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Last update 23 Jan 2025

LIMS1

Last update 23 Jan 2025

Basic Info

Synonyms

LIM and senescent cell antigen-like-containing domain protein 1, LIM zinc finger domain containing 1, LIMS1

+ [5]

Introduction

Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation.

Drugs associated with LIMS1

SDI-1

Target

LIMS1

Mechanism

LIMS1 inhibitors

Active Org.-

Originator Org.

Baylor College of Medicine

Active Indication-

Inactive Indication

Neoplasms [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with LIMS1

100 Translational Medicine associated with LIMS1

0 Patents (Medical) associated with LIMS1

270

Literatures (Medical) associated with LIMS1

01 Jan 2025·Human Immunology

Genomic collision at the LIMS-1 locus increases risk of cellular mediated allograft rejection in heart transplanted recipients

Article

Author: Clemmensen, Tor Skibsted ; Eiskjær, Hans ; Hansen, Sandra Maria ; Koefoed-Nielsen, Pernille ; Staunstrup, Nicklas Heine

Genomic collision at the LIM and senescent cell antigen-like-containing domain protein 1 (LIMS1) locus between donor and heart recipient was examined for the association with diagnosis of acute cellular or antibody-mediated allograft rejection, ACR or ABMR, respectively. In this single center retrospective study, 129 heart transplanted patients and donors were genotyped for the LIMS1 rs893403 variant, where the G-allele is in almost complete linkage disequilibrium with a loss of function deletion. A total of 14 cases with genomic collision (recipient genotype GG and donor genotype AA/AG) were identified. After a median follow-up time of 723 days, the multivariate adjusted hazard ratio for ACR of 1.64 (95 % CI 0.66-4.1) indicated that genomic collision indeed was a risk factor, while the risk of ABMR was less affected by genotype. Although statistically not significant, due to low power, this study indicates that LIMS1 is a minor histocompatibility antigen in heart transplantation, associated with allograft rejection.

01 Dec 2024·Cytoskeleton

Sequences in the myosin A rod interact with UNC‐89/obscurin and the zinc‐finger protein UNC‐98 during thick filament assembly and M‐line formation in C. elegans striated muscle

Article

Author: Lee, Kar Men ; Almuhanna, Sarah A. ; Hoppe, Pamela E. ; Oishi, Humayra Z.

AbstractThe M‐line of striated muscle is a complex structure that anchors myosin‐containing thick filaments and also participates in signaling and proteostasis. While the physical associations among many M‐line components have been defined, the mechanism of thick filament attachment is not completely understood. In Caenorhabditis elegans, myosin A is essential for viability and forms the site of M‐line attachment at the center of the filament, whereas myosin B forms the filament arms. Using a mutant myosin A that forms ectopic filaments, we examined interactions between myosin A and M‐line proteins in intact muscle cells. Ectopic myosin A recruits the giant kinase UNC‐89/obscurin, a presumed scaffolding protein, in an interaction that requires the zinc‐finger protein UNC‐98, but not UNC‐82/NUAK, UNC‐97/PINCH, or UNC‐96. In myosin A mutants, UNC‐89/obscurin patterning is highly defective in embryos and adults. A chimeric myosin containing 169 residues of the myosin A C‐terminal rod, coincident with the UNC‐98/ZnF binding site, is sufficient for colocalization of UNC‐89/obscurin and UNC‐98/ZnF in M‐line structures whereas a myosin chimera lacking these residues colocalizes with UNC‐89/obscurin in M‐lines that lack UNC‐98. Thus, at least two myosin A rod regions contribute independently to M‐line organization. We hypothesize that these M‐line‐organizing functions correspond to the essential “filament initiation function” performed by this isoform.

01 Sep 2024·The Journal of Dermatology

Coexistence of systemic sclerosis and cryopyrin‐associated periodic syndrome

Article

Author: Sato, Shinichi ; Kuzumi, Ai ; Nagai, Kojiro ; Yoshizaki, Ayumi ; Matsuda, Kazuki

AbstractSystemic sclerosis (SSc) and cryopyrin‐associated periodic syndrome (CAPS) are distinct clinical entities belonging to the autoimmune and autoinflammatory diseases, respectively. The coexistence of the two entities has rarely been reported and is poorly characterized. Here, we described a case of a 38‐year‐old Japanese woman diagnosed with anti‐centromere antibody‐positive SSc and CAPS carrying the pathogenic mutation in the NLRP3 gene, with a detailed autoantibody profile by a high‐throughput comprehensive protein array covering approximately 90% of the human transcriptome. The clinical manifestations of the patient were typical of both SSc and CAPS. Comprehensive autoantibody profiling identified 65 autoantibodies in the patient's serum and 78 autoantibodies in the serum of her daughter with CAPS, who carried the same NLRP3 mutation as the patient. SSc‐associated autoantibodies (anti‐DBT, anti‐ CENP‐B, and anti‐CENP‐A) and anti‐CD320 antibody were detected at high levels only in the patient's serum, while autoantibodies to the following four proteins were detected in the sera of both the patient and her daughter: TRIM21, LIMS1, CLIP4, and KAT2A. The TRRUST enrichment analysis identified NF‐κB1 and RelA as overlapping key transcription factors that regulate the genes encoding proteins to which autoantibodies were detected in the patient and her daughter, therefore the autoantibody profile of the patient cannot be solely attributed to SSc, but may also be influenced by CAPS. Although autoimmune and autoinflammatory diseases are considered to be at opposite ends of the immunological spectrum, detailed autoantibody profiling may reveal a unique immunological landscape in an overlapping case of the two entities.

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