LIMS1 antibody
- Known as:
- LIMS1 (anti-)
- Catalog number:
- orb100306
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- LIMS1 antibody
Related genes to: LIMS1 antibody
- Gene:
- LIMS1 NIH gene
- Name:
- LIM zinc finger domain containing 1
- Previous symbol:
- -
- Synonyms:
- PINCH, PINCH1
- Chromosome:
- 2q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-01-15
- Date modifiied:
- 2016-02-12
Related products to: LIMS1 antibody
Related articles to: LIMS1 antibody
- Non-HLA donor-recipient (D-R) genetic mismatches contribute to kidney allograft injury and long-term graft loss, but their clinical use is limited by the unavailability of donor DNA after transplantation. We tested whether non-invasively obtained, recipient-derived samples could be used to infer donor genotype and D-R mismatches. Genomic DNA (g-DNA) of 11 unselected kidney transplant recipients and donors underwent whole-exome sequencing (100x). Additional customized probes were added for intronic coverage (300x) of 55 targeted non-HLA genes of reported clinical relevance. Variants identified from sequencing results were compared with plasma cell-free DNA (cfDNA), urine cell-pellet DNA (U-DNA) obtained from the same recipients. Genome-wide-, exonic-, or non-synonymous exonic- mismatches in transmembrane or secreted proteins, and mismatches within target genes were benchmarked using donor g-DNA to generate mismatch scores for each D-R pair. Within each of these genomic scales of mismatch, U-DNA identified D-R mismatches significantly better than the corresponding cfDNA (P<0.001 for each comparison). U-DNA also identified gene-level mismatches in the gene, and correctly inferred established donor-origin risk alleles, including . Our findings demonstrate proof-of-concept that U-DNA in tandem with recipient genome, can non-invasively infer relevant non-HLA loci/mismatches circumventing the need for the donor's genomic DNA. - Source: PubMed
Publication date: 2026/06/02
Rajeevan NallakkandiBarsotti Gabriel CKumar AshwaniSun ZeguoReghuvaran AnandTikhonova IrinaTanvir E MSareen NiketaSwan AshleyFormica RichardMandel-Brehm CaleighRao ArundatiBesse WhitneyMiller MaureenBow LaurineDe Kumar BonyMenon Madhav C - Red blood cells (RBCs) play an important role in thrombosis, yet the molecular mechanisms by which they contribute to thrombus formation remain incompletely defined. Semaphorin 7A (Sema7A) is highly expressed on RBCs as a JMH antigen, but its functional contribution to arterial thrombosis has not been fully elucidated. - Source: PubMed
Publication date: 2026/05/21
Ren LijieLiu ChuZhang JiayuRui YuWang AnniZheng ZhongLiu HuihuiLu QiongyuZhu LiTang Chaojun - During the development of the peripheral nervous system, Schwann cells rely on intricate interactions among extracellular matrix proteins, integrins, and growth factor signaling pathways to ensure survival, axonal sorting, and the myelination of axons. Central to these interactions is the IPP complex, a heterotrimeric assembly of Pinch ('particularly interesting new cysteine-histidine-rich') proteins, integrin-linked kinase (Ilk) and parvins, which serves as a crucial signaling hub linking integrins to diverse cellular pathways. Through Schwann cell-specific conditional gene ablation in mice, we reveal distinct and essential roles for Pinch1 and Pinch2 in Schwann cell function. While Pinch1 is primarily required for proper radial sorting of axons and maturation of Remak bundles, Pinch2 modulates myelin thickness and is crucial for effective remyelination following sciatic nerve injury. Our data suggest that Pinch1-mediated specific modulation of Rho GTPase signaling is essential for sorting of axon bundles, and that Pinch2 likely modulates RhoA to relieve its inhibitory effect on myelination and remyelination. These findings support a dual intrinsic function of the IPP complex regulating active Rho GTPase signaling, shedding light on the molecular mechanisms underlying developmental peripheral nervous system myelination and repair. - Source: PubMed
Publication date: 2026/04/02
Paes-de-Faria JoanaDias Nuno GonçaloGonçalves Ana FilipaFässler ReinhardRelvas João Bettencourt - Vascular mural cells (VMCs) are crucial for vascular stability, and their dysfunction underlies cardiovascular pathologies including atherosclerosis and aortic aneurysms. PINCH proteins are core focal adhesion components mediating integrin signaling, yet their roles in VMC development remain elusive. Here, we generated mice with conditional deletion of both PINCH1 and PINCH2 in Pdgfrb-lineage VMCs, which resulted in perinatal lethality accompanied by severe arterial enlargement, hemorrhage and defective angiogenesis. Mutant VMCs exhibited profound defects in cytoskeletal organization, proliferation, differentiation, adhesion and extracellular matrix assembly. Multi-omics analyses revealed that PINCH deficiency dysregulated phospho-signaling networks, hyperactivating PDGFR/EGFR/AKT/ERK and STAT/NF-κB pathways while impairing integrin-FAK-SRC and cell cycle-associated pathways (p53, p27). RNA-seq demonstrated altered expression of genes enriched in immune response (CD74, Tlr2), cytoskeleton (TUBB3, ACTA2) and VMC differentiation (Rgs5, Kcnj8, ABCC9). Importantly, we identified PINCH1 as a nuclear transcriptional coregulator that directly represses proliferative-inflammatory programs while promoting contractile-adhesive and cytoskeletal organization signatures. The clinical relevance of these findings is underscored by downregulation of PINCH genes in human atherosclerosis and Marfan syndrome aneurysms, with conserved dysregulation of key PINCH targets including CD74 and RGS5. Our work reveals a dual cytoplasmic-nuclear mechanism for PINCH in maintaining vascular homeostasis, providing both mechanistic insights and therapeutic targets for vascular diseases. - Source: PubMed
Publication date: 2026/03/08
Wang ChunxiaoJin YaoXin YuanfengXing QiankeZhu HongmingZou QichengYan JieLuo LinaLiang XingqunSun YunfuLiu Zhongmin - Cancer-associated fibroblasts (CAFs) are vital in advancing pancreatic ductal adenocarcinoma (PDAC) cancer growth and fibrosis. Although their roles are recognized, the precise molecular mechanisms remain incompletely understood. The study focuses on PINCH-1, a molecule elevated in various tumors, and its lesser-known effects on tumor stromal cells. This work reveals that PINCH-1 ablation in pancreatic CAFs (P-CAFs) significantly reduces extracellular matrix (ECM) expression, particularly collagen I and fibronectin. For collagen I, this effect is due to PINCH-1's ability to stabilize Notch1 protein, preventing Notch1 degradation, which is crucial for collagen I production. Reintroducing PINCH-1 can reverse collagen I reduction, highlighting a novel mechanism for matrix remodeling through the PINCH-1-Notch1 axis. Moreover, PINCH-1 also boosts cancer cell proliferation via the AKT signaling pathway, as demonstrated in both in vitro and in vivo experiments. We identify PINCH-1 as a master regulator within P-CAFs that promotes PDAC progression through dual mechanisms: (1) sustaining desmoplasia via Notch1-dependent collagen I production and (2) fueling cancer cell proliferation via AKT activation. Targeting the PINCH-1/Notch1/AKT axis presents a novel theragnostic strategy to simultaneously disrupt the fibrotic tumor microenvironment and inhibit tumor growth in PDAC. (188 words). - Source: PubMed
Publication date: 2026/02/10
Wang RongYang XingxingWong Yu HinGuo LingWu ChuanyueChan Barbara Pui