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Article ; Online: Storage-Related Changes in Autologous Whole Blood and Irradiated Allogeneic Red Blood Cells and Their Ex Vivo Effects on Deformability, Indices, and Density of Circulating Erythrocytes in Patients Undergoing Cardiac Surgery With Cardiopulmonary Bypass.

Ichikawa, Junko / Koshino, Ichiro / Arashiki, Nobuto / Nakamura, Fumio / Komori, Makiko

Journal of cardiothoracic and vascular anesthesia

2021 Volume 36, Issue 3, Page(s) 855–861

Abstract: Objectives: Blood-processing techniques and preservation conditions cause storage lesions, possibly leading to adverse outcomes after transfusion. The authors investigated the metabolic changes and deformability of red blood cells (RBCs) during storage ... ...

Abstract	Objectives: Blood-processing techniques and preservation conditions cause storage lesions, possibly leading to adverse outcomes after transfusion. The authors investigated the metabolic changes and deformability of red blood cells (RBCs) during storage and determined the effect of storage lesions on circulating RBCs during cardiac surgery. Design: Prospective study. Setting: Tertiary care center affiliated with a university hospital. Participants: Adults who underwent elective cardiac surgery requiring cardiopulmonary bypass. Interventions: The authors collected aliquots of autologous and irradiated allogeneic RBCs and blood samples from seven patients who received autologous whole blood and nine patients who received irradiated allogeneic RBCs before incision (baseline), at the start and end of cardiopulmonary bypass, and at completion of surgery. Measurements and main results: The authors analyzed RBC deformability, erythrocyte indices, and density distribution to evaluate blood banking-induced alterations of autologous and allogeneic RBCs and changes in circulating RBCs in recipients, after blood transfusion. Time-dependent biochemical changes and significant decreases in deformability during storage occurred in both groups; however, homologous RBCs had significantly lower deformability than autologous RBCs. Trends in mean corpuscular volume and mean corpuscular hemoglobin concentration differed in both groups. In the homologous transfusion group, during cardiac surgery, RBC deformability, mean corpuscular volume, and mean corpuscular hemoglobin concentration showed significant changes compared with baseline values, and a greater number of denser subpopulations was observed at surgery completion. Conclusions: Blood-processing techniques contribute to storage lesions, suggesting that transfusion of autologous whole blood, rather than allogeneic RBCs, could maintain the ability of circulating RBCs to deform and lead to potentially better transfusion outcomes.
MeSH term(s)	Blood Preservation/adverse effects ; Blood Preservation/methods ; Cardiac Surgical Procedures/adverse effects ; Cardiopulmonary Bypass/adverse effects ; Erythrocyte Deformability ; Erythrocytes ; Hematopoietic Stem Cell Transplantation ; Humans ; Prospective Studies
Language	English
Publishing date	2021-06-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	1067317-9
ISSN	1532-8422 ; 1053-0770
ISSN (online)	1532-8422
ISSN	1053-0770
DOI	10.1053/j.jvca.2021.06.016
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Zs.A 2203: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 31: Show issues

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Article ; Online: Novel multivalent S100A8 inhibitory peptides attenuate tumor progression and metastasis by inhibiting the TLR4-dependent pathway.

Deguchi, Atsuko / Watanabe-Takahashi, Miho / Mishima, Taishi / Omori, Tsutomu / Ohto, Umeharu / Arashiki, Nobuto / Nakamura, Fumio / Nishikawa, Kiyotaka / Maru, Yoshiro

Cancer gene therapy

2023 Volume 30, Issue 7, Page(s) 973–984

Abstract: The tumor-elicited inflammation is closely related to tumor microenvironment during tumor progression. S100A8, an endogenous ligand of Toll-like receptor 4 (TLR4), is known as a key molecule in the tumor microenvironment and premetastatic niche formation. ...

