Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.3.1 (Mg2+-ATPase)
 1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Membrane fractions enriched in sarcoplasmic reticulum (SR) were isolated from the cardiac ventricles of 10-month-old, stroke-prone spontaneously hypertensive rats (SHRSP) which had been maintained for nine months on one of four experimental diets: low protein (LP) (19% protein), standard (STD) (24% protein), high protein (HP) (32% protein), or high methionine (1.9% methionine) (MET). ATPase activities, as well as ATP-dependent Ca2+ binding and Ca2+-uptake activities, of the isolated SR were determined to examine the influence of diet on myocardial Ca2+-pump activity. SR from all four groups exhibited similar Mg2+-ATPase activity. However, the (Ca2+ + Mg2+)-ATPase activity was significantly elevated in SR from rats on the MET diet while the activity in the other groups showed no significant differences. After 15 sec of incubation, Ca2+-uptake (presence of oxalate) in SR from the LP group was significantly less than Ca2+-uptake in SR from each of the three other diet groups. Ca2+ binding (absence of oxalate) in the SR from the LP group was also significantly less than that from each of the three other diet groups. Kinetic analysis of SR Ca2+-uptake over 60 sec revealed that the Bmax of the MET group was significantly higher than Bmax of the STD diet group. In addition, the Bmax of the LP group was significantly lower than Bmax of the HP and MET groups. There was no significant difference in affinity of the SR Ca2+-uptake system among the four diet groups. These results indicate that modification of dietary protein can influence myocardial SR Ca2+-pump function.
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PMID:ATP-dependent calcium uptake in myocardial sarcoplasmic reticulum from spontaneously hypertensive rats: effect of modification of dietary protein. 293 82

Cancer is a leading cause of mortality and morbidity globally. Many prominent cancer-associated molecules have been identified over the recent years which include EGFR, CD44, TGFbRII, HER2, miR-497, NMP22, BTA, Fibrin/FDP etc. These biomarkers are often used for screening, detection, diagnosis, prognosis, prediction and monitoring of cancer development. Phosphatidylserine (PS) is an essential component in all human cells which is present on the inner leaflet of the cell membrane. The oxidative stress causes exposure of PS on the surface of the vascular endothelium in the cancer cells (lung, breast, pancreatic, bladder, skin, brain metastasis, rectal adenocarcinoma etc.) but not on the normal cells. The external PS is regulated by calcium-dependent flippase activity. Cancer cell lines with high surface PS have low flippase activity and high intracellular calcium content. Human Annexin-V, PS targeting antibodies (PGN635 and bavituximab and mch1N11), lysosomal protein, phospholipid Saposin C dioleoylphosphatidylserine (SapC-DOPS), peptide-peptoid hybrid PPS1, PS-binding 14-mer peptide (PSBP-6) and hexapeptide (E3) have been reported to target PS present on cancer cell surface. High expression of CD47 inhibits tumor cell phagocytosis by macrophages. The PS cancer biomarker has also been used to target the drugs to cancer cells specifically without affecting other healthy cells. Currently, the fusion protein (FP) consisting of L-methionase linked to human Annexin-V has been reported to target the cancer cells. The FP catalyzes the conversion of non-toxic prodrug selenomethionine into toxic methyl selenol which thus also prevents the methionine (essential amino acid) supplementation to the cancer cells.
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PMID:Phosphatidylserine: A cancer cell targeting biomarker. 2887 Aug 43