PDLIM5 antibody - middle region (ARP34273_T100)
- Known as:
- PDLIM5 (anti-) - middle region (ARP34273_T100)
- Catalog number:
- arp34273_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- PDLIM5 antibody - middle region (ARP34273_T100)
Related genes to: PDLIM5 antibody - middle region (ARP34273_T100)
- Gene:
- PDLIM5 NIH gene
- Name:
- PDZ and LIM domain 5
- Previous symbol:
- -
- Synonyms:
- LIM, Enh
- Chromosome:
- 4q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-12
- Date modifiied:
- 2016-10-05
Related products to: PDLIM5 antibody - middle region (ARP34273_T100)
Related articles to: PDLIM5 antibody - middle region (ARP34273_T100)
- Cerebral amyloid angiopathy (CAA) is a cerebrovascular disorder characterized by the deposition of amyloid-β (Aβ) in the walls of leptomeningeal and cortical blood vessels that increases risk of intracerebral hemorrhages and progressive cognitive decline. More than 90% of individuals with Alzheimer's disease (AD) exhibit some level of CAA. Notably, in the new era of disease-modifying treatments for AD, CAA is a significant risk factor for amyloid-related imaging abnormalities (ARIA), an adverse event associated with anti-amyloid treatments. Therefore, there is great need for accessible, reliable and accurate in vivo biomarkers (e.g., blood-based) to improve antemortem identification of CAA that would improve risk stratification and reduce symptomatic ARIA. In this study, we employed the Nucleic Acid-Linked Immuno-Sandwich Assay (NULISA™) central nervous system panel for exploratory biomarker quantification in antemortem plasma of participants with neuropathological assessments for CAA from the Banner Sun Health Research Institute Brain and Body Donation Program (N = 251) and independently validated in the University of California Irvine Alzheimer Disease Research Center cohort (N = 110). We evaluated the differential protein expression in antemortem plasma sample taken < 5 years (mean 1.76 ± 1.3) from death using a logistic regression model. We further compared multi-biomarker models and found that a combination of CRP, IL4, CCL11, NPY and PDLIM5, plus demographic covariates showed an area under the curve (AUC) of 0.90 (95% CI 0.86-0.94) to identify neuropathologically confirmed CAA in the discovery cohort. In our independent replication, the antemortem plasma signature performed better than the basic demographics model showing a potential to predict CAA. The exploration and validation in antemortem plasma indicate that a multi-analyte panel, when combined with in vivo blood biomarkers for AD pathology, may be capable of identifying the presence of CAA and could have an meaningful impact on the clinical evaluation of patients under the investigation for cognitive decline. Further developments in biomarkers for this condition are crucial so that CAA identification could inform treatment decisions by highlighting ARIA risk. - Source: PubMed
Publication date: 2026/05/20
Singh AlpanaDenkinger Marisa NLeuzy AntoineDieckhoff KariLiu JameMarques Taina MMonuki EdwinStark CraigGrill Joshua DHom ChristySultzer DavidDoran EricLott IraWood KevinGawronski BriannaGonzalez LourdesChoudhury ParichitaAtri AlirezaBeach Thomas GSerrano Geidy ESajjadi S AhmadVan Keuren-Jensen KendallReiman Eric MHead ElizabethAshton Nicholas J - Bipolar disorder (BD) exhibits significant sex differences in its frequency, symptom presentation, and treatment response, suggesting distinct underlying neurobiological mechanisms. However, transcriptomic studies investigating these sex-specific pathways have been fragmented and underpowered. - Source: PubMed
Publication date: 2026/05/08
Davarinejad OmranMoradi Mohammad-TaherSafarzadeh ArashJalalvand MasumehKazemisafa Fatemeh - Intracellular calcium (Ca) signaling controls myoblast proliferation, fusion, and myofiber formation. In myoblasts, Transient Receptor Potential Canonical (TRPC) channels, with TRPC1 as a predominant isoform, mediate store-operated Ca²⁺ entry (SOCE) and are essential for myogenesis. PDLIM5 (ENH1), a PDZ-LIM scaffold protein, organizes signaling events, including ion channel regulation and transcriptional control in muscles. This study aims to test the hypothesis that PDLIM5 regulates TRPC1-mediated Ca entry in myoblasts. Thapsigargin-induced SOCE was suppressed by the SOCE inhibitors Gd and 2-APB, as well as by TRPC1 siRNA, supporting the involvement of TRPC1 in SOCE in C2C12 myoblasts. Additionally, SOCE inhibition decreased the number of nuclei per myotube and reduced the size of myotubes. ENH1 siRNA knockdown significantly