Abstract	The tumor-elicited inflammation is closely related to tumor microenvironment during tumor progression. S100A8, an endogenous ligand of Toll-like receptor 4 (TLR4), is known as a key molecule in the tumor microenvironment and premetastatic niche formation. We firstly generated a novel multivalent S100A8 competitive inhibitory peptide (divalent peptide3A5) against TLR4/MD-2, using the alanine scanning. Divalent peptide3A5 suppressed S100A8-mediated interleukin-8 and vascular endothelial growth factor production in human colorectal tumor SW480 cells. Using SW480-transplanted xenograft models, divalent peptide3A5 suppressed tumor progression in a dose-dependent manner. We demonstrated that combination therapy with divalent peptide3A5 and bevacizumab synergistically suppressed tumor growth in SW480 xenograft models. Using syngeneic mouse models, we found that divalent peptide3A5 improved the efficacy of anti-programmed death (PD)1 antibody, and lung metastasis. In addition, by using multivalent peptide library screening based on peptide3A5, we then isolated two more candidates; divalent ILVIK, and tetravalent ILVIK. Of note, multivalent ILVIK, but not monovalent ILVIK showed competitive inhibitory activity against TLR4/MD-2 complex, and anti-tumoral activity in SW480 xenograft models. As most tumor cells including SW480 cells also express TLR4, S100A8 inhibitory peptides would target both the tumor microenvironment and tumor cells. Thus, multivalent S100A8 inhibitory peptides would provide new pharmaceutical options for aggressive cancers.
MeSH term(s)	Animals ; Mice ; Humans ; Calgranulin B/metabolism ; Toll-Like Receptor 4 ; Vascular Endothelial Growth Factor A/metabolism ; Calgranulin A/metabolism ; Peptides/pharmacology ; Peptides/metabolism
Chemical Substances	Calgranulin B ; Toll-Like Receptor 4 ; Vascular Endothelial Growth Factor A ; Calgranulin A ; Peptides ; TLR4 protein, human
Language	English
Publishing date	2023-03-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1212513-1
ISSN	1476-5500 ; 0929-1903
ISSN (online)	1476-5500
ISSN	0929-1903
DOI	10.1038/s41417-023-00604-3
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Zs.A 4125: Show issues

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Article ; Online: Maintenance and regulation of asymmetric phospholipid distribution in human erythrocyte membranes: implications for erythrocyte functions.

Arashiki, Nobuto / Takakuwa, Yuichi

Current opinion in hematology

2017 Volume 24, Issue 3, Page(s) 167–172

Abstract: Purpose of review: The article summarizes new insights into the molecular mechanisms for the maintenance and regulation of the asymmetric distribution of phospholipids in human erythrocyte membranes. We focus on phosphatidylserine, which is primarily ... ...

Abstract	Purpose of review: The article summarizes new insights into the molecular mechanisms for the maintenance and regulation of the asymmetric distribution of phospholipids in human erythrocyte membranes. We focus on phosphatidylserine, which is primarily found in the inner leaflet of the membrane lipid bilayer under low Ca conditions (<1 μmol/l) and is exposed to the outer leaflet under elevated Ca concentrations (>1 μmol/l), when cells become senescent. Clarification of the molecular basis of phosphatidylserine flipping and scrambling is important for addressing long-standing questions regarding phosphatidylserine functions. Recent findings: ATP11C, a P-IV ATPase, has been identified as a major flippase in analyses of patient erythrocytes with a 90% reduction in flippase activity. Phospholipid scramblase 1 (PLSCR1) has been defined as a Ca-activated scramblase that is completely suppressed by membrane cholesterol under low Ca concentrations. Summary: For survival, phosphatidylserine surface exposure is prevented by cholesterol-mediated suppression of PLSCR1 under low Ca concentrations, irrespective of flipping by ATP11C. In senescent erythrocytes, PLSCR1 is activated by elevated Ca, resulting in phosphatidylserine exposure, allowing macrophage phagocytosis. These recent molecular findings establish the importance of the maintenance and regulation of phosphatidylserine distribution for both the survival and death of human erythrocytes.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Biological Transport ; Erythrocyte Membrane/metabolism ; Erythrocytes/metabolism ; Humans ; Membrane Lipids/metabolism ; Membrane Transport Proteins/metabolism ; Phosphatidylserines/metabolism ; Phospholipid Transfer Proteins/metabolism ; Phospholipids/metabolism ; Time Factors
Chemical Substances	Membrane Lipids ; Membrane Transport Proteins ; PLSCR1 protein, human ; Phosphatidylserines ; Phospholipid Transfer Proteins ; Phospholipids ; ATP11C protein, human (EC 3.6.1.-) ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2017-05
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1153887-9
ISSN	1531-7048 ; 1065-6251
ISSN (online)	1531-7048
ISSN	1065-6251
DOI	10.1097/MOH.0000000000000326
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Article ; Online: Reduction in flippase activity contributes to surface presentation of phosphatidylserine in human senescent erythrocytes.

