PURPOSE: The dipeptidyl peptidase IV (DPPIV) gene family exhibits multiple functions and is involved in the pathogenesis of various diseases. It has attracted pharmaceutical interest in the areas of metabolic disorders as well as cancer. However, clinicopathologic significance of DPPIV family in colorectal cancer is not fully understood. MATERIALS AND METHODS: The clinical relevance of DPPIV and DPP10 expression was determined by immunohistochemical staining, and by assessing its clinicopathologic correlation in 383 colorectal cancer patients with known clinical outcomes. RESULTS: DPPIV was not expressed in normal colon mucosa, but it showed luminal expression in 52 of the 383 colorectal cancers (13.5%). DPPIV expression in tumors was associated with right-sided location of the colon (p=0.010) and more advanced tumor stage (p=0.045). DPP10 was expressed in normal colonic mucosa, but its expression varied in primary colorectal cancer tissues. Loss of DPP10 expression was found in 11 colorectal cancers (CRCs) (2.9%), and multivariate analysis showed that loss of DPP10 expression was an independent factor for poor patient prognosis (p=0.008). CONCLUSION: DPP10 may play a role in disease progression of colorectal cancer and loss of DPP10 expression in primary CRC is significantly associated with poor survival outcomes.
Colorectal Neoplasms/*metabolism/*pathology ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/*metabolism ; Disease Progression ; Female ; Humans ; Immunohistochemistry ; Male ; Prognosis ; Tumor Markers, Biological/*metabolism

BACKGROUNDAmyotrophic lateral sclerosis (ALS) is a progressive degenerative disease characterized by the loss of motor neurons in the spinal cord, brainstem, and cerebral cortex, which results in muscle weakness, atrophy. Sporadic ALS (SALS) accounts for about 90% of ALS cases, but the etiology is largely unknown. Most of the researchers consider it to be a complex disease. There have been several genome-wide association (GWA) studies reporting several single nucleotide polymorphisms (SNPs) which are susceptible to ALS, but no data of Asians (including Chinese) yet. We investigate whether the polymorphism of rs10260404 in DPP6 gene is associated with SALS in Chinese Han origin to compare the ethnic differences between Chinese Han origin and other populations.

METHODSThe genomic DNA was extracted from the leukocytes of whole blood samples in 58 Chinese Han patients with SALS and 52 healthy controls. The asymmetric PCR was processed in the presence of an unlabeled probe that contained the rs10260404 locus. The product was genotyped on a light scanner using high resolution melting method and some were confirmed with sequencing.

RESULTSThe rs10260404 polymorphism was in Hardy-Weinberg equilibrium in patients and controls. The CC genotype and the C allele were similar in patients compared with healthy subjects and not associated with an increased risk of Chinese SALS patients (chi(2) = 0.29, OR = 1.26, 95% CI 0.55 - 2.87, P > 0.05).

CONCLUSIONSThe rs10260404 is not associated with ALS susceptibility in Chinese people with Han origin which may be due to ethnic differences. More study with large number of cases in Chinese population is really necessary.

Adult ; Alleles ; Amyotrophic Lateral Sclerosis ; genetics ; Asian Continental Ancestry Group ; genetics ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases ; genetics ; Female ; Genotype ; Humans ; Male ; Middle Aged ; Nerve Tissue Proteins ; genetics ; Polymerase Chain Reaction ; Polymorphism, Genetic ; genetics ; Potassium Channels ; genetics ; Sequence Analysis, DNA ; Young Adult

OBJECTIVETo screen the molecular markers for refractory anemia with excess blasts in transformation (RAEB) in myelodysplastic syndromes (MDS) by serum proteome profiling.

METHODSThe serum protein were isolated from patients with RAEB, acute myeloid leukemia or normal subjects by 2-dimensional electrophoresis (2-DE), and the electrophoresis gels were obtained to identify the differentially reacting protein spots. The replica gels of the differentially reacting proteins were analyzed to locate the matching protein spots, which were identified by peptide mass fingerprint based on matrix-assisted laser desorption/ionization time of-flight mass spectrometry (MALDI-TOF-MS) and database searching.

