pH Homeostasis (ph + homeostasi)

Distribution by Scientific Domains

Kinds of pH Homeostasis

  • intracellular ph homeostasi


  • Selected Abstracts


    Protein Kinase C Regulation of Rat Jejunal Transport Systems: Mechanisms Involved in Lactate Movement

    EXPERIMENTAL PHYSIOLOGY, Issue 6 2002
    Marisa Tosco
    We examined whether protein kinase C (PKC) modulates the transport systems involved in lactate movements across the plasma membranes of rat jejunum. In vitro phosphorylated membrane vesicles were used to perform uptake studies, the results of which suggested that PKC activation exerts an inhibitory effect on basolateral H+ -lactate symport, as well as on apical Na+ -glucose cotransport. The specificity of the response to PKC was confirmed by using staurosporine, chelerythrine or 4-,-PMA. Experiments performed using the whole tissue incubated in vitro confirmed the reduction of lactate transport elicited by PKC and gave evidence for an associated inhibition of fluid transport. Na+,K+ -ATPase activity seems to be unaffected by the kinase and inhibited by Ca2+. Taken together, our results suggest that the overall action of PKC results from the simultananeous modulation of multiple pathways, targeted to a reduction of both lactate and bicarbonate transports without altering cell pH homeostasis. [source]


    Intracellular pH homeostasis in the filamentous fungus Aspergillus niger

    FEBS JOURNAL, Issue 14 2002
    Stephan J. A. Hesse
    Intracellular pH homeostasis in the filamentous fungus Aspergillus niger was measured in real time by 31P NMR during perfusion in the NMR tube of fungal biomass immobilized in Ca2+ -alginate beads. The fungus maintained constant cytoplasmic pH (pHcyt) and vacuolar pH (pHvac) values of 7.6 and 6.2, respectively, when the extracellular pH (pHex) was varied between 1.5 and 7.0 in the presence of citrate. Intracellular metabolism did not collapse until a ,pH over the cytoplasmic membrane of 6.6,6.7 was reached (pHex 0.7,0.8). Maintenance of these large pH differences was possible without increased respiration compared to pHex 5.8. Perfusion in the presence of various hexoses and pentoses (pHex 5.8) revealed that the magnitude of ,pH values over the cytoplasmic and vacuolar membrane could be linked to the carbon catabolite repressing properties of the carbon source. Also, larger ,pH values coincided with a higher degree of respiration and increased accumulation of polyphosphate. Addition of protonophore (carbonyl cyanide m -chlorophenylhydrazone, CCCP) to the perfusion buffer led to decreased ATP levels, increased respiration and a partial (1 µm CCCP), transient (2 µm CCCP) or permanent (10 µm CCCP) collapse of the vacuolar membrane ,pH. Nonlethal levels of the metabolic inhibitor azide (N3,, 0.1 mm) caused a transient decrease in pHcyt that was closely paralleled by a transient vacuolar acidification. Vacuolar H+ influx in response to cytoplasmic acidification, also observed during extreme medium acidification, indicates a role in pH homeostasis for this organelle. Finally, 31P NMR spectra of citric acid producing A. niger mycelium showed that despite a combination of low pHex (1.8) and a high acid-secreting capacity, pHcyt and pHvac values were still well maintained (pH 7.5 and 6.4, respectively). [source]


    pH and carbon supply control the expression of phosphoenolpyruvate carboxylase kinase genes in Arabidopsis thaliana

    PLANT CELL & ENVIRONMENT, Issue 12 2008
    ZHI-HUI CHEN
    ABSTRACT Phosphoenolpyruvate carboxylase (PEPC) is thought to play many roles in C3 plants including the provision of biosynthetic precursors and control of pH during N assimilation. Its activity is controlled via phosphorylation catalysed by PEPC kinases, which are encoded by PPCK genes. We examined PPCK expression in response to changes in the supply of N or C, and to changes in intracellular pH, using cultured Arabidopsis cells and seedlings. The results show that expression of both PPCK1 and PPCK2 is increased by C availability, but does not respond to N availability. Expression of the two PPCK genes and the phosphorylation state of PEPC are increased in response to increasing intracellular pH. Elevated pH also reduces the repression of PPCK gene expression by Pi. Expression of phosphoenolpyruvate carboxykinase (PEPCK), which catalyses the decarboxylation of oxaloacetate, is decreased in response to increasing intracellular pH. pH homeostasis may be mediated at least partly by reciprocal changes in the expression of PPCK genes and PEPCK. [source]


    The Shigella dysenteriae serotype 1 proteome, profiled in the host intestinal environment, reveals major metabolic modifications and increased expression of invasive proteins

    PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 22 2009
    Rembert Pieper
    Abstract Shigella dysenteriae serotype 1 (SD1) causes the most severe form of epidemic bacillary dysentery. We present the first comprehensive proteome analysis of this pathogen, profiling proteins from bacteria cultured in vitro and bacterial isolates from the large bowel of infected gnotobiotic piglets (in vivo). Overall, 1061 distinct gene products were identified. Differential display analysis revealed that SD1 cells switched to an anaerobic energy metabolism in vivo. High in vivo abundances of amino acid decarboxylases (GadB and AdiA) which enhance pH homeostasis in the cytoplasm and protein disaggregation chaperones (HdeA, HdeB and ClpB) were indicative of a coordinated bacterial survival response to acid stress. Several type III secretion system effectors were increased in abundance in vivo, including OspF, IpaC and IpaD. These proteins are implicated in invasion of colonocytes and subversion of the host immune response in S. flexneri. These observations likely reflect an adaptive response of SD1 to the hostile host environment. Seven proteins, among them the type III secretion system effectors OspC2 and IpaB, were detected as antigens in Western blots using piglet antisera. The outer membrane protein OmpA, the heat shock protein HtpG and OspC2 represent novel SD1 subunit vaccine candidates and drug targets. [source]


    The effect of low pH on protein expression by the probiotic bacterium Lactobacillus reuteri

    PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 8 2008
    KiBeom Lee Dr.
    Abstract The ability of a lactic acid bacterium to survive passage through the gastrointestinal tract is a key point in its function as a probiotic. In this study, protein synthesis by the probiotic bacterium, Lactobacillus reuteri, was analyzed under transiently decreased pH conditions. L. reuteri cells grown to the midexponential growth phase at 37°C were exposed to transient (1,h) low-pH stresses from pH,6.8 to pH,5.0, 4.5, or 4.0. 2-DE allowed us to identify 40 common proteins that were consistently and significantly altered under all three low-pH conditions. PMF was used to identify these 40 proteins, and functional annotation allowed them to be distributed to six major classes: (i) transport and binding proteins; (ii) transcription,translation; (iii) nucleotide metabolism and amino acid biosynthesis; (iv) carbon energy metabolism; (v) pH homeostasis and stress; and (vi) unassigned. These findings provide new insight into the inducible mechanisms underlying the capacity of gastrointestinal L. reuteri to tolerate acid stress. [source]


    The Role of Acidocalcisomes in Parasitic Protists,

    THE JOURNAL OF EUKARYOTIC MICROBIOLOGY, Issue 3 2009
    SILVIA N. J. MORENO
    ABSTRACT. Acidocalcisomes are acidic organelles with a high concentration of phosphorus present as pyrophosphate (PPi) and polyphosphate (poly P) complexed with calcium and other cations. The acidocalcisome membrane contains a number of pumps (Ca2+ -ATPase, V-H+ -ATPase, H+ -PPase), exchangers (Na+/H+, Ca2+/H+), and channels (aquaporins), while its matrix contains enzymes related to PPi and poly P metabolism. Acidocalcisomes have been observed in pathogenic, as well as non-pathogenic prokaryotes and eukaryotes, e.g. Chlamydomonas reinhardtii, and Dictyostelium discoideum. Some of the potential functions of the acidocalcisome are the storage of cations and phosphorus, the participation of phosphorus in PPi and poly P metabolism, calcium homeostasis, maintenance of intracellular pH homeostasis, and osmoregulation. In addition, acidocalcisomes resemble lysosome-related organelles (LRO) from mammalian cells in many of their properties. For example, we found that platelet dense granules, which are LROs, are very similar to acidocalcisomes. They share a similar size, acidic properties, and both contain PPi, poly P, and calcium. Recent work that indicates that they also share the system for targeting of their membrane proteins through adaptor protein 3 reinforces this concept. The fact that acidocalcisomes interact with other organelles in parasitic protists, e.g. the contractile vacuole in Trypanosoma cruzi, and other vacuoles observed in Toxoplasma gondii, suggests that these cellular compartments may be associated with the endosomal/lysosomal pathway. [source]


    Essential role of the V-ATPase in male gametophyte development

    THE PLANT JOURNAL, Issue 1 2005
    Jan Dettmer
    Summary Intracellular pH homeostasis is a prerequisite for biological processes and requires the action of proton pumps. The vacuolar H+ -ATPase (V-ATPase) is involved in regulating pH in endomembrane compartments of all eukaryotic cells. In plants, there is an additional endomembrane proton pump, H+ -pyrophosphatase (H+ -PPase). However, the relative roles of the two types of pumps in endomembrane acidification and energization of secondary active transport are unclear. Here, we show that a strong T-DNA insertion allele of VHA-A, the single copy gene encoding the catalytic subunit of the Arabidopsis V-ATPase, causes complete male and partial female gametophytic lethality. Severe changes in the morphology of Golgi stacks and Golgi-derived vesicles in male gametophytes are the first visible symptoms of cell degeneration leading to a failure to develop mature pollen. Similar effects on Golgi morphology were observed in pollen tubes when growth was blocked by Concanamycin A, a specific V-ATPase inhibitor. Taken together, our results suggests that V-ATPase function is essential for Golgi organization and development of the male gametophyte. [source]