-139
OXA-140
OXA-141OXA-2ES-OXAP. aeruginosaA+49.99.1EF552405UP
OXA-142OXA-10ES-OXAP. aeruginosaA+426.3EU358785UP
OXA-143CHDLA. baumanniiA34.48.7UP
OXA-144
OXA-145OXA-10ES-OXAP. aeruginosaA+41.18.7FJ790516UP
OXA-146
OXA-147OXA-10ES-OXAP. aeruginosaA418.1FJ848783UP
Open in a separate windowaThe nomenclature is in accordance with that provided by G. Jacoby on the Lahey website (http://www.lahey.org/Studies/other.asp#table1). Lacking variants (in boldface) are those for which a number has been assigned on this website but for which no information is yet available.bA, acquired; N, natural.c+, the oxacillinase gene was found to be associated with an integron-borne gene cassette; −, the gene is not associated with an integron-borne gene cassette.dExperimentally obtained pI values (when available) versus calculated values. Theoretical values were calculated using software found at the ExPASy proteomics tools website (http://www.expasy.ch/tools/) and the amino acid sequences of the mature proteins only. Peptide cleavage site identification was performed with SignalP (http://www.cbs.dtu.dk/services/SignalP/), and pI computing was performed with the Compute pI/Mw tool (http://www.expasy.ch/tools/pi_tool.html).eUP, unpublished.  相似文献   

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Tenofovir disoproxil fumarate (TDF) causes bone, endocrine, and renal changes by an unknown mechanism(s). Data are limited on tenofovir pharmacokinetics and these effects. Using baseline data from a multicenter study of HIV-infected youth on stable treatment with regimens containing TDF (n = 118) or lacking TDF (n = 85), we measured cross-sectional associations of TDF use with markers of renal function, vitamin D-calcium-parathyroid hormone balance, phosphate metabolism (tubular reabsorption of phosphate and fibroblast growth factor 23 [FGF23]), and bone turnover. Pharmacokinetic-pharmacodynamic associations with plasma tenofovir and intracellular tenofovir diphosphate concentrations were explored among those receiving TDF. The mean age was 20.9 (standard deviation [SD], 2.0) years; 63% were male; and 52% were African American. Compared to the no-TDF group, the TDF group showed lower mean estimated glomerular filtration rates and tubular reabsorption of phosphate, as well as higher parathyroid hormone and 1,25-dihydroxy vitamin D [1,25-OH(2)D] levels. The highest quintile of plasma tenofovir concentrations was associated with higher vitamin D binding protein, lower free 1,25-OH(2)D, higher 25-OH vitamin D, and higher serum calcium. The highest quintile of intracellular tenofovir diphosphate concentration was associated with lower FGF23. Higher plasma tenofovir concentrations were associated with higher vitamin D binding protein and lower free 1,25-OH(2)D, suggesting a functional vitamin D deficiency explaining TDF-associated increased parathyroid hormone. The finding of lower FGF23 accompanying higher intracellular tenofovir diphosphate suggests that different mechanisms mediate TDF-associated changes in phosphate handling. Separate pharmacokinetic properties may be associated with distinct TDF toxicities: tenofovir with parathyroid hormone and altered calcium balance and tenofovir diphosphate with hypophosphatemia and FGF23 regulation.(The clinical trial registration number for this study is NCT00490412 and is available online at http://clinicaltrials.gov/ct2/show/NCT00490412.)  相似文献   

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BackgroundAntihypertensive and tissue-protective properties of vitamin D metabolites are increasingly attributed to the inhibition of renin synthesis by 1,25-dihydroxyvitamin D [1,25(OH)2D] in the kidney.MethodWe aimed to document a potential association between 25-hydroxyvitamin D [25(OH)D], 1,25(OH)2D and the circulating renin–angiotensin system (RAS) in a large cohort of patients referred (n = 3316) to coronary angiography.ResultsOf the 3316 subjects, 3296 (median age: 63.5 (56.3–70.6) years; 30.2% women) had a baseline measurement of 25(OH)D [median: 15.6(10.1–23.0) µg/L)], 1,25(OH)2D [median: 33.2(25.2–42.9) pg/mL], plasma renin concentration [PRC; median: 11.4(6.0–24.6) pg/mL] and angiotensin 2 [median: 20.0(12.0–35.0) ng/L]. Multivariate adjusted ANCOVA showed a steady increase of PRC values across declining deciles of 25(OH)D and 1,25(OH)2D values (P = 0.013 and P = 0.045), respectively. Additionally, mean angiotensin 2 values increased significantly across decreasing 25(OH)D and 1,25(OH)2D values (P = 0.020 and P = 0.024, respectively). In contrast, multivariate adjusted ANCOVA revealed no significant associations between aldosterone, aldosterone-to-renin ratio and 25(OH)D/1,25(OH)2D values. In multivariate stepwise regression analyses both, 25(OH)D and 1,25(OH)2D emerged as independent predictors of plasma renin and angiotensin 2 concentrations.ConclusionsOur data showed for the first time in humans that both, lower 25(OH)D and 1,25(OH)2D values are independently related to an upregulated circulating RAS.  相似文献   

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