-
Something wrong with this record ?
Calreticulin and cancer
J. Fucikova, R. Spisek, G. Kroemer, L. Galluzzi
Language English Country Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Review
NLK
Free Medical Journals
from 2011
PubMed Central
from 2011 to 1 year ago
Europe PubMed Central
from 2011 to 1 year ago
ProQuest Central
from 2000-03-01 to 1 year ago
Open Access Digital Library
from 1999-01-01
Health & Medicine (ProQuest)
from 2000-03-01 to 1 year ago
- MeSH
- Calreticulin genetics metabolism MeSH
- Humans MeSH
- Mutation MeSH
- Myeloproliferative Disorders metabolism pathology MeSH
- Neoplasms metabolism pathology MeSH
- Antigen Presentation MeSH
- Prognosis MeSH
- Signal Transduction MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
Calreticulin (CALR) is an endoplasmic reticulum (ER)-resident protein involved in a spectrum of cellular processes. In healthy cells, CALR operates as a chaperone and Ca2+ buffer to assist correct protein folding within the ER. Besides favoring the maintenance of cellular proteostasis, these cell-intrinsic CALR functions support Ca2+-dependent processes, such as adhesion and integrin signaling, and ensure normal antigen presentation on MHC Class I molecules. Moreover, cancer cells succumbing to immunogenic cell death (ICD) expose CALR on their surface, which promotes the uptake of cell corpses by professional phagocytes and ultimately supports the initiation of anticancer immunity. Thus, loss-of-function CALR mutations promote oncogenesis not only as they impair cellular homeostasis in healthy cells, but also as they compromise natural and therapy-driven immunosurveillance. However, the prognostic impact of total or membrane-exposed CALR levels appears to vary considerably with cancer type. For instance, while genetic CALR defects promote pre-neoplastic myeloproliferation, patients with myeloproliferative neoplasms bearing CALR mutations often experience improved overall survival as compared to patients bearing wild-type CALR. Here, we discuss the context-dependent impact of CALR on malignant transformation, tumor progression and response to cancer therapy.
Caryl and Israel Englander Institute for Precision Medicine New York NY USA
Department of Dermatology Yale University School of Medicine New Haven CT USA
Department of Radiation Oncology Weill Cornell Medical College New York NY USA
Metabolomics and Cell Biology Platforms Institut Gustave Roussy Villejuif France
Pôle de Biologie Hôpital Européen Georges Pompidou AP HP Paris France
Sandra and Edward Meyer Cancer Center New York NY USA
Suzhou Institute for Systems Medicine Chinese Academy of Sciences Suzhou Jiangsu China
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc22004692
- 003
- CZ-PrNML
- 005
- 20220127145045.0
- 007
- ta
- 008
- 220113s2021 xxk f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1038/s41422-020-0383-9 $2 doi
- 035 __
- $a (PubMed)32733014
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxk
- 100 1_
- $a Fucikova, Jitka $u Sotio, Prague, Czech Republic $u Department of Immunology, Charles University, 2nd Faculty of Medicine and University Hospital Motol, Prague, Czech Republic
- 245 10
- $a Calreticulin and cancer / $c J. Fucikova, R. Spisek, G. Kroemer, L. Galluzzi
- 520 9_
- $a Calreticulin (CALR) is an endoplasmic reticulum (ER)-resident protein involved in a spectrum of cellular processes. In healthy cells, CALR operates as a chaperone and Ca2+ buffer to assist correct protein folding within the ER. Besides favoring the maintenance of cellular proteostasis, these cell-intrinsic CALR functions support Ca2+-dependent processes, such as adhesion and integrin signaling, and ensure normal antigen presentation on MHC Class I molecules. Moreover, cancer cells succumbing to immunogenic cell death (ICD) expose CALR on their surface, which promotes the uptake of cell corpses by professional phagocytes and ultimately supports the initiation of anticancer immunity. Thus, loss-of-function CALR mutations promote oncogenesis not only as they impair cellular homeostasis in healthy cells, but also as they compromise natural and therapy-driven immunosurveillance. However, the prognostic impact of total or membrane-exposed CALR levels appears to vary considerably with cancer type. For instance, while genetic CALR defects promote pre-neoplastic myeloproliferation, patients with myeloproliferative neoplasms bearing CALR mutations often experience improved overall survival as compared to patients bearing wild-type CALR. Here, we discuss the context-dependent impact of CALR on malignant transformation, tumor progression and response to cancer therapy.
- 650 _2
- $a prezentace antigenu $7 D017951
- 650 _2
- $a kalretikulin $x genetika $x metabolismus $7 D037282
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a mutace $7 D009154
- 650 _2
- $a myeloproliferativní poruchy $x metabolismus $x patologie $7 D009196
- 650 _2
- $a nádory $x metabolismus $x patologie $7 D009369
- 650 _2
- $a prognóza $7 D011379
- 650 _2
- $a signální transdukce $7 D015398
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 655 _2
- $a Research Support, U.S. Gov't, Non-P.H.S. $7 D013486
- 655 _2
- $a přehledy $7 D016454
- 700 1_
- $a Spisek, Radek $u Sotio, Prague, Czech Republic $u Department of Immunology, Charles University, 2nd Faculty of Medicine and University Hospital Motol, Prague, Czech Republic
- 700 1_
- $a Kroemer, Guido $u Equipe labellisée par la Ligue contre le cancer, Centre de Recherche des Cordeliers, INSERM U1138, Université de Paris, Sorbonne Université, Paris, France. kroemer@orange.fr $u Metabolomics and Cell Biology Platforms, Institut Gustave Roussy, Villejuif, France. kroemer@orange.fr $u Pôle de Biologie, Hôpital Européen Georges Pompidou, AP-HP, Paris, France. kroemer@orange.fr $u Suzhou Institute for Systems Medicine, Chinese Academy of Sciences, Suzhou, Jiangsu, China. kroemer@orange.fr $u Karolinska Institute, Deparment of Women's and Children's Health, Karolinska University Hospital, Stockholm, Sweden. kroemer@orange.fr
- 700 1_
- $a Galluzzi, Lorenzo $u Department of Radiation Oncology, Weill Cornell Medical College, New York, NY, USA. deadoc80@gmail.com $u Sandra and Edward Meyer Cancer Center, New York, NY, USA. deadoc80@gmail.com $u Caryl and Israel Englander Institute for Precision Medicine, New York, NY, USA. deadoc80@gmail.com $u Department of Dermatology, Yale University School of Medicine, New Haven, CT, USA. deadoc80@gmail.com $u Université de Paris, Paris, France. deadoc80@gmail.com
- 773 0_
- $w MED00006780 $t Cell research $x 1748-7838 $g Roč. 31, č. 1 (2021), s. 5-16
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/32733014 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y p $z 0
- 990 __
- $a 20220113 $b ABA008
- 991 __
- $a 20220127145041 $b ABA008
- 999 __
- $a ok $b bmc $g 1751996 $s 1155841
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2021 $b 31 $c 1 $d 5-16 $e 20200730 $i 1748-7838 $m Cell Research $n Cell Res $x MED00006780
- LZP __
- $a Pubmed-20220113
