P2Y purinoceptors mediate ATP-induced changes in intracellular calcium and amylase release in acinar cells of mouse parotid glands. 2016

Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
Department of Anatomy (Cell Biology), Iwate Medical University.

Adenosine 5'-triphosphate (ATP) can act as an extracellular signal that regulates various cellular functions. The present study aimed to determine which purinoceptors play a role in ATP-induced changes in intracellular Ca(2+) ([Ca(2+)]i) and amylase secretion in mouse parotid glands. ATP induced a steep increase in [Ca(2+)]i in acinar cells. The removal of extracellular Ca(2+) or the use of Ca(2+) channel blockers slightly inhibited this increase. Inhibition of PLCγ by U73122 and of IP3 by xestospongin C did not completely block this increase. The purinoceptor antagonists suramin and reactive blue-2 strongly inhibited the ATP-induced changes in [Ca(2+)]i. 2-MeSATP induced a strong increase in [Ca(2+)]i, while Bz-ATP induced a small [Ca(2+)]i increase, and UTP and α,β-MeATP had no effect. The potency order of ATP analogs (2-MeSATP > ATP >> UTP) suggested that P2Y1 and P2Y12 play a significant role in the cellular response to ATP. RT-PCR revealed that P2X2,4,7 and P2Y1,2,10,12,14 were expressed in acinar cells. Ca(2+)-dependent exocytotic secretion of amylase was detected in parotid glands. These findings indicated that ATP activates P2Y receptors more than P2X receptors at low concentrations. Thus, P2Y receptors were found to be the main receptors involved in Ca(2+)-related cell homeostasis and amylase secretion in mouse parotid glands.

UI MeSH Term Description Entries
D010306 Parotid Gland The largest of the three pairs of SALIVARY GLANDS. They lie on the sides of the FACE immediately below and in front of the EAR. Gland, Parotid,Glands, Parotid,Parotid Glands
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000255 Adenosine Triphosphate An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. ATP,Adenosine Triphosphate, Calcium Salt,Adenosine Triphosphate, Chromium Salt,Adenosine Triphosphate, Magnesium Salt,Adenosine Triphosphate, Manganese Salt,Adenylpyrophosphate,CaATP,CrATP,Manganese Adenosine Triphosphate,MgATP,MnATP,ATP-MgCl2,Adenosine Triphosphate, Chromium Ammonium Salt,Adenosine Triphosphate, Magnesium Chloride,Atriphos,Chromium Adenosine Triphosphate,Cr(H2O)4 ATP,Magnesium Adenosine Triphosphate,Striadyne,ATP MgCl2
D000681 Amylases A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-. Diastase,Amylase
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D015870 Gene Expression The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION. Expression, Gene,Expressions, Gene,Gene Expressions
D042541 Intracellular Space The area within CELLS. Subcellular Space,Intracellular Spaces,Space, Intracellular,Space, Subcellular,Spaces, Intracellular,Spaces, Subcellular,Subcellular Spaces
D051379 Mice The common name for the genus Mus. Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus

Related Publications

Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
January 2012, Histochemistry and cell biology,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
December 1976, The Biochemical journal,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
October 1997, European journal of pharmacology,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
December 1987, Biochemical and biophysical research communications,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
August 2004, American journal of physiology. Renal physiology,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
December 2002, The Journal of biological chemistry,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
March 1979, Biochimica et biophysica acta,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
January 1988, Journal of submicroscopic cytology and pathology,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
November 1982, Life sciences,
Kasumi Moriguchi-Mori, and Hironori Higashio, and Kanako Isobe, and Miho Kumagai, and Kana Sasaki, and Yoh-ichi Satoh, and Akiyoshi Kuji, and Tomoyuki Saino
November 1973, The Journal of physiology,
Copied contents to your clipboard!