Use of alpha-N-benzoyl-L-arginine-p-nitroanilide as trypsin substrate in estimation of alpha 1-antitrypsin.

Dietz, Albert A.; Rubinstein, Herbert M.; Hodges, LaVerne K.

doi:10.1093/clinchem/22.10.1754

Cited by 13 publications

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“…STIC was determined by enzymatic assay using alpha‐N‐benzoyl‐L‐arginine‐p‐nitroanilide (BAPNA; Sigma, St. Louis, MO, USA) as substrate [20]. The assay was carried out at 25°C using a water bath.…”

Section: Methodsmentioning

confidence: 99%

T lymphocyte subset profile and serum alpha-1-antitrypsin in pathogenesis of chronic obstructive pulmonary disease

Gupta

Chattopadhaya

Bhadoria

et al. 2007

Clinical and Experimental Immunology

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SummaryChronic obstructive pulmonary disease (COPD) is an inflammatory disorder characterized by the presence of non-fully reversible airflow limitation. The study was undertaken to investigate the involvement of alpha-1-antitrypsin (a1AT) and T lymphocyte subsets in the pathogenesis of COPD. Blood samples of 50 subjects, including 25 healthy volunteers and 25 patients with COPD, were analysed. Serum trypsin inhibitory capacity (STIC) was determined by enzymatic assay. CD4+ and CD8 + T lymphocytes were enumerated in heparinized blood using a fluorescence activated cell sorter counter. The STIC in COPD patients was found to be decreased significantly than in controls (P < 0·01). In COPD patients with lower expression levels of a1AT, a highly significant decrease in the number of CD4 + T lymphocytes (P < 0·0009) and CD4/CD8 ratio was observed compared with control subjects (P < 0·008). The mean Ϯ standard error of CD8 + lymphocytes was found to be little different (only marginally decreased) in COPD patients compared to healthy controls; however, an alteration in the individual count of CD8 + lymphocytes cells was observed in COPD patients. Using linear regression analysis, a negative correlation was observed between STIC and CD4 + lymphocytes and CD8+ lymphocytes (r = -0·40, P < 0·04; r = -0·42, P < 0·03, respectively) in COPD patients. An alteration in a1AT and T lymphocyte subsets in COPD patients suggested that interplay of these factors may be responsible for the progression of COPD.

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Section: Methodsmentioning

confidence: 99%

T lymphocyte subset profile and serum alpha-1-antitrypsin in pathogenesis of chronic obstructive pulmonary disease

Gupta

Chattopadhaya

Bhadoria

et al. 2007

Clinical and Experimental Immunology

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“…Serum A1AT concentration was measured on NOR-Partigen plates (Dade Behring). Serum trypsin inhibitory capacity (TIC) was measured with N-benzoyl-dl-arginine-p-nitroaniline (BAPNA, Sigma) as substrate by the method of Dietz and coworkers which was adapted for IL 600 Clinical Chemistry Analyzer (Instrumentation Laboratory) ( Dietz, 1976 ). All TIC measurements were performed in triplicate.…”

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confidence: 99%

Identification of a rare p.G320R alpha-1-antitrypsin variant in emphysema and lung cancer patients

Ljujić¹,

Topić

Nikolić³

et al. 2009

Genet. Mol. Biol.

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The alpha-1-antitrypsin (A1AT) gene is highly polymorphic, with more than 100 genetic variants identified of which some can affect A1AT protein concentration and/or function and lead to pulmonary and/or liver disease. This study reports on the characterization of a p.G320R variant found in two patients, one with emphysema and the other with lung cancer. This variant results from a single base-pair substitution in exon 4 of the A1AT gene, and has been characterized as P by isoelectric focusing. Functional evaluation of the A1AT p.G320R variant was through comparing specific trypsin inhibitory activity in two patients with pulmonary disorders, carriers of the p.G320R variant, and 19 healthy individuals, carriers of normal A1AT M variants. Results showed that specific trypsin inhibitory activity was lower in both emphysema (2.45 mU/g) and lung cancer (2.07 mU/g) patients than in carriers of the normal variants (range 2.51-3.71 mU/g). This rare A1AT variant is associated with reduced functional activity of A1AT protein. Considering that it was found in patients with severe pulmonary disorders, this variant could be of clinical significance.