Seki, Momoko / Arashiki, Nobuto / Takakuwa, Yuichi / Nitta, Kosaku / Nakamura, Fumio

Journal of cellular and molecular medicine

2020 Volume 24, Issue 23, Page(s) 13991–14000

Abstract: Mature human erythrocytes circulate in blood for approximately 120 days, and senescent erythrocytes are removed by splenic macrophages. During this process, the cell membranes of senescent erythrocytes express phosphatidylserine, which is recognized as a ...

Abstract	Mature human erythrocytes circulate in blood for approximately 120 days, and senescent erythrocytes are removed by splenic macrophages. During this process, the cell membranes of senescent erythrocytes express phosphatidylserine, which is recognized as a signal for phagocytosis by macrophages. However, the mechanisms underlying phosphatidylserine exposure in senescent erythrocytes remain unclear. To clarify these mechanisms, we isolated senescent erythrocytes using density gradient centrifugation and applied fluorescence-labelled lipids to investigate the flippase and scramblase activities. Senescent erythrocytes showed a decrease in flippase activity but not scramblase activity. Intracellular ATP and K
MeSH term(s)	Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Biological Transport ; Calcium/metabolism ; Cell-Derived Microparticles/metabolism ; Cellular Senescence/genetics ; Enzyme Activation ; Erythrocyte Membrane/metabolism ; Erythrocytes/metabolism ; Humans ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Phosphatidylserines/metabolism ; Potassium/metabolism
Chemical Substances	Membrane Transport Proteins ; Phosphatidylserines ; Adenosine Triphosphate (8L70Q75FXE) ; ATP11C protein, human (EC 3.6.1.-) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Potassium (RWP5GA015D) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2020-10-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2074559-X
ISSN	1582-4934 ; 1582-4934 ; 1582-1838
ISSN (online)	1582-4934
ISSN	1582-4934 ; 1582-1838
DOI	10.1111/jcmm.16010
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Zs.A 5752: Show issues

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Article ; Online: Membrane skeleton hyperstability due to a novel alternatively spliced 4.1R can account for ellipsoidal camelid red cells with decreased deformability.

Chen, Yuqi / Miyazono, Kosuke / Otsuka, Yayoi / Kanamori, Mariko / Yamashita, Aozora / Arashiki, Nobuto / Matsumoto, Takehisa / Takada, Kensuke / Sato, Kota / Mohandas, Narla / Inaba, Mutsumi

The Journal of biological chemistry

2023 Volume 299, Issue 2, Page(s) 102877

Abstract: The red blood cells (RBCs) of vertebrates have evolved into two basic shapes, with nucleated nonmammalian RBCs having a biconvex ellipsoidal shape and anuclear mammalian RBCs having a biconcave disk shape. In contrast, camelid RBCs are flat ellipsoids ... ...

