Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nuclear localization serves as a regulatory mechanism in the activity of several transcription factors. KNOTTED-1 (Kn1) is a homeodomain protein likely to regulate vegetative development in maize. At least twelve genes related to Kn1 are known in maize and six in Arabidopsis. Ectopic expression of the maize, rice and Arabidopsis Kn1-related genes have been shown to alter cell fate determination. In this paper, we study the nuclear localization capabilities of the Kn1 homeodomain and the proximal amino acid residues (the ELK region) which is highly conserved among Kn1-related homeodomain proteins. The ELK homeodomain (ELK-HD) of Kn1 was fused to the reporter gene uidA encoding the bacterial enzyme beta-glucuronidase (GUS) and transformed into tobacco and onion cells. Quantitation of GUS activity in nuclear and total protein extracts from transgenic tobacco revealed a highly localized GUS activity in the nucleus for the ELK-HD/GUS fusion protein, as compared to the basal level of GUS activity in the nucleus for the GUS only protein. The ELK-HD/GUS transformants showed no unusual characteristics, thus indicating that expression of the putative Kn1 DNA-binding domain fused to GUS may be insufficient to create a dominant negative phenotype. Histochemical analysis of the onion epidermal cells transfected by particle bombardment demonstrated that greater than 50 % of the transformed onion epidermal cells showed higher levels of GUS staining in the nucleus relative to the cytoplasm. Deletion analysis of the ELK-HD revealed that the Kn1 homeodomain comprising the three predicted alpha-helices and the conserved ELK domain can each function independently as nuclear localization signals.
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PMID:The conserved ELK-homeodomain of KNOTTED-1 contains two regions that signal nuclear localization. 861 27

Metabolic acidosis induces net calcium efflux (JCa+) from cultured bone, in part, through an increase in osteoclastic resorption and a decrease in osteoblastic formation. In humans provision of base as potassium (K+) citrate, but not sodium (Na+) citrate, reduces urine Ca (UCa), and oral KHCO3 decreases bone resorption and UCa in postmenopausal women. Potassium deprivation alone leads to an increase in UCa. To determine whether decreased extracellular K+ concentration ([K+]) at a constant pH, PCO2, and [HCO-3] alters JCa+ and bone cell activity, we measured JCa+, osteoblastic collagen synthesis, and osteoclastic beta-glucuronidase release from neonatal mouse calvariae cultured for 48 h in medium of varying [K+]. Calvariae were cultured in control medium (approximately 4 mM [K+]) or medium with mildly low K+ (MLK, approximately 3 mM [K+]), very low K+ (VLK, approximately 2 mM [K+]), or extremely low K+ (ELK, approximately 1 mM [K+]) (n > or = 9 in each group). Compared with control, ELK, but not MLK or VLK, resulted in a marked increase in JCa+ and an increase in beta-glucuronidase release and a decrease in collagen synthesis. JCa+ was correlated directly with medium beta-glucuronidase activity and inversely with collagen synthesis. To determine whether the reduction in medium [K+] was associated with a decrease in intracellular pH (pHi), we measured pHi in MC3T3-E1 cells, a mouse osteoblastic cell line. Incubation in 1 mM [K+] led to a significant decrease in pHi compared with 3 mM [K+]. Thus incubation in a reduced [K+] medium stimulates JCa+ and osteoclastic enzyme release and inhibits osteoblastic collagen synthesis, which may be mediated by a reduction in bone cell pH.
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PMID:Decreased potassium stimulates bone resorption. 922 39