ATPase Activity of the Subcellular Fractions of Colorectal
Cancer Samples under the Action of Nicotinic Acid Adenine
Dinucleotide Phosphate

J 2021

ATPase Activity of the Subcellular Fractions of Colorectal Cancer Samples under the Action of Nicotinic Acid Adenine Dinucleotide Phosphate

KUSHKEVYCH, Ivan, Mykola BYCHKOV, Solomiia BYCHKOVA, Márió GAJDÁCS, Romana MERZA et. al.

Základní údaje

Originální název

ATPase Activity of the Subcellular Fractions of Colorectal Cancer Samples under the Action of Nicotinic Acid Adenine Dinucleotide Phosphate

Autoři

KUSHKEVYCH, Ivan (203 Česká republika, garant, domácí), Mykola BYCHKOV, Solomiia BYCHKOVA, Márió GAJDÁCS, Romana MERZA a Monika VÍTĚZOVÁ (203 Česká republika, domácí)

Vydání

Biomedicines, Basel, MDPI, 2021, 2227-9059

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

30101 Human genetics

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.757

Kód RIV

RIV/00216224:14310/21:00123056

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.3390/biomedicines9121805

UT WoS

000736223100001

Klíčová slova anglicky

cancer; NAADP; Ca2+; autophagy; acidic store; ATPase; Ca2+ ATPase; EPR; Ca2+ ATPase PM; Na+/K+ ATPase; basal ATPase activity

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 20. 1. 2022 13:18, Mgr. Marie Šípková, DiS.

Anotace

V originále

In tumor cells with defects in apoptosis, autophagy allows prolonged survival. Autophagy leads to an accumulation of damaged mitochondria by autophagosomes. An acidic environment is maintained in compartments of cells, such as autophagosomes, late endosomes, and lysosomes; these organelles belong to the “acid store” of the cells. Nicotinic acid adenine dinucleotide phosphate (NAADP) may affect the release of Ca2+ from these organelles and affect the activity of Ca2+ ATPases and other ion transport proteins. Recently, a growing amount of evidence has shown that the variations in the expression of calcium channels or pumps are associated with the occurrence, disease-presentation, and the prognosis of colorectal cancer. We hypothesized that activity of ATPases in cancer tissue is higher because of intensive energy metabolism of tumor cells. The aim of our study was to ascertain the effect of NAADP on ATPase activity on tissue samples of colorectal cancer patients’ and healthy individuals. We tested the effect of NAADP on the activity of Na+/K+ ATPase; Ca2+ ATPase of endoplasmic reticulum (EPR) and plasma membrane (PM) and basal ATPase activity. Patients’ colon mucus cancer samples were obtained during endoscopy from cancer and healthy areas (control) of colorectal mucosa of the same patients. Results. The mean activity of Na+/K+ pump in samples of colorectal cancer patients (n = 5) was 4.66 ± 1.20 μmol Pi/mg of protein per hour, while in control samples from healthy tissues of the same patient (n = 5) this value was 3.88 ± 2.03 μmol Pi/mg of protein per hour. The activity of Ca2+ ATPase PM in control samples was 6.42 ± 0.63 μmol Pi/mg of protein per hour and in cancer −8.50 ± 1.40 μmol Pi/mg of protein per hour (n = 5 pts). The mean activity of Ca2+ ATPase of EPR in control samples was 7.59 ± 1.21 μmol Pi/mg versus 7.76 ± 0.24 μmol Pi/mg in cancer (n = 5 pts). Basal ATPase activity was 3.19 ± 0.87 in control samples versus 4.79 ± 1.86 μmol Pi/mg in cancer (n = 5 pts). In cancer samples, NAADP reduced the activity of Na+/K+ ATPase by 9-times (p < 0.01) and the activity of Ca2+ ATPase EPR about 2-times (p < 0.05). NAADP caused a tendency to decrease the activity of Ca2+ ATPase of PM, but increased basal ATPase activity by 2-fold vs. the mean of this index in cancer samples without the addition of NAADP. In control samples NAADP caused only a tendency to decrease the activities of Na+/K+ ATPase and Ca2+ ATPase EPR, but statistically decreased the activity of Ca2+ ATPase of PM (p < 0.05). In addition, NAADP caused a strong increase in basal ATPase activity in control samples (p < 0.01). Conclusions: We found that the activity of Na+/K+ pump, Ca2+ ATPase of PM and basal ATPase activity in cancer tissues had a strong tendency to be higher than in the controls. NAADP caused a decrease in the activities of Na+/K+ ATPase and Ca2+ ATPase EPR in cancer samples and increased basal ATPase activity. In control samples, NAADP decreased Ca2+ ATPase of PM and increased basal ATPase activity. These data confirmed different roles of NAADP-sensitive “acidic store” (autophagosomes, late endosomes, and lysosomes) in control and cancer tissue, which hypothetically may be connected with autophagy role in cancer development. The effect of NAADP on decreasing the activity of Na+/K+ pump in cancer samples was the most pronounced, both numerically and statistically. Our data shows promising possibilities for the modulation of ion-transport through the membrane of cancer cells by influence on the “acidic store” (autophagosomes, late endosomes and lysosomes) as a new approach to the treatment of colorectal cancer.

