Rat ileal alkaline phosphatase activity and secretion is stimulated by alterations in calcium metabolism
The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5 µg/animal, intraperitoneally) alkaline phosphatase (ALP) activity was elevated 11-fold in the ileum, 1.5-fold in the duodenum and calvarium, 3-fold in serum, and not at all in...
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Published in | Biochimica et Biophysica Acta (BBA) - General Subjects Vol. 990; no. 2; pp. 165 - 174 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
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Amsterdam
Elsevier B.V
24.02.1989
Elsevier BV Elsevier North-Holland |
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Abstract | The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5
µg/animal, intraperitoneally) alkaline phosphatase (ALP) activity was elevated 11-fold in the ileum, 1.5-fold in the duodenum and calvarium, 3-fold in serum, and not at all in liver. The elevated ALP activity was prevented by prior treatment with flunarizine, a calcium channel blocker, and by W-7, a calmodulin antagonist. cAMP content in ileum paralleled the timing and changes in ALP activity, but was not elevated in the duodenum or calvarium. Calcium ionophore A23187 and calcitonin treatment also increased ileal, duodenal, and calvarial ALP activity, but by less than the response to calmodulin. All of these treatments caused a 2-fold elevation in serum 1,25-dihydroxyvitamin D-3 (l,25(OH)
2D
3) levels. Pretreatment of the animals with parathyroid hormone prevented the rise of both ALP activity and of 1,25(OH)
2D
3. Administration of l,25(OH)
2D
3 alone stimulated a different pattern of increased ALP activity, greater in duodenum than ileum. The uptake of
45Ca by calmodulin was also elevated in ileum and calvarium. These data suggest that shifts in calcium movement, perhaps mediated by vitamin D, can alter ALP activity, and may provide a mechanism for rapid control of the secretion of this enzyme. |
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AbstractList | The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5
µg/animal, intraperitoneally) alkaline phosphatase (ALP) activity was elevated 11-fold in the ileum, 1.5-fold in the duodenum and calvarium, 3-fold in serum, and not at all in liver. The elevated ALP activity was prevented by prior treatment with flunarizine, a calcium channel blocker, and by W-7, a calmodulin antagonist. cAMP content in ileum paralleled the timing and changes in ALP activity, but was not elevated in the duodenum or calvarium. Calcium ionophore A23187 and calcitonin treatment also increased ileal, duodenal, and calvarial ALP activity, but by less than the response to calmodulin. All of these treatments caused a 2-fold elevation in serum 1,25-dihydroxyvitamin D-3 (l,25(OH)
2D
3) levels. Pretreatment of the animals with parathyroid hormone prevented the rise of both ALP activity and of 1,25(OH)
2D
3. Administration of l,25(OH)
2D
3 alone stimulated a different pattern of increased ALP activity, greater in duodenum than ileum. The uptake of
45Ca by calmodulin was also elevated in ileum and calvarium. These data suggest that shifts in calcium movement, perhaps mediated by vitamin D, can alter ALP activity, and may provide a mechanism for rapid control of the secretion of this enzyme. The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5 micrograms/animal, intraperitoneally) alkaline phosphatase (ALP) activity was elevated 11-fold in the ileum, 1.5-fold in the duodenum and calvarium, 3-fold in serum, and not at all in liver. The elevated ALP activity was prevented by prior treatment with flunarizine, a calcium channel blocker, and by