Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the gastrocnemius muscle of cat and rat, staining for oxidative enzymes differentiated three fiber types (A,B,C) and staining for adenosine triphosphate at pH 9.4 differentiated two fiber types (I, II) with a reliability of 90% and 98%, respectively. In cat 96% and in rat 90% of the fibers were typed identically after staining for nicotinamide adenine dinucleotidelinked lactic dehydrogenase (LDH) and succinic dehydrogenase (SDH). When differentiated by staining for LDH, A and B fibers were of type I. IN RAT, 80-90% OF ALL FIBERS WERE OF TYPE 22, COMPPRISING A, B and C fibers. Type I fibers stained for LDH intensely as did C fibers of type II, but stained intermediately for SDH. The degree of staining was measured by photometry. When fibers were stained for LDH, histograms of density showed three peaks corresponding to A, B and C fibers in cat, but only two peaks corresponding to A and C fibers in rat, In cat and rat, the densities of A, B and C fibers belonged to different populations. In soleus muscle of cat and rat stained for LDH, menadione-linked alpha-glycerophosphate dehydrogenase and adenosine triphosphatase at pH 9.4, the degree of staining differed from thatin any type of fiber in gastrocnemius muscle
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PMID:Histochemical fiber typing and staining intensity in cat and rat muscles. 12 97

IN DORSAL ROOT GANGLIA AND PERIPHERAL NERVE OF THE RAT AND OTHER SPECIES, NUCLEOSIDE PHOSPHATASE AND UNSPECIFIC CHOLINESTERASE REACTION PRODUCTS ARE FOUND IN THE PLASMA MEMBRANES AND SPACES BETWEEN THEM AT TWO SITES: (1) Schwann cell-axon interfaces and mesaxons of unmyelinated fibers, and (2) sheath cell-perikaryon interfaces and interfaces between adjacent sheath cells. Acetylcholinesterase reaction product is found in the perikaryon (within the endoplasmic reticulum) and the axon (axoplasmic surface). Nucleoside phosphatase reaction product is also found in the numerous vacuoles at the surface of perineurium cells, ganglion sheath cells, and cells surrounding some ganglion blood vessels. Nucleoside phosphatase activities in the sections fail to respond, in the manner described for "transport ATPase," to diisopropylphosphofluoridate, sodium and potassium ions, and ouabain. Nucleoside diphosphates are hydrolyzed more slowly than triphosphates in unmyelinated fibers, and are not hydrolyzed at the perikaryon surface. Nucleoside monophosphates are either not hydrolyzed or hydrolyzed very slowly. In contrast to these localizations, which are believed to demonstrate sites of enzyme activity, it is considered likely that diffusion artifacts account for the nucleoside phosphatase reaction product frequently found along the outer surfaces of myelinated fibers and within vacuoles at the Schwann cell surfaces of these fibers. The diffuse reaction product seen in basement membranes of ganglion and nerve may also be artifact.
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PMID:Nucleoside phosphatase and cholinesterase activities in dorsal root ganglia and peripheral nerve. 422 92

In an increasing number of plant-microbe interactions, it has become evident that the abundance of immunity-related proteins is controlled by the ubiquitin-26S proteasome system. In the interaction of barley with the biotrophic barley powdery mildew fungus Blumeria graminis f.sp. hordei (Bgh), the RAC/ROP [RAT SARCOMA-related C3 botulinum toxin substrate/RAT SARCOMA HOMOLOGUE (RHO) of plants] guanosine triphosphatase (GTPase) HvRACB supports the fungus in a compatible interaction. By contrast, barley HvRBK1, a ROP-binding receptor-like cytoplasmic kinase that interacts with and can be activated by constitutively activated HvRACB, limits fungal infection success. We have identified a barley type II S-phase kinase 1-associated (SKP1)-like protein (HvSKP1-like) as a molecular interactor of HvRBK1. SKP1 proteins are subunits of the SKP1-cullin 1-F-box (SCF)-E3 ubiquitin ligase complex that acts in the specific recognition and ubiquitination of protein substrates for subsequent proteasomal degradation. Transient induced gene silencing of either HvSKP1-like or HvRBK1 increased protein abundance of constitutively activated HvRACB in barley epidermal cells, whereas abundance of dominant negative RACB only weakly increased. In addition, silencing of HvSKP1-like enhanced the susceptibility of barley to haustorium establishment by Bgh. In summary, our results suggest that HvSKP1-like, together with HvRBK1, controls the abundance of HvRACB and, at the same time, modulates the outcome of the barley-Bgh interaction. A possible feedback mechanism from RAC/ROP-activated HvRBK1 on the susceptibility factor HvRACB is discussed.
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PMID:A barley SKP1-like protein controls abundance of the susceptibility factor RACB and influences the interaction of barley with the barley powdery mildew fungus. 2589 38