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“…The following tests were performed in blood serum according to the methods given below: (1) CB was determined with the use of fluorogenic substrate using the Barrett method[ 33 ]; (2) LE in a complex with AAT was determined immunoenzymatically using the MERCK test; (3) Total sialic acid (TSA) was determined colorimetrically using the periodate-resorcinol method, according to Jourdian et al [ 34 ]; (4) Lipid-bound sialic acid (LASA) was determined colorimetrically using Tautu et al [ 35 ]; and (5) The antitrypsin activity (ATA) in blood plasma (in the study referred to as antitrypsin capacity — ATA) was determined colorimetrically against trypsin using the method proposed by Warwas et al [ 36 ] and Dietz et al [ 37 ].…”

Section: Methodsmentioning

confidence: 99%

Diagnostic usefulness of selected proteases and acute phase factors in patients with colorectal adenocarcinoma

Sebzda¹,

Gnus²,

Dziadkowiec³

et al. 2021

WJG

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BACKGROUND Uncontrolled growth and loss of control over basic metabolic functions, leading to invasive proliferation and metastases, are the salient traits of malignant tumors in general and colorectal cancer in particular. Invasion and metastases hinder effective tumor treatment. While surgical techniques and radiotherapy can be used to remove tumor focus, only chemotherapy can eliminate dispersed neoplastic cells. However, the efficacy of the latter method is limited in the advanced stages of the disease. Therefore, recognition of the mechanisms involved in neoplastic cell spreading is indispensable for developing effective therapies. AIM To use a number of biomarkers involved in cancer progression and identify a panel that could be used for effective early diagnosis. METHODS We recruited 185 patients with colorectal adenocarcinoma (98 men, 87 women with median age 63). Thirty-five healthy controls were sex and age-matched. Dukes’ staging was as follows: A = 22, B = 52, C = 72, D = 39. We analyzed patients' blood serum before surgery. We determined: (1) Cathepsin B (CB) with Barrett's method (fluorogenic substrate); (2) Leukocytic elastase (LE) in a complex with alpha 1 trypsin inhibitor (AAT) using the immunoenzymatic MERCK test; (3) Total sialic acid (TSA) with the colorimetric periodate-resorcinol method; (4) Lipid-bound sialic acid (LASA) with the colorimetric Taut's method; and (5) The antitrypsin activity (ATA) employing the colorimetric test. RESULTS In patients, the values of the five biochemical parameters were as follows: CB = 16.1 ± 8.8 mU/L, LE = 875 ± 598 µg/L, TSA = 99 ± 31 mg%, LASA = 0.68 ± 0.33 mg%, and ATA = 3211 ± 1504 U/mL. Except for LASA, they were significantly greater than those of controls: CB = 11.4 ± 6.5 mU/L, LE = 379 ± 187 µg/L, TSA = 71.4 ± 15.1 mg%, LASA = 0.69 ± 0.28 mg%, and ATA = 2016 ± 690 U/mL. For CB and LASA, the differences between the four Dukes’ stages and controls were not statistically significant. The inter-stage differences for CB and LASA were also absent. The receiver operating characteristic (ROC) analysis revealed the potential diagnostic value of CB, TSA, and ATA. The area under ROC, sensitivity, and specificity for these three parameters were: 0.85, 72%, 90%; 0.75, 66%, 77%; and 0.77, 63%, 84%, respectively. The sensitivity and specificity for the three-parameter panel CB-TSA-ATA were equal to 88.2% and 100%, respectively. CONCLUSION The increased value of CB, TSA, and ATA parameters are associated with tumor biology, invasion, and metastasis of colorectal cancer. The presented evidence suggests the potential value of the CB-TSA-ATA biochemical marker panel in early diagnostics.

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Use of alpha-N-benzoyl-L-arginine-p-nitroanilide as trypsin substrate in estimation of alpha 1-antitrypsin.

Cited by 13 publications

References 0 publications

T lymphocyte subset profile and serum alpha-1-antitrypsin in pathogenesis of chronic obstructive pulmonary disease

T lymphocyte subset profile and serum alpha-1-antitrypsin in pathogenesis of chronic obstructive pulmonary disease

Identification of a rare p.G320R alpha-1-antitrypsin variant in emphysema and lung cancer patients

Diagnostic usefulness of selected proteases and acute phase factors in patients with colorectal adenocarcinoma

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