Abstract	The red blood cells (RBCs) of vertebrates have evolved into two basic shapes, with nucleated nonmammalian RBCs having a biconvex ellipsoidal shape and anuclear mammalian RBCs having a biconcave disk shape. In contrast, camelid RBCs are flat ellipsoids with reduced membrane deformability, suggesting altered membrane skeletal organization. However, the mechanisms responsible for their elliptocytic shape and reduced deformability have not been determined. We here showed that in alpaca RBCs, protein 4.1R, a major component of the membrane skeleton, contains an alternatively spliced exon 14-derived cassette (e14) not observed in the highly conserved 80 kDa 4.1R of other highly deformable biconcave mammalian RBCs. The inclusion of this exon, along with the preceding unordered proline- and glutamic acid-rich peptide (PE), results in a larger and unique 90 kDa camelid 4.1R. Human 4.1R containing e14 and PE, but not PE alone, showed markedly increased ability to form a spectrin-actin-4.1R ternary complex in viscosity assays. A similar facilitated ternary complex was formed by human 4.1R possessing a duplication of the spectrin-actin-binding domain, one of the mutations known to cause human hereditary elliptocytosis. The e14- and PE-containing mutant also exhibited an increased binding affinity to β-spectrin compared with WT 4.1R. Taken together, these findings indicate that 4.1R protein with the e14 cassette results in the formation and maintenance of a hyperstable membrane skeleton, resulting in rigid red ellipsoidal cells in camelid species, and suggest that membrane structure is evolutionarily regulated by alternative splicing of exons in the 4.1R gene.
MeSH term(s)	Animals ; Humans ; Actins/metabolism ; Alternative Splicing ; Camelids, New World ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Erythrocytes/cytology ; Erythrocytes/metabolism ; Membranes/metabolism ; Peptides/metabolism ; Protein Binding ; Spectrin/genetics ; Spectrin/metabolism ; Cell Shape/genetics
Chemical Substances	Actins ; Cytoskeletal Proteins ; erythrocyte membrane band 4.1 protein ; Peptides ; Spectrin (12634-43-4)
Language	English
Publishing date	2023-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.102877
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Article ; Online: ATP11C T418N, a gene mutation causing congenital hemolytic anemia, reduces flippase activity due to improper membrane trafficking.

Arashiki, Nobuto / Niitsuma, Kusumi / Seki, Momoko / Takakuwa, Yuichi / Nakamura, Fumio

Biochemical and biophysical research communications

2019 Volume 516, Issue 3, Page(s) 705–712

Abstract: Distribution of phosphatidylserine (PS) in the erythrocyte membrane is essential for its activity. Flippase transports phospholipids from the outer to the inner leaflet of the lipid bilayer and maintains asymmetric distribution of phospholipids in the ... ...

Abstract	Distribution of phosphatidylserine (PS) in the erythrocyte membrane is essential for its activity. Flippase transports phospholipids from the outer to the inner leaflet of the lipid bilayer and maintains asymmetric distribution of phospholipids in the plasma membrane. ATP11C, a flippase, catalyzes PS flipping at the plasma membrane in association with cell cycle control protein 50A (CDC50A). ATP11C T418 N mutation causes 90% decrease in erythrocyte PS-flippase activity. However, the mechanism of the activity reduction remains unknown. To study the endogenous expression of ATP11C in erythrocytes, we produced a monoclonal antibody against human ATP11C. Immunoblotting analyses with this antibody revealed the absence of ATP11C in erythrocyte membranes derived from a patient with the T418 N mutation. Transiently expressed ATP11C wild-type in cultured cells localized in the cell membranes in the presence of CDC50A. Contrastingly, ATP11C T418 N mutants stacked at the endoplasmic reticulum (ER) even in the presence of CDC50A, suggesting improper intracellular trafficking. Expression of the T418 N mutant in cultured cells was lower than that in the wild-type. However, reduced expression of the T418 N mutant was partially restored by treatment with proteasome inhibitors, suggesting ER-associated degradation of the mutant protein. Cells expressing T418 N did not show flippase activity at the plasma membrane. These data show that the loss of PS-flippase activity in erythrocytes carrying ATP11C T418 N mutation is due to impaired enzymatic activity, improper membrane trafficking, and increased proteasome degradation.
MeSH term(s)	Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Anemia, Hemolytic, Congenital/genetics ; Anemia, Hemolytic, Congenital/metabolism ; Animals ; Biological Transport/genetics ; COS Cells ; Chlorocebus aethiops ; Endoplasmic Reticulum/metabolism ; Erythrocyte Membrane/chemistry ; Erythrocyte Membrane/metabolism ; Erythrocytes/metabolism ; Female ; Genetic Predisposition to Disease/genetics ; HeLa Cells ; Humans ; Immunoblotting ; Male ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mutation, Missense ; Phosphatidylserines/chemistry ; Phosphatidylserines/metabolism
Chemical Substances	Membrane Proteins ; Membrane Transport Proteins ; Phosphatidylserines ; TMEM30a protein, human ; ATP11C protein, human (EC 3.6.1.-) ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2019-06-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2019.06.092
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Zs.A 116: Show issues