W-7, a calmodulin antagonist. cAMP content in ileum paralleled the timing and changes in ALP activity, but was not elevated in the duodenum or calvarium. Calcium ionophore A23187 and calcitonin treatment also increased ileal, duodenal, and calvarial ALP activity, but by less than the response to calmodulin. All of these treatments caused a 2-fold elevation in serum 1,25-dihydroxyvitamin D-3 (1,25(OH)2D3) levels. Pretreatment of the animals with parathyroid hormone prevented the rise of both ALP activity and of 1,25(OH)2D3. Administration of 1,25(OH)2D3 alone stimulated a different pattern of increased ALP activity, greater in duodenum than ileum. The uptake of 45Ca by calmodulin was also elevated in ileum and calvarium. These data suggest that shifts in calcium movement, perhaps mediated by vitamin D, can alter ALP activity, and may provide a mechanism for rapid control of the secretion of this enzyme. The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5 micrograms/animal, intraperitoneally) alkaline phosphatase (ALP) activity was elevated 11-fold in the ileum, 1.5-fold in the duodenum and calvarium, 3-fold in serum, and not at all in liver. The elevated ALP activity was prevented by prior treatment with flunarizine, a calcium channel blocker, and by W-7, a calmodulin antagonist. cAMP content in ileum paralleled the timing and changes in ALP activity, but was not elevated in the duodenum or calvarium. Calcium ionophore A23187 and calcitonin treatment also increased ileal, duodenal, and calvarial ALP activity, but by less than the response to calmodulin. All of these treatments caused a 2-fold elevation in serum 1,25-dihydroxyvitamin D-3 (1,25(OH)2D3) levels. Pretreatment of the animals with parathyroid hormone prevented the rise of both ALP activity and of 1,25(OH)2D3. Administration of 1,25(OH)2D3 alone stimulated a different pattern of increased ALP activity, greater in duodenum than ileum. The uptake of 45Ca by calmodulin was also elevated in ileum and calvarium. These data suggest that shifts in calcium movement, perhaps mediated by vitamin D, can alter ALP activity, and may provide a mechanism for rapid control of the secretion of this enzyme.The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5 micrograms/animal, intraperitoneally) alkaline phosphatase (ALP) activity was elevated 11-fold in the ileum, 1.5-fold in the duodenum and calvarium, 3-fold in serum, and not at all in liver. The elevated ALP activity was prevented by prior treatment with flunarizine, a calcium channel blocker, and by W-7, a calmodulin antagonist. cAMP content in ileum paralleled the timing and changes in ALP activity, but was not elevated in the duodenum or calvarium. Calcium ionophore A23187 and calcitonin treatment also increased ileal, duodenal, and calvarial ALP activity, but by less than the response to calmodulin. All of these treatments caused a 2-fold elevation in serum 1,25-dihydroxyvitamin D-3 (1,25(OH)2D3) levels. Pretreatment of the animals with parathyroid hormone prevented the rise of both ALP activity and of 1,25(OH)2D3. Administration of 1,25(OH)2D3 alone stimulated a different pattern of increased ALP activity, greater in duodenum than ileum. The uptake of 45Ca by calmodulin was also elevated in ileum and calvarium. These data suggest that shifts in calcium movement, perhaps mediated by vitamin D, can alter ALP activity, and may provide a mechanism for rapid control of the secretion of this enzyme. |
Author | Sekine, T. Komoda, T. Arai, Y. Alpers, D.H. Kumegawa, M. Sakagishi, Y. Koyama, I. |
