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PubMed1997

Quantifying CPD.

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Education, Medical, Continuing↗
PubMed2005

Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells.

CPD-N is a cytokine-inducible CPD (carboxypeptidase-D) isoform identified in rat Nb2 T-lymphoma cells. The prototypic CPD (180 kDa) has three CP domains, whereas CPD-N (160 kDa) has an incomplete N-terminal domain I but intact domains II and III. CPD processes polypeptides in the TGN (trans-Golgi network) but the Nb2 CPD-N is nuclear. The present study identified a cryptic exon 1', downstream of exon 1 of the rat CPD gene, as an alternative transcription start site that encodes the N-terminus of CPD-N. Western-blot analysis showed exclusive synthesis of the 160 kDa CPD-N in rat Nb2 and Nb2-Sp lymphoma cells. Several haematopoietic cell lines including human K562 myeloma, Jurkat T-lymphoma and murine CTLL-2 cytotoxic T-cells express a 160 kDa CPD-immunoreactive protein, whereas mEL4 T-lymphoma cells express the 180 kDa CPD. The CPD-immunoreactive protein in hK562 cells is also nuclear and cytokine-inducible. In contrast, MCF-7 breast cancer cells express only the 180 kDa CPD, which is mainly in the TGN. CPD/CPD-N assays using substrate dansyl-L-alanyl-L-arginine show approx. 98% of CPD-N activity in the Nb2 nucleus, whereas MCF-7 CPD activity is enriched in the post-nuclear 10000 g pellet. The K(m) for CPD-N and CPD are 132+/-30 and 63+/-9 microM respectively. Specific activity/K(m) ratios show that dansyl-L-alanyl-L-arginine is a better substrate for CPD-N than for CPD. CPD-N has an optimal pH of 5.6 (due to domain II), whereas CPD has activity peaks at pH 5.6 (domain II) and pH 6.5-7.0 (domain I). CPD and CPD-N are inhibited non-competitively by zinc chelator 1,10-phenanthroline and competitively by peptidomimetic inhibitor DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid. The Nb2 CPD-N co-immunoprecipitated with phosphatase PP2A (protein phosphatase 2A) and alpha4 phosphoprotein. In summary, a cytokine-inducible CPD-N is selectively expressed in several haematopoietic tumour cells. Nuclear CPD-N is enzymatically active and interacts with known partners of CPD.

Animals↗
PubMed1982

Posttransfusion viability of rabbit erythrocytes preserved in a medium containing inosine, adenine, and isoosmotic sucrose.

A sucrose medium containing relatively great amounts of adenine and inosine (AIS-CPD) was more effective for maintaining adenosine triphosphate (ATP) and 2,3-diphosphoglyceric acid (DPG) levels of human erythrocytes for more than 35 days at 4 degrees C than control ACD-packed cells, sucrose medium (S-CPD), and sucrose medium containing a small amount of adenine. Then rabbit erythrocytes were used prior to in vivo test of human cells. (1) After storage for 5 weeks the ATP level (mumol/g Hb) was 3.25 in AIS-CPD, 2.65 in AISNa-CPD (AIS-CPD containing NACl plus sucrose instead of sucrose), 0.77 in S-CPD, and 0.42 in CPD (fresh: 5.39; n = 4-10). (2) The DPG level (mumol/g Hb) was AIS-CPD not equal to fresh greater than AISNa-CPD greater than S-CPD not equal to CPD. (3) The mean corpuscular volume decreased gradually in AIS-CPD. (4) The fragility of red cells decreased in AIS-CPD. (5) The posttransfusion viability measured by the 51Cr method after storage of erythrocytes for 5 weeks was 84.5% in AIS-CPD, 70.6% in AISNa-CPD, 59.5% in S-CPD, and 28.5% in CPD, 24 h after transfusion 14.9 in AIS-CPD, 9.9 in AISNa-CPD, 12.8 in S-CPD, and 8.4 in CPD (fresh: 14.0; n = 7-8).

Adenine↗
PubMedDate not supplied

Barriers to utilization of chronic peritoneal dialysis in network #1, New England.

OBJECTIVE: The percentage of prevalent end-stage renal disease (ESRD) patients maintained on chronic peritoneal dialysis (CPD) therapy in the United States declined from 15% in 1991 to 8.1% in 2002. Previous studies indicate that nephrologists in the United States feel 32.6% of prevalent ESRD patients should be on CPD therapy. The present study was designed to better understand the reasons for the discrepancy in actual versus desired prevalence of CPD utilization. METHODS: The medical directors of all dialysis centers in New England were mailed a questionnaire about the nephrologists' opinions concerning the percentage of patients that should be maintained on CPD therapy, reasons that limited patients' selection of CPD as initial therapy, and concerns about the current status of CPD therapy. The nephrologists were also invited to free text any other comments or concerns. RESULTS: A total of 117 questionnaires were sent; 59 (50.4%) were returned. These medical directors cared for a median of 10 (range 1 - 100) patients on CPD therapy, meaning 15% of dialysis patients in New England are maintained on CPD therapy. The medical directors felt that 29% (range 10% - 50%) of prevalent ESRD patients should be maintained on CPD therapy. The most common reasons cited by the nephrologists as barriers to CPD therapy included patient preference (54%), contraindications to performing CPD therapy (32%), poor social support (31%), significant comorbid disease (20%), late referrals and acute hospital starts (19%), problems with education re chronic kidney disease (12%), and problems with the structure and organization of CPD facilities (12%). These same medical directors stated that concerns about technique failure (25%), long-term viability of CPD therapy (25%), and mortality rates of CPD patients (17%) impacted on their use of CPD therapy as renal replacement therapy for patients with ESRD. CONCLUSION: Nephrologists in New England felt that 29% of prevalent ESRD patients should be maintained on CPD therapy, yet the actual incidence of CPD utilization in New England is 15%. A variety of factors were cited by the nephrologists as important reasons limiting CPD utilization. These nephrologists were also concerned about technique failure and long-term viability of CPD therapy. It is necessary that we look closely at each domain cited by the nephrologists if CPD therapy is to remain a viable option for patients with ESRD in the United States.