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Article ; Online: Changes in Erythrocyte Morphology at Initiation of Cardiopulmonary Bypass Without Blood Transfusion Were Not Associated With Less Deformability During Cardiac Surgery.

Ichikawa, Junko / Koshino, Ichiro / Arashiki, Nobuto / Nakamura, Fumio / Komori, Makiko

Journal of cardiothoracic and vascular anesthesia

2019 Volume 33, Issue 11, Page(s) 2960–2967

Abstract: Objectives: During cardiac surgery, circulating red blood cells (RBCs) are at risk of exposure to environmental factors during extracorporeal circulation and transfusion of stored RBCs. For this study, the authors observed morphological differences, ... ...

Abstract	Objectives: During cardiac surgery, circulating red blood cells (RBCs) are at risk of exposure to environmental factors during extracorporeal circulation and transfusion of stored RBCs. For this study, the authors observed morphological differences, deformability, density distribution, and erythrocyte indices of RBCs during cardiac surgery with cardiopulmonary bypass (CPB). Design: Prospective study. Setting: Tertiary care center affiliated with a university hospital. Participants: Adults who underwent elective cardiac surgery requiring CPB. Interventions: Blood samples were obtained from 13 patients before incision (baseline), at initiation of CPB, after separation from CPB, and at completion of surgery. Measurements and main results: The morphological index (MI) in RBCs using light microscopy and the maximum deformability index (DImax) using an ektacytometer were evaluated. In addition, the fractionation of RBCs and erythrocyte indices were measured. The MI at initiation of CPB was significantly higher without blood transfusion compared with baseline, although the DImax did not significantly decrease simultaneously. The DImax after separation from CPB and at completion of surgery were significantly lower than that at baseline. This lowered DImax was accompanied by a significantly reduced mean corpuscular volume and elevated mean corpuscular hemoglobin concentration compared with baseline. Dense RBC subpopulations increased after initiating CPB. The MI after separation from CPB and at completion of surgery partially recovered. Administered stored RBCs showed a high MI and the lowest DImax. Conclusions: Morphological changes at initiation of CPB are considered potentially reversible transformations without loss of the membrane surface area and do not have a significant effect on the DImax. A decrease in deformability likely is due to transfusion of stored RBCs.
MeSH term(s)	Aged ; Blood Transfusion ; Cardiopulmonary Bypass/methods ; Erythrocyte Deformability/physiology ; Erythrocytes/pathology ; Female ; Heart Diseases/blood ; Heart Diseases/surgery ; Humans ; Intraoperative Period ; Male ; Prognosis ; Prospective Studies
Language	English
Publishing date	2019-03-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	1067317-9
ISSN	1532-8422 ; 1053-0770
ISSN (online)	1532-8422
ISSN	1053-0770
DOI	10.1053/j.jvca.2019.03.030
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Zs.A 2203: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 31: Show issues

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Article: ATP11C T418N, a gene mutation causing congenital hemolytic anemia, reduces flippase activity due to improper membrane trafficking

