Disease relevance of PLDN

• One amino acid substitution in the PA gene, encoding a protein involved in virus RNA replication, and one amino acid substitution in the haemagglutinin (HA) protein were observed [1].
• Five factors were associated with a decrement in CrCl greater than the average decrease (17.6%): presence of hydronephrosis, age <50, no history of cisplatin treatment, a BED to gross adenopathy exceeding mean BED, and salvage treatment of PA node recurrence [2].

High impact information on PLDN

• Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteins [3].
• Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles [4].
• We show that pallidin is a ubiquitously expressed approximately 25 kDa protein found both in the cytosol and peripherally associated to membranes [4].
• Fibroblasts derived from the muted mouse strain exhibit reduced levels of pallidin, suggesting that the absence of the muted protein destabilizes pallidin [4].
• Human erythrocyte membrane protein band 4.2 (pallidin) [5].

Biological context of PLDN

• We also show that pallidin can be phosphorylated by a red-cell membrane kinase which partially co-purifies with it, and has properties similar to the catalytic subunit of cAMP-dependent kinase [6].
• Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2) [6].

Associations of PLDN with chemical compounds

• The inclusion compound formation between linear amylose of molecular weight 102500 (AS100) and p-aminobenzoic acid (PA) during the sealed-heating process was investigated by powder X-ray diffractometry, infrared spectroscopy and solid state NMR spectroscopy [7].
• It is found that the concentration of both AgNO3 and p-aminoazobenzene (PA) molecules has a significant effect on the formation and growth of these novel nanostructures [8].
• OBJECTIVE: To assess kidney function via creatinine clearance before and after radiotherapy in gynecologic cancer patients treated to the para-aortic (PA) area via Intensity Modulated Radiotherapy (IMRT) [2].
• The weight-average molecular weight of pallidin is 250 000 +/- 50 000 determined by equilibrium sedimentation in the presence of D-galactose compared to 100 000 +/- 2000 for discoidin [9].
• Pallidin has a subunit molecular weight of 24 800 +/- 1100 determined by polyacrylamide electrophoresis in the presence of dodecyl sulfate and 2-mercaptoethanol, compared to 26 100 +/- 1000 for discoidin [9].

Other interactions of PLDN

• Seven major erythrocyte membrane proteins, alpha-and beta-spectrin, ankyrin 2.1, band 3 (anion-exchanger), 4.1a and b, and 4.2 (pallidin), were separated and identified by SDS-CGE method [10].

Analytical, diagnostic and therapeutic context of PLDN

• NMR titration studies have also revealed that 3 binds to the CRD2 with a potency similar in magnitude to PA but much less potently than 1 [11].

References