RESULTSSeven differentially expressed proteins in RAEB were found by 2-DE. Of the 7 proteins, 4 were identified by MALDI-TOF-MS to have significantly differential expression in RAEB, including dipeptidyl peptidase (DPP/CD26), polymerase (DNA directed) kappa, PRO2044 and an albumin-like protein.

CONCLUSION2-DE-based serum proteome profiling helps identify serum proteomic biomarkers related to MDS. DDP/CD26 has increased expression in the serum in RAEB subtype MDS, suggesting its possible role in advanced MDS.

Anemia, Refractory, with Excess of Blasts ; blood ; genetics ; Bone Marrow ; pathology ; DNA-Directed DNA Polymerase ; blood ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases ; blood ; Female ; Humans ; Male ; Middle Aged ; Myelodysplastic Syndromes ; blood ; classification ; genetics ; Proteomics

No abstract available.
Meningitis ; Peptidyl-Dipeptidase A

Background: Hypertension is a worldwide epidemic that has been recognized as the most leading global risk for mortality, with its prevalence associated with increased blood pressure, concomitant risks of cardiovascular and kidney diseases, and major commonality in individuals advanced in age. With the current treatment options for hypertension management, there is still a need to develop therapies that directly target receptors that aid in hypertension treatment. Methodology: The study focused on the in-silico profiling of the reported compounds from Areca catechu L. (fam. Arecaceae) towards the n-domain and c-domain angiotensin converting enzyme (ACE) receptor models. Bioisosteric replacement was used to create bioisosteres investigated for similar binding affinity. Results: Some A. catechu compounds exhibited favorable binding energies towards the n- and c-domain receptor models of ACE, binding in the same ACE ligand binding site as lisinopril, benazepril, and sampatrilat via similar interactions and amino acid residues. The majority of A. catechu compounds with favorable ACE binding energies belong to the phytochemical classes of flavonoids, polyphenols and phenolics, glycosides, and steroids. After in silico toxicity and pharmacokinetic profiling, the bioisosteres Leuco-DM02-39, Leuco-DM02-66, Leuco-DM05-60, Querc-DM09-63, and Querc-DM14-31 with binding energies higher than their parent compounds and comparable to lisinopril, benazepril, and sampatrilat were deemed the best. Conclusion A. catechu compounds have the potential to target ACE n-domain and c-domain receptor models. Three leucocyanidin and two quercetin bioisosteres exhibited favorable binding to the n-domain and c-domain ACE receptor models and could be further optimized to derive a promising antihypertensive agent through ACE inhibition.
Peptidyl-Dipeptidase A ; Areca ; Hypertension

We describe a patient with hyponatremia induced by the use of angiotensin-converting enzyme (ACE) inhibitor; imidapril HCl. Although the mechanism of severe hyponatremia due to ACE inhibitor is not clear, it is conceivable that ACE inhibitor therapy may complicate the syndrome of inappropriate secretion of antidiuretic hormone and induce hyponatremia. In addition, the possibility should be considered that hyponatremia in our patient is a presumptive interaction between oxcarbazepine and imidapril HCl.
Angiotensins* ; Humans ; Hyponatremia* ; Peptidyl-Dipeptidase A*

No abstract available.
Angiotensins* ; Cough* ; Peptidyl-Dipeptidase A* ; Reflex*

No abstract available.
Angiotensins* ; Diabetes Mellitus* ; Peptidyl-Dipeptidase A* ; Renal Insufficiency*

No abstract available.
Angiotensins* ; Humans ; Lung Neoplasms* ; Lung* ; Peptidyl-Dipeptidase A*

Atrial Fibrillation ; pathology ; Humans ; Peptidyl-Dipeptidase A