Serum Carnosinase Activity in Plasma and Serum: Validation of a Method and Values in Cardiopulmonary Bypass Surgery

Schoen, Pieter; Everts, Hilco; Boer, Theo de; Oeveren, Wim van

doi:10.1373/clinchem.2003.019398

Cited by 19 publications

(20 citation statements)

References 18 publications

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“…Reduced levels of CNDP1 have been observed in patients with Parkinson disease or multiple sclerosis and in patients after a cerebrovascular accident [34]. Our analysis, for the first time, shows that serum CNDP1 is present at reduced levels in the plasma of GBM patients, which may be important in the maintenance of carnosine levels and bioavailability of carnosine as a drug for GBM [33].…”

Section: Resultsmentioning

confidence: 55%

“…Carnosine is also reported to have anti-growth property and has been discussed for its therapeutic potential against tumors including GBM [32]. Carnosinase, which hydrolyzes carnosine, exists in two distinct isoforms and has been discussed in the context of major neurodegenerative condition [33]. The serum isoform, CNDP1, is distinct and our identification is supported by the unique peptides for this form.…”

Section: Resultsmentioning

confidence: 58%

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Proteins with Altered Levels in Plasma from Glioblastoma Patients as Revealed by iTRAQ-Based Quantitative Proteomic Analysis

et al. 2012

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Glioblastomas (GBMs) are the most common and lethal primary tumors of the central nervous system with high level of recurrence despite aggressive therapy. Tumor-associated proteins/peptides may appear in the plasma of these patients as a result of disruption of the blood-brain barrier in them, raising the scope for development of plasma-based tests for diagnosis and monitoring the disease. With this objective, we analyzed the levels of proteins present in the plasma from GBM patients using an iTRAQ based LC-MS/MS approach. Analysis with pooled plasma specimens from the patient and healthy control samples revealed high confidence identification of 296 proteins, of which 61 exhibited a fold-change ≥1.5 in the patient group. Forty-eight of them contained signal sequence. A majority have been reported in the differentially expressed transcript or protein profile of GBM tissues; 6 have been previously studied as plasma biomarkers for GBM and 16 for other types of cancers. Altered levels of three representative proteins–ferritin light chain (FTL), S100A9, and carnosinase 1 (CNDP1)–were verified by ELISA in a test set of ten individual plasma specimens. FTL is an inflammation marker also implicated in cancer, S100A9 is an important member of the Ca2+ signaling cascade reported to be altered in GBM tissue, and CNDP1 has been reported for its role in the regulation of the levels of carnosine, implicated as a potential drug for GBM. These and other proteins in the dataset may form useful starting points for further clinical investigations for the development of plasma-based biomarker panels for GBM.

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Section: Resultsmentioning

confidence: 55%

Section: Resultsmentioning

confidence: 58%

Proteins with Altered Levels in Plasma from Glioblastoma Patients as Revealed by iTRAQ-Based Quantitative Proteomic Analysis

et al. 2012

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“…Subsequently, these antibodies were immobilized on beads to create a bead array (supplemental Table 1). An attempt to classify the set of antibody targets revealed proteins from different classes (29), such as transmembrane proteins (38), G-protein-coupled receptors (4), plasma proteins (8), cancer-related proteins (10), proteins with a signal peptide (30), enzymes (12), and transcription factors (5).…”

Section: Concept For Multiplex Analysis Of Plasma or Serum-mentioning

confidence: 99%

“…For CNDP1 discovered both at the 23 and 56°C retrieval temperatures, an interesting pattern was observed. For this protein, tissue and serum isoforms have been suggested (30), and it is predicted to be N 4 -glycosylated at two asparagines (Asn-322 and Asn-382). Although bands detected at Ϯ190 kDa probably refer to the glycosylated isoform, CNDP1 appeared to be present in similar amounts for all six samples.…”

Section: Concept For Multiplex Analysis Of Plasma or Serum-mentioning

confidence: 99%

Toward Next Generation Plasma Profiling via Heat-induced Epitope Retrieval and Array-based Assays

Schwenk

Igel

Neiman

et al. 2010

Molecular & Cellular Proteomics

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There is a need for high throughput methods for screening patient samples in the quest for potential biomarkers for diagnostics and patient care. Here, we used a combination of undirected target selection, antibody suspension bead arrays, and heat-induced epitope retrieval to allow for protein profiling of human plasma in a novel and systematic manner. Several antibodies were found to reveal altered protein profiles upon epitope retrieval at elevated temperatures with limits of detection improving into lower ng/ml ranges. In a study based on prostate cancer patients, several proteins with differential profiles were discovered and subsequently validated in an independent cohort. For one of the potential biomarkers, the human carnosine dipeptidase 1 protein (CNDP1), the differences were determined to be related to the glycosylation status of the targeted protein. The study shows a path of pursuit for large scale screening of biobank repositories in a flexible and proteome-wide fashion by utilizing heat-induced epitope retrieval and using an antibody suspension bead array format. Molecular & Cellular Proteomics 9: 2497-2507, 2010.

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“…It occurs in excitable tissues, such as skeletal muscle cells [15] and oligodendrocytes [16]. On the other hand, the cleavage of carnosine and homocarnosine is carried out by serum carnosinase [8], which is synthesized in brain and liver [17] and secreted into the cerebrospinal fluid (CSF) and blood [18]. Other dipeptidase able to cleave carnosine in biological tissues is the cytosol nonspecific dipeptidase (CNDP, EC 3.…”

Section: Carnosinementioning

confidence: 99%

Carnosine and Related Peptides: Therapeutic Potential in Age-Related Disorders

Cararo¹,

Streck²,

Schuck³

et al. 2015

Aging and disease

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Imidazole dipeptides (ID), such as carnosine (β-alanyl-L-histidine), are compounds widely distributed in excitable tissues of vertebrates. ID are also endowed of several biochemical properties in biological tissues, including antioxidant, bivalent metal ion chelating, proton buffering, and carbonyl scavenger activities. Furthermore, remarkable biological effects have been assigned to such compounds in age-related human disorders and in patients whose activity of serum carnosinase is deficient or undetectable. Nevertheless, the precise biological role of ID is still to be unraveled. In the present review we shall discuss some evidences from clinical and basic studies for the utilization of ID as a drug therapy for age-related human disorders.

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Serum Carnosinase Activity in Plasma and Serum: Validation of a Method and Values in Cardiopulmonary Bypass Surgery

Cited by 19 publications

References 18 publications

Proteins with Altered Levels in Plasma from Glioblastoma Patients as Revealed by iTRAQ-Based Quantitative Proteomic Analysis

Proteins with Altered Levels in Plasma from Glioblastoma Patients as Revealed by iTRAQ-Based Quantitative Proteomic Analysis

Toward Next Generation Plasma Profiling via Heat-induced Epitope Retrieval and Array-based Assays

Carnosine and Related Peptides: Therapeutic Potential in Age-Related Disorders

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