scholarly journals Role of Carboxylic Group on Feeding Repellence of Acidic Amino Acids and Organic Acids for Oriental Weatherfish

1989 ◽  
Vol 55 (5) ◽  
pp. 927-927 ◽  
Author(s):  
Katsuhiko Harada
2008 ◽  
Vol 132 (6) ◽  
pp. 681-692 ◽  
Author(s):  
Qinghuan Xiao ◽  
Andrew Prussia ◽  
Kuai Yu ◽  
Yuan-yuan Cui ◽  
H. Criss Hartzell

Human bestrophin-1 (hBest1), which is genetically linked to several kinds of retinopathy and macular degeneration in both humans and dogs, is the founding member of a family of Cl− ion channels that are activated by intracellular Ca2+. At present, the structures and mechanisms responsible for Ca2+ sensing remain unknown. Here, we have used a combination of molecular modeling, density functional–binding energy calculations, mutagenesis, and patch clamp to identify the regions of hBest1 involved in Ca2+ sensing. We identified a cluster of a five contiguous acidic amino acids in the C terminus immediately after the last transmembrane domain, followed by an EF hand and another regulatory domain that are essential for Ca2+ sensing by hBest1. The cluster of five amino acids (293–308) is crucial for normal channel gating by Ca2+ because all but two of the 35 mutations we made in this region rendered the channel incapable of being activated by Ca2+. Using homology models built on the crystal structure of calmodulin (CaM), an EF hand (EF1) was identified in hBest1. EF1 was predicted to bind Ca2+ with a slightly higher affinity than the third EF hand of CaM and lower affinity than the second EF hand of troponin C. As predicted by the model, the D312G mutation in the putative Ca2+-binding loop (312–323) reduced the apparent Ca2+ affinity by 20-fold. In addition, the D312G and D323N mutations abolished Ca2+-dependent rundown of the current. Furthermore, analysis of truncation mutants of hBest1 identified a domain adjacent to EF1 that is rich in acidic amino acids (350–390) that is required for Ca2+ activation and plays a role in current rundown. These experiments identify a region of hBest1 (312–323) that is involved in the gating of hBest1 by Ca2+ and suggest a model in which Ca2+ binding to EF1 activates the channel in a process that requires the acidic domain (293–308) and another regulatory domain (350–390). Many of the ∼100 disease-causing mutations in hBest1 are located in this region that we have implicated in Ca2+ sensing, suggesting that these mutations disrupt hBest1 channel gating by Ca2+.


2015 ◽  
Vol 52 (4) ◽  
pp. 470
Author(s):  
Hamed M. Shatla ◽  
Hoda Y. Tomoum ◽  
Solaf M. Elsayed ◽  
Iman A. Elagouza ◽  
Rania H. Shatla ◽  
...  

2014 ◽  
Vol 51 (6) ◽  
pp. 820-825 ◽  
Author(s):  
Hamed M. Shatla ◽  
Hoda Y. Tomoum ◽  
Solaf M. Elsayed ◽  
Iman A. Elagouza ◽  
Rania H. Shatla ◽  
...  

2003 ◽  
Vol 179 (3) ◽  
pp. 151-159 ◽  
Author(s):  
Avinash Sonawane ◽  
Ute Klöppner ◽  
Christian Derst ◽  
Klaus-Heinrich Röhm

2019 ◽  
Vol 52 (2) ◽  
Author(s):  
Naeem Khan ◽  
Shahid Ali ◽  
Peiman Zandi ◽  
Asif Mehmood ◽  
Shariat Ullah ◽  
...  

1981 ◽  
Vol 59 (12) ◽  
pp. 2550-2557 ◽  
Author(s):  
Monica Madore ◽  
John A. Webb

To determine the role of the apoplast in the loading of the minor veins of Cucurbita pepo L., leaves were examined either for the ability to release selectively the transport sugars, sucrose and stachyose, from the metabolic space (MS) to the free space (FS) or to accumulate selectively exogenously fed transport sugars from the FS into the minor veins. FS extracts collected by vacuum infiltration and centrifugation of specially trimmed leaves were found to contain all sugars also present in ethanol extracts of the MS of the same leaves, but in amounts two orders of magnitude lower. Similarly, 14C activity in FS extracts from 14CO2-labelled leaves, which was distributed between all sugars, amino acids, and organic acids also found labelled in the MS, was nearly three orders of magnitude lower than in MS ethanol extracts. No excess of the transport sugars was evident in FS extracts. When 14C-labelled sucrose, stachyose, or galactose (all 1–2 mM) were infiltrated into the FS a rapid accumulation of these sugars into the mesophyll was apparent, as all sugars were rapidly interconverted into the various sugars normally found labelled in the MS after exposure of leaves to 14CO2. However, while leaves exposed to 14CO2 translocated label predominantly in the form of [14C]stachyose, label in exogenously fed leaves was translocated predominantly as [14C]sucrose, irrespective of the nature of the fed sugar. Exogenously fed transport sugars did not therefore appear to be taken up directly into the minor veins from the FS.The absence of significant levels of transport sugars in the FS as well as the failure of C. pepo leaves to load any appreciable amount of exogenously supplied [14C]stachyose, the predominant transport sugar in this species, would tend to preclude both a selective release of transport sugars into the apoplast and a selective uptake of transport sugars from the apoplast into the minor veins. A completely symplastic pathway for minor vein loading in C. pepo leaves therefore remains a possibility.


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