Návaznosti

MUNI/A/1425/2020, interní kód MU

Název: Podpora výzkumné činnosti studentů Mikrobiologie

Investor: Masarykova univerzita, Podpora výzkumné činnosti studentů Mikrobiologie

Citovat

KUSHKEVYCH, Ivan, Mykola BYCHKOV, Solomiia BYCHKOVA, Márió GAJDÁCS, Romana MERZA a Monika VÍTĚZOVÁ. ATPase Activity of the Subcellular Fractions of Colorectal Cancer Samples under the Action of Nicotinic Acid Adenine Dinucleotide Phosphate. Biomedicines. Basel: MDPI, 2021, roč. 9, č. 12, s. 1805-1814. ISSN 2227-9059. Dostupné z: https://dx.doi.org/10.3390/biomedicines9121805.

@article{1806532,
   author = {Kushkevych, Ivan and Bychkov, Mykola and Bychkova, Solomiia and Gajdács, Márió and Merza, Romana and Vítězová, Monika},
   article_location = {Basel},
   article_number = {12},
   doi = {http://dx.doi.org/10.3390/biomedicines9121805},
   keywords = {cancer; NAADP; Ca2+; autophagy; acidic store; ATPase; Ca2+ ATPase; EPR; Ca2+ ATPase PM; Na+/K+ ATPase; basal ATPase activity},
   language = {eng},
   issn = {2227-9059},
   journal = {Biomedicines},
   title = {ATPase Activity of the Subcellular Fractions of Colorectal Cancer Samples under the Action of Nicotinic Acid Adenine Dinucleotide Phosphate},
   url = {https://www.mdpi.com/2227-9059/9/12/1805},
   volume = {9},
   year = {2021}
}

