Enzyme-linked immunosorbent assay for the detection of total cathepsin H in human tissue cytosols and sera

Schweiger, Ana; Štabuc, Borut; Popović, Tatjana; Türk, Vito; Kos, Janko

doi:10.1016/s0022-1759(96)00218-9

Cited by 43 publications

(31 citation statements)

References 16 publications

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“…ditional prognostic information. In the last decade, numerous studies have detected cathepsin B and H expression in sera from patients with various cancer types, suggesting that these markers may provide diagnostic information (23)(24)(25)(26)(27)(28)(29). So far, the relative increase in cathepsin H serum levels with respect to controls was larger than for cathepsin B in patients with melanoma, colorectal cancer and lung cancer (23,28,29).…”

Section: Discussionmentioning

confidence: 99%

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Cathepsin B, Cathepsin H, Cathepsin X and Cystatin C in Sera of Patients with Early-Stage and Inflammatory Breast Cancer

et al. 2008

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Numerous studies have linked cathepsins and their inhibitor cystatin C to tumor invasion and metastasis. We examined whether cathepsin B, cathepsin H, cathepsin X and cystatin C could be detected in sera from women with earlystage or inflammatory breast cancer and whether they correlated with clinicopathological characteristics. Preoperative serum was obtained from 176 patients with early-stage breast cancer (tumor size ≤5 cm, negative lymph nodes) and 31 patients with inflammatory breast cancer. Cathepsin and cystatin C levels were measured by ELISA. The patient and tumor characteristics under study were age at diagnosis, menopausal status, tumor size, tumor grade, and steroid hormone receptor status. Serum cathepsin B levels were significantly lower in patients with poorly differentiated tumors. High cystatin C levels were associated with tumor size, postmenopausal status and patient age. Interestingly, significantly lower levels of cathepsin X and H were found in patients with inflammatory breast cancer, a trend also observed for cathepsin B and cystatin C.

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Section: Discussionmentioning

confidence: 99%

“…Cathepsin H For detection of cathepsin H, sheep polyclonal antibody was used as capture antibody and murine 1D10 monoclonal antibody for detection, as described (24). They both recognize free antigen and enzyme-inhibitor complexes.…”

Section: Cystatin Cmentioning

confidence: 99%

Cathepsin B, Cathepsin H, Cathepsin X and Cystatin C in Sera of Patients with Early-Stage and Inflammatory Breast Cancer

et al. 2008

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“…Antibodies-Mouse monoclonal antibody (mAb) 1D10 and sheep polyclonal antibody (pAb) against CtsH were raised by our group (27). Goat pAbs against talin (sc-7534) and against ␤ 3 -integrin (sc-6627) were purchased from Santa Cruz Biotechnology.…”

Section: Methodsmentioning

confidence: 99%

“…The peptide substrate (200 M) was incubated with active CtsH (1.42 M) isolated from human liver (27) for 1 h at 37°C in phosphate buffer (pH 6.8) containing 1 mM EDTA and 2.5 mM dithiothreitol. For inhibition of CtsH, CTSHi (5 M) was preincubated with active CtsH for 10 min at 37°C.…”

Section: Methodsmentioning

confidence: 99%

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Cathepsin H Mediates the Processing of Talin and Regulates Migration of Prostate Cancer Cells

Jevnikar

Rojnik

Jamnik

et al. 2013

Journal of Biological Chemistry

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Background: Cathepsin H (CtsH) is an aminopeptidase that is involved in tumor progression. Results: CtsH cleaves talin, and its inhibition reduces the migration of prostate cancer cells. Conclusion: CtsH affects cell migration by influencing the activity of integrins, a process that could be regulated by talin cleavage. Significance: Identification of novel CtsH proteolytic targets is important to understand and control tumor progression.

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Functional protease profiling for diagnosis of malignant disease

Findeisen

Neumaier

2011

Proteomics Clinical Apps

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Clinical proteomic profiling by mass spectrometry (MS) aims at uncovering specific alterations within mass profiles of clinical specimens that are of diagnostic value for the detection and classification of various diseases including cancer. However, despite substantial progress in the field, the clinical proteomic profiling approaches have not matured into routine diagnostic applications so far. Their limitations are mainly related to high-abundance proteins and their complex processing by a multitude of endogenous proteases thus making rigorous standardization difficult. MS is biased towards the detection of low-molecular-weight peptides. Specifically, in serum specimens, the particular fragments of proteolytically degraded proteins are amenable to MS analysis. Proteases are known to be involved in tumour progression and tumour-specific proteases are released into the blood stream presumably as a result of invasive progression and metastasis. Thus, the determination of protease activity in clinical specimens from patients with malignant disease can offer diagnostic and also therapeutic options. The identification of specific substrates for tumour proteases in complex biological samples is challenging, but proteomic screens for proteases/substrate interactions are currently experiencing impressive progress. Such proteomic screens include peptide-based libraries, differential isotope labelling in combination with MS, quantitative degradomic analysis of proteolytically generated neo-N-termini, monitoring the degradation of exogenous reporter peptides with MS, and activity-based protein profiling. In the present article, we summarize and discuss the current status of proteomic techniques to identify tumour-specific protease-substrate interactions for functional protease profiling. Thereby, we focus on the potential diagnostic use of the respective approaches.

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Enzyme-linked immunosorbent assay for the detection of total cathepsin H in human tissue cytosols and sera

Cited by 43 publications

References 16 publications

Cathepsin B, Cathepsin H, Cathepsin X and Cystatin C in Sera of Patients with Early-Stage and Inflammatory Breast Cancer

Cathepsin B, Cathepsin H, Cathepsin X and Cystatin C in Sera of Patients with Early-Stage and Inflammatory Breast Cancer

Cathepsin H Mediates the Processing of Talin and Regulates Migration of Prostate Cancer Cells

Functional protease profiling for diagnosis of malignant disease

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