downregulated TRPC1 and STIM1 mRNA expression, increased basal cytosolic Ca level, and impaired SOCE response and myotube maturation. Overexpression of ENH4, a skeletal muscle-specific short splice variant of ENH1, similarly repressed TRPC1-mediated SOCE and myotube formation. Conversely, ENH1 overexpression enhanced SOCE without altering the mRNA levels of TRPC1, Orai1, or STIM1. Immunoprecipitation showed a physical interaction between ENH1/ENH4 and TRPC1. In differentiated myotubes, TRPC1 also contributed to thapsigargin-induced SOCE, as evidenced by the reduced Ca entry following TRPC1 knockdown. ENH1 knockdown and ENH4 overexpression significantly attenuated SOCE in myotubes; notably, ENH1 knockdown also increased basal cytosolic Ca level. In contrast to myoblasts, ENH1 overexpression did not enhance SOCE in myotubes, concomitant with the absence of a detectable interaction between ENH1 and TRPC1, whereas ENH4 retained its association with TRPC1. These findings suggest that ENH1 and ENH4 differentially modulate TRPC1-dependent Ca entry in C2C12 cells, thereby regulating myogenic differentiation and contributing to skeletal muscle formation and development. - Source: PubMed
Dong MingyiNiimi TomoakiMaturana Andrés Daniel - AAK1 and BMP2K are serine/threonine kinases traditionally known for phosphorylating AP2 during clathrin-mediated endocytosis (CME), but their broader roles remained incompletely defined. Here, using motif-guided in silico, biochemical, and phosphoproteomic screens, we identify PDLIM5 and Talin1 as direct AAK1/BMP2K substrates. Despite high kinase-domain similarity, only AAK1 promotes cell migration and potentiates focal adhesion (FA) turnover. Live-cell imaging shows that AAK1 recruitment to FAs peaks as disassembly begins. The conserved AAK1 C-terminal PDZ-binding motif mediates direct, low-affinity binding to PDLIM5, providing a plausible mechanism for localized substrate access. Dynamic analyses of phospho-mimetic and phospho-null mutants support a model in which AAK1-dependent phosphorylation promotes timely release of PDLIM5 and Talin1 during FA disassembly. These findings reveal a kinase-driven contribution to FA turnover distinct from protease- and phosphatase-based mechanisms and suggest that functional divergence between AAK1 and BMP2K may provide a strategy to modulate cell migration with reduced impact on CME. - Source: PubMed
Publication date: 2026/05/04
Krocianova DanielaDagg Alexander DClayton Rory APotesil DavidFedorova VeronikaHarmanec AdamBenova ViktoriaBosakova VeronikaKaufman Jonathan G GMartinkova PetraAlblova MiroslavaKelly Bernard THanakova KaterinaRoudnicky PavelSpielman Stephanie JFric JanSroubek FilipHouser JosefWrobel Antoni GBoura EvzenOwen David JZdrahal ZbynekKadlecova Zuzana - Poly-L-lactic acid (PLLA) microspheres have been successfully commercialized for skin rejuvenation. However, the inherent material properties, notably their hydrophobic surface and the acidic byproducts generated during degradation, have the potential to incite inflammatory responses and compromise long-term efficacy in tissue regeneration. In order to overcome these limitations, integrating biodegradable polymers with bioactive components are highly desirable to synergistically improve biocompatibility and actively stimulate tissue regeneration. In this study, we engineered novel composite microspheres that integrate PLLA with bioactive glass (BG). In vitro, PLLA/BG composite microspheres functioned as potent biomimetic cues, dramatically boosting cell biological behaviors of human foreskin fibroblasts (HFFs). Furthermore, the microspheres upregulated the expression of critical extracellular matrix (ECM) proteins, which underscores their potential to drive skin regeneration, and orchestrated a pro-regenerative response by upregulating key signaling factors, including transforming growth factor β1 (TGF-β1) and PDZ and LIM domain 5 (PDLIM5). The microspheres effectively polarized macrophages toward the pro-regenerative M2 phenotype and enhanced angiogenesis. In vivo experiments using a wrinkle-induced mouse model demonstrated that PLLA/BG composite microspheres significantly suppressed wrinkle formation, enhanced the deposition of ECM proteins, and stimulated new blood vessel formation. Collectively, our results established that PLLA/BG composite microspheres could modulate the skin microenvironment and achieve rejuvenation of aging skin. - Source: PubMed
Publication date: 2026/03/15
Li Zi LinWang GangDing YilinDai QiyuanLuo HuitongShi ZhifengXu XinrongCao Xiaodong