Author_xml | – sequence: 1 givenname: T. surname: Komoda fullname: Komoda, T. organization: Department of Biochemistry, Saitama Medical School, Saitama – sequence: 2 givenname: I. surname: Koyama fullname: Koyama, I. organization: Department of Biochemistry, Saitama Medical School, Saitama – sequence: 3 givenname: Y. surname: Arai fullname: Arai, Y. organization: Department of Biochemistry, Saitama Medical School, Saitama – sequence: 4 givenname: T. surname: Sekine fullname: Sekine, T. organization: Department of Biochemistry, Saitama Medical School, Saitama – sequence: 5 givenname: Y. surname: Sakagishi fullname: Sakagishi, Y. organization: Department of Biochemistry, Saitama Medical School, Saitama – sequence: 6 givenname: M. surname: Kumegawa fullname: Kumegawa, M. organization: Department of Oral Anatomy, Dental School of Meikai University, Saitama (Japan) – sequence: 7 givenname: D.H. surname: Alpers fullname: Alpers, D.H. organization: Department of Medicine, Washington University School of Medicine, St. Louis, MO (U.S.A.) |
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Cites_doi | 10.1016/S0021-9258(19)70149-5 10.1210/endo-118-2-727 10.1002/hep.1840060307 10.1016/0003-9861(86)90080-9 10.1111/j.1432-1033.1982.tb06718.x 10.1172/JCI112597 10.1172/JCI112241 10.1016/0003-2697(76)90527-3 10.1016/0143-4160(81)90025-7 10.1016/0378-4347(87)80184-6 10.1007/BF02411244 10.1016/S0021-9258(19)69249-5 10.1016/0006-291X(70)90199-3 10.1016/0304-4165(70)90296-5 10.1083/jcb.103.4.1615 10.1021/jm00360a001 10.1007/BF02555840 10.1210/endo-119-3-1131 10.1016/0165-6147(85)90052-5 10.1016/0003-9861(88)90100-2 10.1016/0003-9861(85)90024-4 10.1016/0005-2744(78)90042-6 10.1016/S0021-9258(19)68693-X 10.1111/j.1365-2265.1983.tb02977.x 10.1016/0304-4165(70)90034-6 10.1016/S0021-9258(20)81948-6 10.1152/ajplegacy.1973.224.3.548 10.1146/annurev.ph.47.030185.001311 10.1016/0014-5793(84)81071-6 10.1042/bj1050779 10.1016/0016-5085(86)90558-5 10.1016/0009-8981(87)90246-4 10.1016/0304-4165(83)90139-3 10.1038/291327a0 10.1016/S0021-9258(19)68719-3 10.1016/0304-4165(84)90110-7 10.1042/bj2250127 10.1016/0006-291X(84)91555-9 10.1042/bst0100147 |
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Keywords | 1,25-Dihydroxyvitamin D-3 Alkaline phosphatase 1,25(OH) 2D 3 ALP PMSF PTH Calcium metabolism Rat organs Calcium ionophore Calmodulin CAM Calcium Rat Enzyme Secretion Rodentia Gut Stimulation Metabolism Vertebrata Regulation(control) Mammalia Colecalciferol |
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References | Carafoli (bib38) 1981; 2 Komoda, Koyama, Nagata, Sakagishi, DeSchryver-Kecskemeti, Alpers (bib18) 1986; 91 Fraher, Adami, Clements, Jones, O’Riordan (bib21) 1983; 18 Yusufi, Low, Turner, Dousa (bib5) 1983; 258 Nellans, Popovitch (bib13) 1981; 256 Bernard, Bianco, Bonucci, Costantini, Lunazzi, Martinuzzig, Modricky, Moro, Paufili, Pollesello, Stagni, Vittur (bib40) 1986; 103 Speeding (bib24) 1985; 6 Lazo, Rivaya, Velasco (bib27) 1984; 798 Norman, Mirecheff, Adam, Spietvogel (bib3) 1970; 215 Wilson, Lawson (bib4) 1982; 125 Stirpe, Fiume (bib23) 1967; 105 Komoda, Koyama, Nagata, Sakagishi, Kurata, Kumegawa (bib14) 1986; 251 Rasmussen (bib2) 1983 Henning (bib10) 1985; 47 Koyama, Arai, Sakagishi, Ikazawa, Komoda (bib28) 1987; 420 Bikle, Munson (bib31) 1986; 118 Kakiuchi, Yamazaki (bib22) 1970; 41 Kravitt, Subbert, Ennis (bib41) 1978; 224 Komoda, Sakagishi (bib19) 1978; 523 Kubo, Matsuda, Kase, Yamada (bib32) 1984; 124 Bikle, Munson (bib35) 1985; 76 Lee, Reimers, Cowan, Fullmer, Wasserman (bib36) 1988; 261 Bradford (bib20) 1976; 72 Janis, Triggle (bib25) 1983; 26 Ausiello, Hall (bib26) 1981; 256 Miura, Matsuzaki, Sakagishi, Komoda (bib17) 1987; 163 Yedlin, Young, Seetharam, Alpers (bib34) 1981; 256 Koyama, Komoda, Sakagishi, Kurata (bib15) 1983; 760 Stigbrand, Fishman (bib1) 1984 Jaeger, Jones, Clements, Hayslett (bib42) 1986; 78 Moreno, Cortes, Asteggiano, Pereira, Tolosa, Cartas, Blanco (bib11) 1985; 240 Seetharam, Sussman, Komoda, Alpers (bib8) 1986; 6 Glickman, Alpers, Drummey, Isselbacher (bib7) 1970; 201 Krieger, Tashjian (bib29) 1982; 34 Bikle, Munson, Chafouleas (bib33) 1984; 174 Smith, Bruns, Lawson (bib12) 1985; 225 Taft, Shaw, Danks, Prince, Larkings (bib43) 1986; 119 Komoda, Nagata, Kiyoki, Miura, Koyama, Sakagishi, Kumegawa (bib16) 1988; 42 DeLuca (bib37) 1982; 10 Komoda, Kumegawa, Yajima, Tamura, Alpers (bib9) 1984; 246 Kawashima, Torikai, Kurokawa (bib30) 1981; 291 Niggli, Adunyash, Penniston, Carafoli (bib39) 1981; 256 Chan, Stinson (bib6) 1986; 261 Seetharam (10.1016/S0304-4165(89)80030-3_bib8) 1986; 6 Nellans (10.1016/S0304-4165(89)80030-3_bib13) 1981; 256 Jaeger (10.1016/S0304-4165(89)80030-3_bib42) 1986; 78 Stigbrand (10.1016/S0304-4165(89)80030-3_bib1) 1984 Kawashima (10.1016/S0304-4165(89)80030-3_bib30) 1981; 291 Bikle (10.1016/S0304-4165(89)80030-3_bib33) 1984; 174 Bikle (10.1016/S0304-4165(89)80030-3_bib35) 1985; 76 Janis (10.1016/S0304-4165(89)80030-3_bib25) 1983; 26 Chan (10.1016/S0304-4165(89)80030-3_bib6) 1986; 261 Bradford (10.1016/S0304-4165(89)80030-3_bib20) 1976; 72 Kakiuchi (10.1016/S0304-4165(89)80030-3_bib22) 1970; 41 Fraher (10.1016/S0304-4165(89)80030-3_bib21) 1983; 18 Carafoli (10.1016/S0304-4165(89)80030-3_bib38) 1981; 2 Krieger (10.1016/S0304-4165(89)80030-3_bib29) 1982; 34 Bikle (10.1016/S0304-4165(89)80030-3_bib31) 1986; 118 Yedlin (10.1016/S0304-4165(89)80030-3_bib34) 1981; 256 Ausiello (10.1016/S0304-4165(89)80030-3_bib26) 1981; 256 Kravitt (10.1016/S0304-4165(89)80030-3_bib41) 1978; 224 Miura (10.1016/S0304-4165(89)80030-3_bib17) 1987; 163 Taft (10.1016/S0304-4165(89)80030-3_bib43) 1986; 119 Niggli (10.1016/S0304-4165(89)80030-3_bib39) 1981; 256 Norman (10.1016/S0304-4165(89)80030-3_bib3) 1970; 215 Komoda (10.1016/S0304-4165(89)80030-3_bib19) 1978; 523 Lazo (10.1016/S0304-4165(89)80030-3_bib27) 1984; 798 DeLuca (10.1016/S0304-4165(89)80030-3_bib37) 1982; 10 Bernard (10.1016/S0304-4165(89)80030-3_bib40) 1986; 103 Smith (10.1016/S0304-4165(89)80030-3_bib12) 1985; 225 Koyama (10.1016/S0304-4165(89)80030-3_bib15) 1983; 760 Stirpe (10.1016/S0304-4165(89)80030-3_bib23) 1967; 105 Speeding (10.1016/S0304-4165(89)80030-3_bib24) 1985; 6 Wilson (10.1016/S0304-4165(89)80030-3_bib4) 1982; 125 Moreno (10.1016/S0304-4165(89)80030-3_bib11) 1985; 240 Rasmussen (10.1016/S0304-4165(89)80030-3_bib2) 1983 Glickman (10.1016/S0304-4165(89)80030-3_bib7) 1970; 201 Henning (10.1016/S0304-4165(89)80030-3_bib10) 1985; 47 Koyama (10.1016/S0304-4165(89)80030-3_bib28) 1987; 420 Komoda (10.1016/S0304-4165(89)80030-3_bib14) 1986; 251 Komoda (10.1016/S0304-4165(89)80030-3_bib16) 1988; 42 Komoda (10.1016/S0304-4165(89)80030-3_bib9) 1984; 246 Lee (10.1016/S0304-4165(89)80030-3_bib36) 1988; 261 Yusufi (10.1016/S0304-4165(89)80030-3_bib5) 1983; 258 Komoda (10.1016/S0304-4165(89)80030-3_bib18) 1986; 91 Kubo (10.1016/S0304-4165(89)80030-3_bib32) 1984; 124 |
References_xml | – volume: 261 start-page: 7639 year: 1986 end-page: 7645 ident: bib6 publication-title: J. Biol. Chem. – year: 1984 ident: bib1 publication-title: Human Alkaline Phosphatases – volume: 78 start-page: 456 year: 1986 end-page: 461 ident: bib42 publication-title: J. Clin. Invest. – volume: 163 start-page: 279 year: 1987 end-page: 287 ident: bib17 publication-title: Clin. Chim. Acta – volume: 798 start-page: 361 year: 1984 end-page: 367 ident: bib27 publication-title: Biochim. Biophys. Acta – volume: 256 start-page: 9796 year: 1981 end-page: 9798 ident: bib26 publication-title: J. Biol. Chem. – volume: 103 start-page: 1615 year: 1986 end-page: 1623 ident: bib40 publication-title: J. Cell