Humans↗
PubMed2001

Identification and nuclear localization of a novel prolactin and cytokine-responsive carboxypeptidase D.

A full-length, PRL-inducible complementary DNA (cDNA) encoding a novel, nuclear-targeted carboxypeptidase D isoform (designated CPD-N) was identified in the rat PRL-dependent Nb2-11C and PRL-independent Nb2-Sp lymphoma cell lines by differential display. The CPD-N cDNA (3751 bp) has 99% (3582/3583) homology with rat carboxypeptidase D (CPD; 4377 bp). In comparison to the rat CPD cDNA (ORF of 4134 bp; 180-kDa protein), CPD-N was shorter by approximately 600 bases but contained 148 unique bases at the 5'-end to give an ORF of 3399 bp. RT-PCR with primers specific to the 5'-end of CPD-N or to CPD showed that the CPD-N transcript was expressed in the Nb2-11C and Nb2-Sp cells but was not detected in rat brain or lung. Conversely, the CPD transcript was expressed in rat brain but was not detected in the two Nb2 cell lines. CPD-N expression (7.5-kb messenger RNA) was stimulated by PRL (10 ng/ml) and/or by interleukin-2 (24 U/ml) in Nb2-11C and Nb2-Sp cells. Most rat tissues expressed multiple CPD transcripts (7.5, 4.1, and 2 kb). Curiously, CPD transcripts were low or undetectable in male rat liver but readily detected in female liver, suggesting that sex-specific hormone levels may regulate its expression. Indeed, CPD expression in the PRL-responsive HepG2 hepatoma and MCF-7 breast cancer cell lines was low in control cells but was markedly stimulated by PRL after 3 h. Consistent with the shorter ORF of CPD-N, Western analysis detected proteins of smaller molecular sizes of 160 kDa (abundant) and 117 kDa (weak) in the Nb2-11C cells. The Nb2-Sp cells expressed a single and abundant 117-kDa protein, implicating differential protein processing in the two cell lines. Rat CPD has been reported to colocalize with the trans-Golgi network marker TGN38. Subcellular fractionation showed predominant nuclear localization of CPD-N and trace amounts were detected in the 100,000 x g microsomal fraction after PRL treatment (4 h); in contrast, TGN38 was found only in the microsomal fraction at this time. In cells treated with PRL for 24 h, immunofluorescent confocal microscopy showed nuclear and cytoplasmic distribution of CPD-N. Cytoplasmic CPD-N colocalized with TGN-38 whereas nuclear CPD-N had a mesh-like distribution and colocalized with nuclear lamin B.

Animals↗
PubMed2000

Contrast sensitivity and glare disability by halogen light after monofocal and multifocal lens implantation.

BACKGROUND: Standard examination of contrast sensitivity under conditions of glare disability is performed with incandescent light. A new halogen glare test that simulates glare as seen with oncoming vehicle headlights was used to measure glare disability in patients implanted with multifocal and monofocal intraocular lenses (IOLs). METHODS: 28 patients with an average age of 69 years (SD 12 years) were implanted with a monofocal IOL (SI-40NB, Allergan) and 28 patients with an average of 66 years (12 years) were implanted with a refractive multifocal IOL (Array-SA-40N, Allergan). All patients were followed for 5 months postoperatively. Contrast sensitivity at four spatial frequencies (3, 6, 12, and 18 cycles per degree, cpd) with and without a glare source were measured using the halogen glare test (CSV-1000 HGT). Statistical analysis was performed using the two sample Wilcoxon test. The local significance level was set at 0.05. RESULTS: When tested at the lowest spatial frequency (3 cpd) without halogen glare, contrast sensitivity was lower in the multifocal group than in the monofocal group (p=0.0292). With additional glare, there was no difference between both groups. At all other spatial frequencies (6, 12, and 18 cpd), when tested without halogen glare (6 cpd, p=0.5250; 12 cpd, p=0.8483; 18 cpd, p=0.9496) and with moderate (3 cpd, p=0.7993; 6 cpd, p=0.4639; 12 cpd, p=0.7456; 18 cpd, p=1.0) and high halogen glare (3 cpd, p=0. 1513; 6 cpd, p=0.2016; 12 cpd, p=0.3069; 18 cpd, p=0.9933), there was no statistically significant difference between groups. Patients in both groups of age 70 or older had reduced contrast sensitivity without halogen glare and with moderate and strong glare. When monofocal and multifocal patients older than 70 years of age were analysed separately, there was no statistically significant difference in contrast sensitivity with and without glare. Astigmatism >1 dioptre had no significant influence on contrast sensitivity and glare disability when monofocal and multifocal eyes were compared. CONCLUSION: Reduced contrast sensitivity was found in the multifocal group only at the lowest spatial frequency without halogen glare. The monofocal and multifocal groups had no statistically significant differences in contrast sensitivity with moderate and strong glare. These results suggest no difference in glare disability induced by halogen light similar to oncoming vehicle headlights for patients implanted with monofocal and multifocal IOLs.

Adult↗