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our data suggest the involvement of autoimmune reactivity to CRT (show SLC6A8 Proteins) in a subset of patients suffering from DCM or HCM.
Endoplasmic reticulum chaperone CRT (show SLC6A8 Proteins) plays a regulatory role in the invasion of EVTs, suggesting the importance of CRT (show SLC6A8 Proteins) expression in placental development during early pregnancy.
findings demonstrate the potency of CALR mutants to drive expression of megakaryocytic differentiation markers such as NF-E2 (show NFE2 Proteins) and CD41 as well as Mpl (show MPL Proteins). Furthermore, CALR mutants undergo accelerated protein degradation that involves the secretory pathway and/or protein glycosylation.
Essential Thrombocythemia and Primary Myelofibrosis patients with CALR mutations are at high risk for Thrombotic Events.
These findings showed that mutant CALR activates jak (show JAK3 Proteins)-stat (show STAT1 Proteins) signaling through an mpl (show MPL Proteins)-dependent mechanism to mediate pathogenic thrombopoiesis in zebrafish, and illustrated that the signaling machinery related to mutant CALR tumorigenesis are conserved between human and zebrafish.
The present work suggests that Ca(2 (show CA2 Proteins)+)-dependent regulation is caused by different conformations of a long proline-rich loop that changes the accessibility to the peptide/lectin-binding site. Our results indicate that the binding of Ca(2 (show CA2 Proteins)+) to calreticulin may thus not only just be a question of Ca(2 (show CA2 Proteins)+) storage but is likely to have an impact on the chaperone activity.
CRT (show SLC6A8 Proteins) regulates TGF-beta1 (show TGFB1 Proteins)-induced-EMT (show ITK Proteins) through modulating Smad (show SMAD1 Proteins) signaling
Our results showed that a wide range of different CALR mutations are associated with a distinct ET clinical phenotype that is associated with the male gender, younger age at diagnosis, higher platelet and lower leukocyte and erythrocyte counts and lower hemoglobin level, and a milder clinical course.
alpha-Integrin expression and function modulates presentation of cell surface calreticulin.
Although CALR mutations resulted in protein instability and proteosomal degradation, mutant CALR was able to enhance megakaryopoiesis and pro-platelet production from human CD34 (show CD34 Proteins)(+) progenitors.
study provides a model showing that the C-terminal of mutant CALR activated JAK (show JAK3 Proteins)-STAT (show STAT1 Proteins) signaling specifically downstream of MPL (show MPL Proteins) and may have a central role in CALR-induced myeloproliferative neoplasms
the results of this investigation provide the first molecular insights into the phospholipid binding site of calreticulin as a key anchor point for the cell surface expression of calreticulin on apoptotic cells
a profound impairment in calreticulin function when its lectin site was inactivated. Remarkably, inactivation of the polypeptide binding site had little impact. These findings indicate that the lectin-based mode of client interaction is the predominant contributor to the chaperone functions of calreticulin within the endoplasmic reticulum.
This essential role of calreticulin in nucleocytoplasmic communication competency ties its regulatory action with proficiency of cardiac myofibrillogenesis essential for proper cardiac development.
Study provides evidence that chronic stress activates calreticulin and might be one of the pathological mechanisms underlying the motor coordination and motor learning dysfunctions seen in social defeat mice.
This study for the first time revealed that increased CRT (show SLC6A8 Proteins) inhibited Fas (show FAS Proteins)/FasL (show FASL Proteins)-mediated neuronal cell apoptosis during the early stage of ischemic stroke, suggesting it to be a potential protector activated soon after ischemia-reperfusion injury
The findings highlight the importance of CALR in female reproduction and demonstrate that compromised CALR function leads to ovarian insufficiency and female infertility.
Calreticulin mediates vascular smooth muscle cell responses to injury through the regulation of collagen deposition and neointima formation.
CALR mutants are sufficient to induce thrombocytosis through MPL (show MPL Proteins) activation.
Thrombopoietin receptor (show MPL Proteins) activation by myeloproliferative neoplasm associated calreticulin mutants.
Calreticulin plays a key role in olfactory system function, possibly by establishing its overall sensitivity to odorants.
Calreticulin mediates hypersensitivity to diethylether and resistance to isoflurane in association with low expression of the gene.
These results collectively indicate that calreticulin is the first molecule to be identified as a marker for phagocytosis of apoptotic cells by Drosophila phagocytes
Calreticulin is confined to subplasmalemmal vesicles partially overlapping with cortical granule contents. Its exocytosis after the oocyte activation seems to participate in the membrane block to polyspermy in pigs.
Calreticulin was widely expressed in pig tissues and its transcripts were downregulated during maturation, especially at 44 hr, and were undetectable at the blastocyst stage.
the lectin site of CRT is the main target for gentamicin binding
These findings suggest that protein kinase C is involved in the regulation of CRT function.
Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is almost identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. Calreticulin binds to antibodies in certain sera of systemic lupus and Sjogren patients which contain anti-Ro/SSA antibodies, it is highly conserved among species, and it is located in the endoplasmic and sarcoplasmic reticulum where it may bind calcium. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin can inhibit the binding of androgen receptor to its hormone-responsive DNA element and can inhibit androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Thus, calreticulin can act as an important modulator of the regulation of gene transcription by nuclear hormone receptors. Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin but calreticulin is not a Ro/SS-A antigen. Earlier papers referred to calreticulin as an Ro/SS-A antigen but this was later disproven. Increased autoantibody titer against human calreticulin is found in infants with complete congenital heart block of both the IgG and IgM classes.
, Sicca syndrome antigen A (autoantigen Ro; calreticulin)
, endoplasmic reticulum resident protein 60
, pot pourri
, calcium-binding protein 3
, ER-resident chaperone calreticulin
, Endoplasmic reticulum resident protein 60
, calreticulin, like 2