Biol. – volume: 251 start-page: 323 year: 1986 end-page: 335 ident: bib14 publication-title: Arch. Biochem. Biophys. – volume: 72 start-page: 248 year: 1976 end-page: 254 ident: bib20 publication-title: Anal. Biochem. – volume: 18 start-page: 151 year: 1983 end-page: 165 ident: bib21 publication-title: Clin. Endocrinol. – volume: 225 start-page: 127 year: 1985 end-page: 133 ident: bib12 publication-title: Biochem. J. – volume: 34 start-page: 239 year: 1982 end-page: 244 ident: bib29 publication-title: Calcif. Tissue Int. – volume: 47 start-page: 231 year: 1985 end-page: 245 ident: bib10 publication-title: Annu. Rev. Physiol. – volume: 760 start-page: 169 year: 1983 end-page: 174 ident: bib15 publication-title: Biochim. Biophys. Acta – volume: 119 start-page: 1131 year: 1986 end-page: 1136 ident: bib43 publication-title: Endocrinology – volume: 125 start-page: 555 year: 1982 end-page: 559 ident: bib4 publication-title: Eur. J. Biochem. – volume: 215 start-page: 348 year: 1970 end-page: 359 ident: bib3 publication-title: Biochim. Biophys. Acta – volume: 256 start-page: 9932 year: 1981 end-page: 9936 ident: bib13 publication-title: J. Biol. Chem. – volume: 26 start-page: 775 year: 1983 end-page: 785 ident: bib25 publication-title: J. Med. Chem. – volume: 201 start-page: 226 year: 1970 end-page: 233 ident: bib7 publication-title: Biochim. Biophys. Acta – volume: 118 start-page: 727 year: 1986 end-page: 732 ident: bib31 publication-title: Endocrinology – start-page: 1497 year: 1983 end-page: 1507 ident: bib2 publication-title: The Metabolic Basis of Inherited Disease – volume: 291 start-page: 327 year: 1981 end-page: 329 ident: bib30 publication-title: Nature – volume: 256 start-page: 395 year: 1981 end-page: 401 ident: bib39 publication-title: J. Biol. Chem. – volume: 6 start-page: 109 year: 1985 end-page: 114 ident: bib24 publication-title: Trends Pharmacol. Sci. – volume: 224 start-page: 548 year: 1978 end-page: 551 ident: bib41 publication-title: Am. J. Physiol. – volume: 258 start-page: 5693 year: 1983 end-page: 5701 ident: bib5 publication-title: J. Biol. Chem. – volume: 174 start-page: 30 year: 1984 end-page: 33 ident: bib33 publication-title: FEBS Lett. – volume: 256 start-page: 5620 year: 1981 end-page: 5626 ident: bib34 publication-title: J. Biol. Chem. – volume: 240 start-page: 201 year: 1985 end-page: 206 ident: bib11 publication-title: Arch. Biochem. Biophys. – volume: 246 start-page: G394 year: 1984 end-page: G400 ident: bib9 publication-title: Am. J. Physiol. – volume: 6 start-page: 374 year: 1986 end-page: 380 ident: bib8 publication-title: Hepatology – volume: 41 start-page: 1104 year: 1970 end-page: 1110 ident: bib22 publication-title: Biochem. Biophys. Res. Commun. – volume: 261 start-page: 27 year: 1988 end-page: 34 ident: bib36 publication-title: Arch. Biochem. Biophys. – volume: 2 start-page: 353 year: 1981 end-page: 363 ident: bib38 publication-title: Cell Calcium – volume: 42 start-page: 58 year: 1988 end-page: 62 ident: bib16 publication-title: Calcif. Tissue Int. – volume: 105 start-page: 779 year: 1967 end-page: 782 ident: bib23 publication-title: Biochem. J. – volume: 420 start-page: 275 year: 1987 end-page: 286 ident: bib28 publication-title: J. Chromatogr. – volume: 523 start-page: 395 year: 1978 end-page: 406 ident: bib19 publication-title: Biochim. Biophys. Acta – volume: 91 start-page: 277 year: 1986 end-page: 286 ident: bib18 publication-title: Gastroenterology – volume: 76 start-page: 2312 year: 1985 end-page: 2316 ident: bib35 publication-title: J. Clin. Invest. – volume: 124 start-page: 315 year: 1984 end-page: 321 ident: bib32 publication-title: Biochem. Biophys. Res. Commun. – volume: 10 start-page: 147 year: 1982 