Serum proteinase-like peptidase activities and proteinase inhibitors in women with breast disease

Vasishta, Anil; Baker, Peter R.; Preece, P. E.; Wood, Robert A.; Cuschieri, Alfred

doi:10.1016/0277-5379(84)90184-6

Cited by 14 publications

(7 citation statements)

References 18 publications

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“…In addition, significant decrease of plasma A2M level in our study is in accordance with a previous study of prostate cancer [34]. However, the plasma level of A2M in other cancer patients can be varied, it can be increased [35] or unchanged [36] as well. Therefore, the value of A2M as cancer biomarker is still controversial.…”

Section: Discussionsupporting

confidence: 92%

Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer

et al. 2020

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Colorectal cancer (CRC) is a major cause of cancer mortality. Currently used CRC biomarkers provide insufficient sensitivity and specificity; therefore, novel biomarkers are needed to improve the CRC detection. Label-free quantitative proteomics were used to identify and compare glycoproteins, enriched by wheat germ agglutinin, from plasma of CRC patients and age-matched healthy controls. Among 189 identified glycoproteins, the levels of 7 and 15 glycoproteins were significantly altered in the non-metastatic and metastatic CRC groups, respectively. Protein-protein interaction analysis revealed that they were predominantly involved in immune responses, complement pathways, wound healing and coagulation. Of these, the levels of complement C9 (C9) was increased and fibronectin (FN1) was decreased in both CRC states in comparison to those of the healthy controls. Moreover, their levels detected by immunoblotting were validated in another independent cohort and the results were consistent with in the study cohort. Combination of CEA, a commercial CRC biomarker, with C9 and FN1 showed better diagnostic performance. Interestingly, predominant glycoforms associated with acetylneuraminic acid were obviously detected in alpha-2 macroglobulin, haptoglobin, alpha-1-acid glycoprotein 1, and complement C4-A of CRC patient groups. This glycoproteomic approach provides invaluable information of plasma proteome profiles of CRC patients and identification of CRC biomarker candidates.

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Section: Discussionsupporting

confidence: 92%

Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer

et al. 2020

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“…Apart from CRC, various authors have found significantly elevated AAT serum levels in subjects with a range of cancers, including lung [25-30], liver [31,32], pancreas [33], prostate [34], cervix [35], ovary [36,37], breast [38], Hodgkin’s lymphoma [39], larynx and other head and neck carcinomas [40,41]. The data provided by these studies taken together suggest that the presence of elevated serum levels of AAT in patients with any of these types of carcinomas is related to an invasive growth of these tumors.…”

Section: Discussionmentioning

confidence: 99%

Serum concentration of alpha-1 antitrypsin is significantly higher in colorectal cancer patients than in healthy controls

et al. 2014

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BackgroundThe association between alpha-1 antitrypsin (AAT) deficiency and colorectal cancer (CRC) is currently controversial. The present study compares AAT serum concentrations and gene frequencies between a group of CRC patients and a control group of healthy unrelated people (HUP).Methods267 CRC subjects (63% males, 72 ± 10 years old) were enlisted from a Hospital Clinic setting in Asturias, Spain. The HUP group comprised 327 subjects (67% males, mean age 70 ± 7.5 years old) from the same geographical region. Outcome measures were AAT serum concentrations measured by nephelometry, and AAT phenotyping characterization by isoelectric focusing.ResultsSignificantly higher serum concentrations were found among CRC (208 ± 60) than in HUP individuals (144 ± 20.5) (p = 0.0001). No differences were found in the phenotypic distribution of the Pi*S and Pi*Z allelic frequencies (p = 0.639), although the frequency of Pi*Z was higher in CRC (21%) than in HUP subjects (15%).ConclusionsThe only statistically significant finding in this study was the markedly higher AAT serum concentrations found in CRC subjects compared with HUP controls, irrespective of whether their Pi* phenotype was normal (Pi*MM) or deficient (Pi*MS, Pi*MZ and Pi*SZ). Although there was a trend towards the more deficient Pi* phenotype the more advanced the tumor, the results were inconclusive due to the small sample size. Consequently, more powerful studies are needed to reach firmer conclusions on this matter.

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“…There has also been considerable interest in the diagnostic utility of total serum a2M measurements in various diseases. The concentration of native a,M in serum of cancer patients measured immunologically has been reported to be normal (Bartoloni et al, 1985;Marchandise et al, 1989;Gressner et a/., 1984), minimally increased (Vasishita et al, 1984;Millan et al, 1988), and decreased (Dabrowska et al, 1988;Bauman e t a / . , 1985;Ohtani et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

Proteinase‐alpha₂ macroglobulin complexes are not increased in plasma of patients with cancer

Zucker

Lysik

Zarrabi

et al. 1991

Intl Journal of Cancer

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Alpha 2-macroglobulin, a major glycoprotein component of plasma, is unique in its capacity to bind and inhibit the proteolytic activities of all classes of proteinases. Since proteinases implicated in cancer dissemination (type-IV collagenase, plasminogen activator, cathepsins B) are normal constitutents of blood, we have explored the hypothesis that elevated tissue levels of activated proteinases bound to alpha 2M might be detected in plasma of patients with cancer. To test this premise, blood was collected from 149 subjects (33 healthy controls, 31 patients with infections and non-malignant diseases, 16 with myeloproliferative disease, 10 with gastrointestinal cancer, 7 with genito-urinary cancer, 16 with lung cancer, 14 with lymphoma, 11 with miscellaneous cancers and 11 with chronic lymphocytic leukemia and myeloma). Plasma was assayed for alpha 2M-proteinase complexes using a sandwich ELISA which employs a mouse monoclonal antibody (MAb) that binds to a neo-antigenic determinant on complexed alpha 2M and a rabbit polyclonal anti-native human alpha 2M antibody. The concentration of complexed alpha 2M in healthy controls was 14.2 +/- 9.8 micrograms/ml (mean +/- standard deviation). No significant differences in complexed alpha 2M were noted between normal and cancer groups (range 7.4-14.6 micrograms/ml). On the basis of these data, we propose that, in patients with cancer, activated proteinases are bound locally to inhibitors in the tissues and are not available to form complexes with plasma alpha 2M. An alternative explanation is that proteinases are not secreted in excess by cancer cells in vivo.

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Serum proteinase-like peptidase activities and proteinase inhibitors in women with breast disease

Cited by 14 publications

References 18 publications

Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer

Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer

Serum concentration of alpha-1 antitrypsin is significantly higher in colorectal cancer patients than in healthy controls

Proteinase‐alpha₂ macroglobulin complexes are not increased in plasma of patients with cancer

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Serum proteinase-like peptidase activities and proteinase inhibitors in women with breast disease

Cited by 14 publications

References 18 publications

Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer

Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer

Serum concentration of alpha-1 antitrypsin is significantly higher in colorectal cancer patients than in healthy controls

Proteinase‐alpha2 macroglobulin complexes are not increased in plasma of patients with cancer

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Proteinase‐alpha₂ macroglobulin complexes are not increased in plasma of patients with cancer