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C57BL/6JCya-Cavin1em1flox/Cya
Common Name:
Cavin1-flox
Product ID:
S-CKO-04617
Background:
C57BL/6JCya
Product Type
Age
Genotype
Sex
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Basic Information
Strain Name
Cavin1-flox
Strain ID
CKOCMP-19285-Cavin1-B6J-VA
Gene Name
Cavin1
Product ID
S-CKO-04617
Gene Alias
2310075E07Rik; Cav-p60; Cavin; Ptrf
Background
C57BL/6JCya
NCBI ID
19285
Modification
Conditional knockout
Chromosome
11
Phenotype
MGI:1277968
Document
Click here to download >>
Application
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Rare Disease Data Center >>
Note
Note: When using this mouse strain in a publication, please cite “C57BL/6JCya-Cavin1em1flox/Cya mice (Catalog S-CKO-04617) were purchased from Cyagen.”
Strain Description
Ensembl Number
ENSMUST00000060792
NCBI RefSeq
NM_008986
Target Region
Exon 2
Size of Effective Region
~2.9 kb
Detailed Document
Click here to download >>
Overview of Gene Research
Cavin1, also known as caveolae-associated protein 1 and encoded by the polymerase I and transcript release factor (PTRF) gene, is essential for caveolae biogenesis. It functions in processes like regulating membrane tension, signaling cascades, and lipid sorting. Caveolae are small plasma membrane invaginations, and Cavin1's interaction with caveolin 1 is crucial for their formation [3,4,5].

In a study on drug-induced QT prolongation (diLQT), Cavin1 was found to regulate the susceptibility to diLQT. CAVIN1 expression levels in patient-specific induced pluripotent stem cell-derived cardiomyocytes (iPS-CMs) affected the response to hERG blockers like sotalol. Higher CAVIN1 expression in more sensitive iPS-CMs led to hERG channel translocation from the membrane to the cytoskeleton-associated fractions upon sotalol treatment, reducing the delayed-rectifier potassium current (IKr) and prolonging the late repolarization phase [1].

In glioblastoma, the small-molecular inhibitor EPIC-1042 interrupted the interaction between PTRF/Cavin1 and caveolin-1, reducing small extracellular vesicles (sEVs) secretion to decrease temozolomide (TMZ) efflux and inducing PARP1 autophagic degradation, enhancing TMZ efficacy [2].

In congenital generalized lipodystrophy type 4 (CGL4), a novel pathogenic mutation of the CAVIN1/PTRF gene was found in two siblings. Cavin-1 dysfunction led to a clinical phenotype characterized by absence of adipose tissue and muscular dystrophy [3].

Cavin1 deficiency in C57BL/6J mice caused neonatal death due to disorder of hepatic glycogen metabolism, as it impaired fenestration in liver sinusoidal endothelial cells (LSECs) by inhibiting the RhoA-Rho-associated protein kinase 2-LIM domain kinase-Cofilin signaling pathway [6].

In conclusion, Cavin1 plays diverse and crucial roles in multiple biological processes and disease conditions. Its function in caveolae biogenesis has far-reaching impacts on various cellular functions. Studies using genetic models, such as gene-knockout mouse models in the case of Cavin1 deficiency, have revealed its significance in diseases like diLQT, glioblastoma, CGL4, and neonatal hypoglycemia related to hepatic glycogen metabolism disorder.

References:
1. Al Sayed, Zeina R, Pereira, Céline, Le Borgne, Rémi, Trégouët, David-Alexandre, Hulot, Jean-Sébastien. 2024. CAVIN1-Mediated hERG Dynamics: A Novel Mechanism Underlying the Interindividual Variability in Drug-Induced Long QT. In Circulation, 150, 563-576. doi:10.1161/CIRCULATIONAHA.123.063917. https://pubmed.ncbi.nlm.nih.gov/38682330/
2. Hong, Biao, Yang, Eryan, Su, Dongyuan, Cui, Longtao, Kang, Chunsheng. . EPIC-1042 as a potent PTRF/Cavin1-caveolin-1 interaction inhibitor to induce PARP1 autophagic degradation and suppress temozolomide efflux for glioblastoma. In Neuro-oncology, 26, 100-114. doi:10.1093/neuonc/noad159. https://pubmed.ncbi.nlm.nih.gov/37651725/
3. Mancioppi, Valentina, Daffara, Tommaso, Romanisio, Martina, Giordano, Mara, Prodam, Flavia. 2023. A new mutation in the CAVIN1/PTRF gene in two siblings with congenital generalized lipodystrophy type 4: case reports and review of the literature. In Frontiers in endocrinology, 14, 1212729. doi:10.3389/fendo.2023.1212729. https://pubmed.ncbi.nlm.nih.gov/37501786/
4. Liu, Kang-Cheng, Pace, Hudson, Larsson, Elin, Hubert, Madlen, Lundmark, Richard. 2022. Membrane insertion mechanism of the caveola coat protein Cavin1. In Proceedings of the National Academy of Sciences of the United States of America, 119, e2202295119. doi:10.1073/pnas.2202295119. https://pubmed.ncbi.nlm.nih.gov/35696574/
5. Tillu, Vikas A, Rae, James, Gao, Ya, Parton, Robert G, Collins, Brett M. 2021. Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation. In Nature communications, 12, 931. doi:10.1038/s41467-021-21035-4. https://pubmed.ncbi.nlm.nih.gov/33568658/
6. Wei, Zhuang, Lei, Jigang, Shen, Feng, Liao, Kan, Hong, Shangyu. 2020. Cavin1 Deficiency Causes Disorder of Hepatic Glycogen Metabolism and Neonatal Death by Impacting Fenestrations in Liver Sinusoidal Endothelial Cells. In Advanced science (Weinheim, Baden-Wurttemberg, Germany), 7, 2000963. doi:10.1002/advs.202000963. https://pubmed.ncbi.nlm.nih.gov/33042738/
Quality Control Standard
Sperm Test

Pre-cryopreservation: Measurement of sperm concentration, determination of sperm viability.

Post-cryopreservation: A vial of cryopreserved sperms is selected for in-vitro fertilization from each batch.

Environmental Standards:SPF
Available Region:Global
Source:Cyagen
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