end-page: 152 ident: bib37 publication-title: Biochem. Soc. Trans. – year: 1984 ident: 10.1016/S0304-4165(89)80030-3_bib1 – volume: 256 start-page: 395 year: 1981 ident: 10.1016/S0304-4165(89)80030-3_bib39 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)70149-5 – volume: 118 start-page: 727 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib31 publication-title: Endocrinology doi: 10.1210/endo-118-2-727 – volume: 6 start-page: 374 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib8 publication-title: Hepatology doi: 10.1002/hep.1840060307 – volume: 251 start-page: 323 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib14 publication-title: Arch. Biochem. Biophys. doi: 10.1016/0003-9861(86)90080-9 – volume: 125 start-page: 555 year: 1982 ident: 10.1016/S0304-4165(89)80030-3_bib4 publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1982.tb06718.x – volume: 78 start-page: 456 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib42 publication-title: J. Clin. Invest. doi: 10.1172/JCI112597 – volume: 76 start-page: 2312 year: 1985 ident: 10.1016/S0304-4165(89)80030-3_bib35 publication-title: J. Clin. Invest. doi: 10.1172/JCI112241 – volume: 72 start-page: 248 year: 1976 ident: 10.1016/S0304-4165(89)80030-3_bib20 publication-title: Anal. Biochem. doi: 10.1016/0003-2697(76)90527-3 – volume: 2 start-page: 353 year: 1981 ident: 10.1016/S0304-4165(89)80030-3_bib38 publication-title: Cell Calcium doi: 10.1016/0143-4160(81)90025-7 – volume: 420 start-page: 275 year: 1987 ident: 10.1016/S0304-4165(89)80030-3_bib28 publication-title: J. Chromatogr. doi: 10.1016/0378-4347(87)80184-6 – volume: 34 start-page: 239 year: 1982 ident: 10.1016/S0304-4165(89)80030-3_bib29 publication-title: Calcif. Tissue Int. doi: 10.1007/BF02411244 – volume: 256 start-page: 5620 year: 1981 ident: 10.1016/S0304-4165(89)80030-3_bib34 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)69249-5 – volume: 41 start-page: 1104 year: 1970 ident: 10.1016/S0304-4165(89)80030-3_bib22 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(70)90199-3 – volume: 201 start-page: 226 year: 1970 ident: 10.1016/S0304-4165(89)80030-3_bib7 publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(70)90296-5 – volume: 103 start-page: 1615 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib40 publication-title: J. Cell Biol. doi: 10.1083/jcb.103.4.1615 – volume: 26 start-page: 775 year: 1983 ident: 10.1016/S0304-4165(89)80030-3_bib25 publication-title: J. Med. Chem. doi: 10.1021/jm00360a001 – volume: 42 start-page: 58 year: 1988 ident: 10.1016/S0304-4165(89)80030-3_bib16 publication-title: Calcif. Tissue Int. doi: 10.1007/BF02555840 – volume: 119 start-page: 1131 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib43 publication-title: Endocrinology doi: 10.1210/endo-119-3-1131 – volume: 6 start-page: 109 year: 1985 ident: 10.1016/S0304-4165(89)80030-3_bib24 publication-title: Trends Pharmacol. Sci. doi: 10.1016/0165-6147(85)90052-5 – volume: 261 start-page: 27 year: 1988 ident: 10.1016/S0304-4165(89)80030-3_bib36 publication-title: Arch. Biochem. Biophys. doi: 10.1016/0003-9861(88)90100-2 – volume: 240 start-page: 201 year: 1985 ident: 10.1016/S0304-4165(89)80030-3_bib11 publication-title: Arch. Biochem. Biophys. doi: 10.1016/0003-9861(85)90024-4 – volume: 523 start-page: 395 year: 1978 ident: 10.1016/S0304-4165(89)80030-3_bib19 publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2744(78)90042-6 – start-page: 1497 year: 1983 ident: 10.1016/S0304-4165(89)80030-3_bib2 – volume: 256 start-page: 9796 year: 1981 ident: 10.1016/S0304-4165(89)80030-3_bib26 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)68693-X – volume: 18 start-page: 151 year: 1983 ident: 