Amylase-Producing Lung Cancer with a Positive Epidermal Growth Factor Receptor Mutation Treated With Gefitinib: A Case Report

Minami,

doi:10.14740/wjon778w

Cited by 6 publications

(6 citation statements)

References 10 publications

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“…Amylase-producing lung tumors were first reported in 1951, 12 and they are pathologically characterized by adenocarcinoma and the secretion of salivary-type amylase. Previous reports indicated that the increase in serum CEA was not observed in amylase-producing lung adenocarcinoma 13 at the point of diagnosis. Interestingly, the CEA levels gradually increased in spite of treatment, whereas the amylase levels decreased.…”

Section: Discussionmentioning

confidence: 85%

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Alectinib for Miliary Lung Metastasis in ALK-Positive Lung Adenocarcinoma

Satoh¹,

Okuma²,

Kashima

et al. 2021

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Background Miliary pulmonary metastasis characterized by tiny nodules is a rare metastatic pattern in advanced non-small cell lung cancer (NSCLC) and is usually seen in patients harboring an EGFR mutation, and amylase-producing lung cancer is highly uncommon and rarely reported in NSCLC patients who have an EGFR mutation. Case A 32-year-old Japanese female was found to have miliary pulmonary nodules throughout both lung fields on a chest x-ray examination during an annual health check-up. Further examination by computed tomography (CT) revealed diffuse, bilateral, miliary nodules. Blood tests showed no increased tumor marker levels, but there was a significantly increased serum amylase level. A diagnosis of ALK -rearranged adenocarcinoma was made based on the results of a mediastinal lymph node biopsy obtained by endobronchial ultrasound-guided transbronchial needle aspiration (EBUS-TBNA). Treatment with alectinib resulted in rapid regression of the CT shadows and a reduction in the patient’s serum amylase level. Conclusion We have reported a case of ALK -rearranged NSCLC with a miliary pulmonary metastasis pattern that was sensitive to alectinib and in which the serum amylase level decreased in response to treatment with alectinib. Young patients with miliary pulmonary metastasis should be checked for all driver mutations.

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Section: Discussionmentioning

confidence: 85%

“…To our knowledge, two case reports on amylase-producing tumors harboring an EGFR-mutations. 13 , 14 Interestingly, amylase secretion by rat pancreatic cells is thought to be regulated by EGFR downstream signaling. 15 The relationship between ALK -rearranged NSCLC and amylase-producing lung adenocarcinoma remains unclear.…”

Section: Discussionmentioning

confidence: 99%

Alectinib for Miliary Lung Metastasis in ALK-Positive Lung Adenocarcinoma

Satoh¹,

Okuma²,

Kashima

et al. 2021

OTT

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“…Interestingly, our study showed that EGFR-positive lung adenocarcinoma tended to have higher pleural amylase levels than EGFR-negative cancer; however, the relationship between amylase secretion and EGFR mutations is uncertain (16). The EGFR gene is an oncogenic driver of tyrosine kinase activity, and EGFR has been identified as an oncogenic driver of non-small-cell lung carcinoma (NSCLC) (17).…”

Section: Discussionmentioning

confidence: 87%

Differences in Pleural Fluid Amylase Levels in Patients with Malignant Pleural Effusion Based on Cancer Type, Histologic Type, and Epidermal Growth Factor Receptor Mutations

et al. 2023

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Objective High pleural amylase levels have been reported in patients with malignant pleural effusion; however, the characteristics of this association are uncertain. Therefore, this study investigated the factors, such as cancer type and oncogenic drivers, related to pleural amylase levels in patients with malignant pleural effusion. Methods We retrospectively collected the data of 362 cancer patients (lung adenocarcinoma [n=256], lung squamous carcinoma [n=12], small-cell lung carcinoma [n=32], other lung cancers [n=5], mesothelioma [n= 31], and metastatic cancer [n=26]) with malignant pleural effusion at Fukujuji Hospital from January 2012 to October 2022. Pleural amylase levels were compared. Results Pleural amylase levels were significantly higher in patients with lung adenocarcinoma (median 58.6 IU/L [interquartile range (IQR) 33.8-139.3]) than in those with small-cell lung carcinoma (median 37.2 IU/L [IQR 26.3-63.7], p=0.012). The median pleural amylase level was higher in patients with lung adenocarcinoma than in those with other cancer or histologic types, although the difference was not significant. Pleural amylase levels were higher in epidermal growth factor receptor (EGFR) mutation-positive patients than in EGFR mutation-negative patients (median 95.8 IU/L [IQR 52.7-246.5] vs. median 51.2 IU/L [IQR 27.8-96.9], p<0.001). The Kaplan-Meier survival curves of pleural amylase ! 75 IU/L were higher than those of pleural amylase <75 IU/L (log rank test p<0.001, hazard ratio 0.54 [95% confidence interval: 0.41-0.71]). Conclusion This study demonstrates that pleural amylase levels were elevated in patients with lung adenocarcinoma and EGFR mutations. Furthermore, a high pleural amylase level was associated with a good prognosis.

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“…In addition to that, α-AMY has been identified in cases of lung cancer (12) , breast cancer, and ovarian cancer (13) . α-AMY inhibitors, commonly known as starch blockers, may offer possible mitigation by inactivating Amylase in saliva or pancreatic digesting juice, lowering blood glucose.…”

Section: Introductionmentioning

confidence: 99%

Inhibition, Characterization and Purification of α-AMY from Sera of Iraqi Breast Cancer Patients

Lafta¹,

Al-Qaisi²

2023

The Egyptian Journal of Hospital Medicine

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Background: α-Amylase enzyme is digestive enzyme that breaks down complex carbohydrates like starch into simpler sugars; it is being studied as a potential target for anti-cancer therapies. Objective: The current study aimed to evaluate the general characterization, and inhibition of α-Amylase enzyme, which had been purified from the sera of patients diagnosed with Breast Carcinoma. Materials and methods: A total of 100 blood serum samples were collected from patients with Breast cancer from Baghdad National Hope Hospital in Baghdad. α-Amylase enzyme was purified from serum clinical isolate in three stages; precipitation with 65% saturated ammonium sulphate, ion exchange chromatography utilizing a DEAEcellulose column, and gel filtration chromatography with a sephadex G-200 column. Changing conditions in pH, temperature, inhibitor concentration, and kinetics all affect the activity of the α-Amylase enzyme. Results: α-Amylase inhibition assay showed that Vitis vinifera L. was the most potent inhibitor (71.8%). During the kinetic investigation of the enzyme, it was discovered that the inhibitory mechanism that the extracts use is noncompetitive. Vmax was 0.023, and 0.012 mmol min -l at 75 μg/ml of Vitis vinifera L. , Verbena Officinalis L .extracts, respectively. Conclusions: High specific activity for α-Amylase purified from sera of Iraqi breast cancer patients was obtained after three purification steps. Ethanolic plant extracts showed inhibitory effect on α-Amylase while Vitis vinifera L. was the most potent inhibitor.

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Amylase-Producing Lung Cancer with a Positive Epidermal Growth Factor Receptor Mutation Treated With Gefitinib: A Case Report

Cited by 6 publications

References 10 publications

Alectinib for Miliary Lung Metastasis in ALK-Positive Lung Adenocarcinoma

Alectinib for Miliary Lung Metastasis in ALK-Positive Lung Adenocarcinoma

Differences in Pleural Fluid Amylase Levels in Patients with Malignant Pleural Effusion Based on Cancer Type, Histologic Type, and Epidermal Growth Factor Receptor Mutations

Inhibition, Characterization and Purification of α-AMY from Sera of Iraqi Breast Cancer Patients

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