Disease relevance of P11

• This study suggests that these proteins, especially PP5 and PP11, may be useful as markers in monitoring patients with ovarian adenocarcinomas as well as for their early diagnosis [1].
• In serous cystadenocarcinomas, SP1 was present in 35.0% of cases, PP5 in 76.2%, PP10 in 9.5%, PP11 in 57.1% and PP12 in 23.8% [1].
• In mucinous cystadenocarcinomas, SP1, was present in 53.3% of cases, PP5 in 80.0%, PP10 in 20.0%, PP11 in 66.7% and PP12 in 46.7% [1].
• We identified an optimal antigenic undecapeptide from the cytomegalovirus gB protein that could form stable HLA-A2 complexes that contained apparent anchor residues at P2 and P11 (sequence FIAGN-SAYEYV), indicating that the spacing between anchor residues can be somewhat variable [2].
• In this in vitro study the effects of a range of concentrations (2-10 microg/ml) of sodium selenite were investigated in one low-passage culture of biopsy-derived glioma cells (IPSB-18, an anaplastic astrocytoma, P 18-22) and a normal human brain cell culture (CC2565, P11) [3].

High impact information on P11

• Sequence analysis of a full-length cDNA for Tcl-30 reveals a potential open reading frame of 454 amino acids that shares sequence identity to a human placental-specific protein of unknown function, PP11 [4].
• Prolonged administration of DEXA (P1-P11) reduced selectively the area and thickness of the outer medulla and the number of PCNA-positive cells [5].
• Redistribution of the labeled terminals closely paralleled the fEPSP distribution, being present in the ventrolateral spinal cord at P7, decreased at P8, further deceased at P10, but unchanged at P11 [6].
• Based on EcoRI plasmid profiles (PP), two types, PP-11 and PP-13, were highly stable over time and were consistently associated with multidrug-sensitive strains recovered from outpatients treated at Native American community clinics [7].
• The peptides S4 from R2 (53%) and P11 from R0 (49%) were identified as immunodominant B cell epitopes and induced higher levels of antibodies [8].

Biological context of P11

• Spontaneous and evoked Ca2+ action potentials (APs) were present in control IHCs from P3-P11 rats and vanished in parallel with the expression of a rapidly activating Ca2+- and voltage-activated K+ (BK) conductance [9].

Anatomical context of P11

• The extrapolation of afferent conduction velocity (CV) measured from sensory nerve potentials along the peripheral nerve to the C6-C7 spinal segments identified the spinal entry time with the onset of the neck N11 or scalp P11 (far field 2 or FF2) [10].
• The syncytiotrophoblast of villi showed clear positive stainings for SP1, PP8, PP9, and PP11, whereas the cytotrophoblast (villi) was found to show clear positive staining for PP9 only [11].
• The peptide sequence shares high homology with human placental protein 11 (PP11) and mouse T-cell specific protein (Tcl-30), which both contain a single somatomedin B-like domain [12].
• In addition, stains for PP8, PP10, and PP12 were taken up by the cytoplasm of histiocytes found in amnion, villi, the intervillous space, and decidua, in contrast to PP11, which was found to be specific to the cytoplasm of trophoblast cells (chorion and villi) [13].

Associations of P11 with chemical compounds

• The use of a 30/70 mixture of trichlorofluoromethane (P11) and dichlorodifluoromethane (P12) resulted in the formation of stable, isotropic systems containing 0.5-2.0% (w/v) SPC and solubilized water; R (moles water/moles SPC), 0.9 to 4.28 [14].
• The rheological profiles of lactose in chloroform, lactose in trichlorofluoromethane (Propellent 11, P11), and salbutamol sulphate in P11 have been investigated in the presence and absence of lecithin, a phospholipid surface-active agent [15].
• A tyrosine residue in the P11 region of serpin, which is conserved in the S11 regions of all known proPOs maturation sites, provides further support for this hypothesis [16].
• Since PP11 has serine protease activity, it is predicted that its teleost homologue, PPSB, may function as a pancreatic digestive enzyme [12].
• By using an immunoglobulin enzyme bridge (PAP) technique, the location of two ubiquitous tissue proteins (PP8, PP9) and three placental specific tissue proteins (PP10, PP11, PP12) was investigated in ethanol/acetic acid-fixed paraffin-embedded human term placentae [13].

References