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PubMed · 9048140

Plant gravitropic response.

Abstract

The gravitropic response of plants to a change in the gravity vector may be divided. in the phase of induction and expression. During the induction phase the amyloplasts, due to their greater density than the cytoplasmic density, shift their position in less than a minute. During this shift there is an interaction with the endoplasmic reticulum, although a role of actin-like proteins of the cytoskeleton may also be involved in this process. The endoplasmatic reticulum maintains a store of sequestered calcium through the action of an ATP-dependent calcium uptake mediated by the Ca2+, Mg(2+)-ATPase system present in the membrane of this organelle. The interaction of the amyloplast with the endoplasmic reticulum leads to the release of free calcium ions from the endoplasmic store. The increased free Ca2+ level in the cytoplasm may modify the activities of certain enzymes and receptor proteins. The gravitropic induction phase is completed when the lateral polarization of the tissues has taken place. These tissues contain information about changes in direction of the IAA transport system and in competition of the IAA-receptor system for the phytohormone. This information is fixed in "memory" and its expression is achieved when the lateral gradient of IAA concentration and of the activity of the IAA-receptor protein complexes is formed in the horizontally oriented plant organ. Flows of IAA and calcium ions in opposite directions may lead to the expression of laterally differentiated growth.

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BibTeXRIS

A Merkys, J Darginaviciene. 1997. Plant gravitropic response.. https://pubmed.ncbi.nlm.nih.gov/9048140/

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Ca(2+) Mg(2+)-ATPase↗

Expression of Mg2+-dependent, HCO3- -stimulated adenine triphosphatase in the human duodenum.

BACKGROUND AND AIM: Mg2+-dependent, HCO3- -stimulated adenine triphosphatase (Mg2+-HCO3- -ATPase) is an enzyme that catabolizes ATP in the presence of HCO3- and Mg2+. The activity of this ATPase is known to be present in the duodenum, but its physiological role remains unclear. In the present study, the aim was to study the distribution and biochemical profiles of Mg2+-HCO3- -ATPase in the human duodenum. METHODS: The histochemistry of Mg2+-HCO3- -ATPase, its localization using electron microscopy (EMS), and the measurement of enzyme activity were carried out by using mucosal samples of the bulb, and the second and third portions of the duodenum, obtained from six volunteers by endoscopic biopsy. RESULTS: The Mg2+-HCO3- -ATPase was detected in the brush border along the luminal surface of human duodenal epithelial cells. The EMS confirmed its localization to the surface of microvilli. The activity of Mg2+-HCO3- -ATPase was higher in the distal portions of the human duodenum than in the bulb. Its maximal activity was obtained under a pH of 8.5, and in the presence of 1.0 mmol/L MgCl2 and 50 mmol/L NaHCO3, but the activity was undetectable in pH <7.4 or >9.5. CONCLUSION: The results of the present study suggested that Mg2+-HCO3- -ATPase may work for luminal alkalization in the distal portions of the human duodenum and may contribute to maintaining the activity of pancreatic digestive enzymes.

Ca(2+) Mg(2+)-ATPase↗