TY  - JOUR
ID  - 1806532
AU  - Kushkevych, Ivan - Bychkov, Mykola - Bychkova, Solomiia - Gajdács, Márió - Merza, Romana - Vítězová, Monika
PY  - 2021
TI  - ATPase Activity of the Subcellular Fractions of Colorectal Cancer Samples under the Action of Nicotinic Acid Adenine Dinucleotide Phosphate
JF  - Biomedicines
VL  - 9
IS  - 12
SP  - 1805
EP  - 1805
PB  - MDPI
SN  - 22279059
KW  - cancer
KW  - NAADP
KW  - Ca2+
KW  - autophagy
KW  - acidic store
KW  - ATPase
KW  - Ca2+ ATPase
KW  - EPR
KW  - Ca2+ ATPase PM
KW  - Na+/K+ ATPase
KW  - basal ATPase activity
UR  - https://www.mdpi.com/2227-9059/9/12/1805
N2  - In tumor cells with defects in apoptosis, autophagy allows prolonged survival. Autophagy leads to an accumulation of damaged mitochondria by autophagosomes. An acidic environment is maintained in compartments of cells, such as autophagosomes, late endosomes, and lysosomes; these organelles belong to the “acid store” of the cells. Nicotinic acid adenine dinucleotide phosphate (NAADP) may affect the release of Ca2+ from these organelles and affect the activity of Ca2+ ATPases and other ion transport proteins. Recently, a growing amount of evidence has shown that the variations in the expression of calcium channels or pumps are associated with the occurrence, disease-presentation, and the prognosis of colorectal cancer. We hypothesized that activity of ATPases in cancer tissue is higher because of intensive energy metabolism of tumor cells. The aim of our study was to ascertain the effect of NAADP on ATPase activity on tissue samples of colorectal cancer patients’ and healthy individuals. We tested the effect of NAADP on the activity of Na+/K+ ATPase; Ca2+ ATPase of endoplasmic reticulum (EPR) and plasma membrane (PM) and basal ATPase activity. Patients’ colon mucus cancer samples were obtained during endoscopy from cancer and healthy areas (control) of colorectal mucosa of the same patients. Results. The mean activity of Na+/K+ pump in samples of colorectal cancer patients (n = 5) was 4.66 ± 1.20 μmol Pi/mg of protein per hour, while in control samples from healthy tissues of the same patient (n = 5) this value was 3.88 ± 2.03 μmol Pi/mg of protein per hour. The activity of Ca2+ ATPase PM in control samples was 6.42 ± 0.63 μmol Pi/mg of protein per hour and in cancer −8.50 ± 1.40 μmol Pi/mg of protein per hour (n = 5 pts). The mean activity of Ca2+ ATPase of EPR in control samples was 7.59 ± 1.21 μmol Pi/mg versus 7.76 ± 0.24 μmol Pi/mg in cancer (n = 5 pts). Basal ATPase activity was 3.19 ± 0.87 in control samples versus 4.79 ± 1.86 μmol Pi/mg in cancer (n = 5 pts). In cancer samples, NAADP reduced the activity of Na+/K+ ATPase by 9-times (p < 0.01) and the activity of Ca2+ ATPase EPR about 2-times (p < 0.05). NAADP caused a tendency to decrease the activity of Ca2+ ATPase of PM, but increased basal ATPase activity by 2-fold vs. the mean of this index in cancer samples without the addition of NAADP. In control samples NAADP caused only a tendency to decrease the activities of Na+/K+ ATPase and Ca2+ ATPase EPR, but statistically decreased the activity of Ca2+ ATPase of PM (p < 0.05). In addition, NAADP caused a strong increase in basal ATPase activity in control samples (p < 0.01). Conclusions: We found that the activity of Na+/K+ pump, Ca2+ ATPase of PM and basal ATPase activity in cancer tissues had a strong tendency to be higher than in the controls. NAADP caused a decrease in the activities of Na+/K+ ATPase and Ca2+ ATPase EPR in cancer samples and increased basal ATPase activity. In control samples, NAADP decreased Ca2+ ATPase of PM and increased basal ATPase activity. These data confirmed different roles of NAADP-sensitive “acidic store” (autophagosomes, late endosomes, and lysosomes) in control and cancer tissue, which hypothetically may be connected with autophagy role in cancer development. The effect of NAADP on decreasing the activity of Na+/K+ pump in cancer samples was the most pronounced, both numerically and statistically. Our data shows promising possibilities for the modulation of ion-transport through the membrane of cancer cells by influence on the “acidic store” (autophagosomes, late endosomes and lysosomes) as a new approach to the treatment of colorectal cancer.
ER  -

KUSHKEVYCH, Ivan, Mykola BYCHKOV, Solomiia BYCHKOVA, Márió GAJDÁCS, Romana MERZA a Monika VÍTĚZOVÁ. ATPase Activity of the Subcellular Fractions of Colorectal Cancer Samples under the Action of Nicotinic Acid Adenine Dinucleotide Phosphate. \textit{Biomedicines}. Basel: MDPI, 2021, roč.~9, č.~12, s.~1805-1814. ISSN~2227-9059. Dostupné z: https://dx.doi.org/10.3390/biomedicines9121805.

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