10.1016/S0304-4165(89)80030-3_bib21 publication-title: Clin. Endocrinol. doi: 10.1111/j.1365-2265.1983.tb02977.x – volume: 215 start-page: 348 year: 1970 ident: 10.1016/S0304-4165(89)80030-3_bib3 publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(70)90034-6 – volume: 258 start-page: 5693 year: 1983 ident: 10.1016/S0304-4165(89)80030-3_bib5 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(20)81948-6 – volume: 224 start-page: 548 year: 1978 ident: 10.1016/S0304-4165(89)80030-3_bib41 publication-title: Am. J. Physiol. doi: 10.1152/ajplegacy.1973.224.3.548 – volume: 47 start-page: 231 year: 1985 ident: 10.1016/S0304-4165(89)80030-3_bib10 publication-title: Annu. Rev. Physiol. doi: 10.1146/annurev.ph.47.030185.001311 – volume: 174 start-page: 30 year: 1984 ident: 10.1016/S0304-4165(89)80030-3_bib33 publication-title: FEBS Lett. doi: 10.1016/0014-5793(84)81071-6 – volume: 261 start-page: 7639 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib6 publication-title: J. Biol. Chem. – volume: 105 start-page: 779 year: 1967 ident: 10.1016/S0304-4165(89)80030-3_bib23 publication-title: Biochem. J. doi: 10.1042/bj1050779 – volume: 91 start-page: 277 year: 1986 ident: 10.1016/S0304-4165(89)80030-3_bib18 publication-title: Gastroenterology doi: 10.1016/0016-5085(86)90558-5 – volume: 246 start-page: G394 year: 1984 ident: 10.1016/S0304-4165(89)80030-3_bib9 publication-title: Am. J. Physiol. – volume: 163 start-page: 279 year: 1987 ident: 10.1016/S0304-4165(89)80030-3_bib17 publication-title: Clin. Chim. Acta doi: 10.1016/0009-8981(87)90246-4 – volume: 760 start-page: 169 year: 1983 ident: 10.1016/S0304-4165(89)80030-3_bib15 publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(83)90139-3 – volume: 291 start-page: 327 year: 1981 ident: 10.1016/S0304-4165(89)80030-3_bib30 publication-title: Nature doi: 10.1038/291327a0 – volume: 256 start-page: 9932 year: 1981 ident: 10.1016/S0304-4165(89)80030-3_bib13 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)68719-3 – volume: 798 start-page: 361 year: 1984 ident: 10.1016/S0304-4165(89)80030-3_bib27 publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(84)90110-7 – volume: 225 start-page: 127 year: 1985 ident: 10.1016/S0304-4165(89)80030-3_bib12 publication-title: Biochem. J. doi: 10.1042/bj2250127 – volume: 124 start-page: 315 year: 1984 ident: 10.1016/S0304-4165(89)80030-3_bib32 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(84)91555-9 – volume: 10 start-page: 147 year: 1982 ident: 10.1016/S0304-4165(89)80030-3_bib37 publication-title: Biochem. Soc. Trans. doi: 10.1042/bst0100147 |
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Snippet | The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5
µg/animal, intraperitoneally)... The mechanism of calmodulin-stimulated alkaline phosphatase activity was studied in the rat. In calmodulin-treated rats (2.5 micrograms/animal,... |
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SubjectTerms | 1,25-Dihydroxyvitamin D-3 Alkaline Phosphatase Alkaline Phosphatase - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calcitonin Calcitonin - pharmacology Calcitriol Calcitriol - blood Calcium Calcium - metabolism Calcium ionophore Calmodulin Calmodulin - pharmacology Cyclic AMP Cyclic AMP - metabolism Enzymes and enzyme inhibitors Flunarizine Flunarizine - pharmacology Fundamental and applied biological sciences. Psychology Hydrolases Ileum Ileum - enzymology Isoenzymes Isoenzymes - metabolism Male Parathyroid Hormone Parathyroid Hormone - pharmacology Rat organs Rats Rats, Inbred Strains |
Title | Rat ileal alkaline phosphatase activity and secretion is stimulated by alterations in calcium metabolism |
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