Disease relevance of PKD2L1

• There is no evidence of linkage to PKDL in six ADPKD families that are unlinked to PKD1 or PKD2 [1].
• Polycystin-L (PCL) shares high homology with polycystin-2, the product of polycystic kidney disease gene-2 [2].
• PKD2L is localized to chromosome 10q25 and is excluded as a candidate gene for autosomal recessive polycystic kidney disease, autosomal dominant polycystic liver disease, and the third form of ADPKD [3].
• In both cities, a suggestive relationship of radiation dose to cirrhosis prevalence, but not to PCL prevalence, was noted [4].
• To confirm these observations, we transfected HBsAg-positive (PCL/PRF/5) and HBsAg-negative (HepG2) transformed liver cell lines with a plasmid containing a hepatitis delta virus cDNA trimer under the control of the SV40 early enhancer/promoter sequences [5].

Psychiatry related information on PKD2L1

• They were assessed using the Posttraumatic Stress Disorder Checklist (PCL), the General Health Questionnaire-28 (GHQ-28), and the Multidimensional Health Locus of Control (MHLC) [6].
• The questionnaire included the General Health Questionnaire (GHQ-12), the post-traumatic stress disorder checklist (PCL), 15 symptoms and an assessment of alcohol intake [7].
• Instruments included demographic data, the computer-based algorithmic Quick Diagnostic Interview Schedule Symptom, and three symptom checklists, one each for substance related problems (MAST/AD), anxiety and depressive symptoms (BSI-57), and combat-related post-trauma symptoms (PCL/M) [8].

High impact information on PKD2L1

• These results suggest that PKD1L3 and PKD2L1 heteromers may function as sour taste receptors [9].
• The specificity of the interaction was demonstrated by the fact that PKD2L, a protein closely related to PKD2, failed to interact with Hax-1 [10].
• The murine PKD2L1 gene comprises 15 exons in chromosome 19C3 [11].
• Mutagenesis within two newly identified ER retention signal-like amino acid sequences caused PKD2L1 to be expressed at the cell surface [11].
• The full-length transcript of PKDL is expressed at high levels in fetal tissues, including kidney and liver, and down-regulated in adult tissues [1].

Biological context of PKD2L1

• We show that PKDL has 16 exons [12].
• Elucidation of the gene structure, exact location, and alternative splicing patterns of PKDL will facilitate its evaluation as a candidate gene in cystic or other genetic disorders [12].
• The positions of introns and the sizes of exons in the PKDL gene are very similar to those of PKD2, except for the last two 3' end exons [12].
• Whilst the predicted protein domain structure of polycystin-1 suggests it is involved in cell-cell or cell-matrix interactions, the similarity of polycystin-2 and polycystin-L to the pore-forming domains of some cation channels suggests that they all form subunits of a large plasma membrane ion channel [13].
• Further analysis revealed one novel gene, PKD2L2, located on chromosome band 5q31, and two recently described genes, PKD2L and PKDREJ, located on chromosome bands 10q31 and 22q13.3, respectively [14].

Anatomical context of PKD2L1

• In the present study, we expressed human PCL in Xenopus oocytes and studied its function utilizing patch-clamp and two-electrode voltage clamp techniques [15].
• Reciprocal co-immunoprecipitation experiments demonstrated that PCL physically associates with the skeletal and cardiac troponin I isoforms in overexpressed Xenopus oocytes and mouse fibroblast NIH 3T3 cells [16].
• PKD2L is expressed in adult heart and skeletal muscle, brain, spleen, testis, and retina, and alternative transcripts of 2.4, 2.7, and 3.0 kb are seen [3].
• The anatomy of the meniscofemoral ligaments (ligaments of Wrisberg and Humphrey) reveals the intimate relationship among the PCL, the popliteus muscle, and the lateral meniscus [17].
• When TDI/PCL/ED was incubated with commercial elastase in vitro, a significant release of radiolabel was found which was comparable to the amount of radiolabelled material released from this polymer in contact with the neutrophils in culture [18].

Associations of PKD2L1 with chemical compounds

• In addition to its permeability to Ca2+, K+ and Na+, PCL was highly permeable to NH4+ and Cs+ with a permeability ratio NH4+:Cs+:Na+ of 2.2:1.02:1 [15].
• We found that PCL is permeable to organic amines, methlyamine (MA, 3.8 A), dimethylamine (DMA, 4.6 A) and triethylamine (TriEA, 6 A), and to tetra-alkylammonium cation (TAA) tetra-methylammonium (TMA, 5.5-6.4 A) [19].
• PURPOSE: This study aims at developing poly(ethylene oxide)-modified poly(epsilon-caprolactone) (PEO-PCL) nanoparticulate system as an intracellular delivery vehicle for saquinavir, an anti-HIV protease inhibitor [20].
• Poly (epsilon-caprolactone-co-alpha-iodo-epsilon-caprolactone) was synthesized by binding iodine to PCL chain bearing carbanionic site on alpha-position of carbonyl groups using lithium diisopropylamide [21].
• Methoxy poly(ethylene glycol) (MPEG)/poly(epsilon-caprolactone) (PCL) diblock copolymers were synthesized by the ring-opening polymerizatrion of epsilon-caprolactone in the presence of a catalyst-free MPEG homopolymer [22].

Other interactions of PKD2L1

• PKD2L2 and PKD2L, which encode proteins of 613 and 805 amino acids, are approximately 65% similar to polycystin-2 [14].
• Polycystin-1 and -2 are mutated in autosomal dominant polycystic kidney disease, but the physiological role of PCL has not been determined [19].

Analytical, diagnostic and therapeutic context of PKD2L1

• PKDL was assigned to 10q24 by fluorescence in situ hybridization and is linked to D10S603 by radiation hybrid mapping [1].
• RT-PCR demonstrates the existence of at least three polycystin-L splice variants: PKDL(Delta5), PKDL(Delta456), and PKDL(Delta15) that are expressed in a tissue-specific manner [12].
• Channel activity was substantially increased when either the extracellular or intracellular calcium-ion concentration was raised, indicating that polycystin-L may act as a transducer of calcium-mediated signalling in vivo [23].
• As the rat appears to be a valuable model for investigating polycystic kidney disease, the characterization of the rat Pkdl gene will help facilitate future studies to elucidate the molecular mechanisms of cystogenesis in this animal model [24].
• In this study, an anti-peptide polyclonal antiserum was generated against the carboxyl terminal domain of human PCL and used to determine the patterns of expression and distribution of PCL by indirect immunofluorescence in both developing and adult mice [25].

References