Arashiki, Nobuto / Nakamura, Fumio / Niitsuma, Kusumi / Seki, Momoko / Takakuwa, Yuichi

Biochemical and biophysical research communications. 2019 Aug. 27, v. 516, no. 3

2019

Abstract	Distribution of phosphatidylserine (PS) in the erythrocyte membrane is essential for its activity. Flippase transports phospholipids from the outer to the inner leaflet of the lipid bilayer and maintains asymmetric distribution of phospholipids in the plasma membrane. ATP11C, a flippase, catalyzes PS flipping at the plasma membrane in association with cell cycle control protein 50A (CDC50A). ATP11C T418 N mutation causes 90% decrease in erythrocyte PS-flippase activity. However, the mechanism of the activity reduction remains unknown. To study the endogenous expression of ATP11C in erythrocytes, we produced a monoclonal antibody against human ATP11C. Immunoblotting analyses with this antibody revealed the absence of ATP11C in erythrocyte membranes derived from a patient with the T418 N mutation. Transiently expressed ATP11C wild-type in cultured cells localized in the cell membranes in the presence of CDC50A. Contrastingly, ATP11C T418 N mutants stacked at the endoplasmic reticulum (ER) even in the presence of CDC50A, suggesting improper intracellular trafficking. Expression of the T418 N mutant in cultured cells was lower than that in the wild-type. However, reduced expression of the T418 N mutant was partially restored by treatment with proteasome inhibitors, suggesting ER-associated degradation of the mutant protein. Cells expressing T418 N did not show flippase activity at the plasma membrane. These data show that the loss of PS-flippase activity in erythrocytes carrying ATP11C T418 N mutation is due to impaired enzymatic activity, improper membrane trafficking, and increased proteasome degradation.
Keywords	catalytic activity ; cell cycle ; cultured cells ; endoplasmic reticulum ; enzyme activity ; erythrocyte membrane ; erythrocytes ; genes ; hemolytic anemia ; humans ; immunoblotting ; lipid bilayers ; monoclonal antibodies ; mutants ; mutation ; patients ; phosphatidylserines ; physiological transport ; plasma membrane ; proteasome endopeptidase complex ; proteasome inhibitors
Language	English
Dates of publication	2019-0827
Size	p. 705-712.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2019.06.092
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Article ; Online: Monoallelic

Ravindran, Ethiraj / Arashiki, Nobuto / Becker, Lena-Luise / Takizawa, Kohtaro / Lévy, Jonathan / Rambaud, Thomas / Makridis, Konstantin L / Goshima, Yoshio / Li, Na / Vreeburg, Maaike / Demeer, Bénédicte / Dickmanns, Achim / Stegmann, Alexander P A / Hu, Hao / Nakamura, Fumio / Kaindl, Angela M

eLife

2022 Volume 11

Abstract: Collapsin response mediator proteins (CRMPs) are key for brain development and function. Here, we link CRMP1 to a neurodevelopmental disorder. We report heterozygous de novo variants in ... ...

Abstract	Collapsin response mediator proteins (CRMPs) are key for brain development and function. Here, we link CRMP1 to a neurodevelopmental disorder. We report heterozygous de novo variants in the
MeSH term(s)	Animals ; Humans ; Mice ; Autism Spectrum Disorder/genetics ; Intellectual Disability/genetics ; Intellectual Disability/metabolism ; Neurodevelopmental Disorders/genetics ; Neurodevelopmental Disorders/metabolism ; Neuronal Outgrowth ; Neurons/metabolism ; Muscle Hypotonia/genetics
Chemical Substances	CRMP1 protein, human
Language	English
Publishing date	2022-12-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.80793
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Article: [Senescence mechanism of human erythrocytes].

Takakuwa, Yuichi / Arashiki, Nobuto / Saito, Masaki

Rinsho ketsueki] The Japanese journal of clinical hematology

2014 Volume 55, Issue 6, Page(s) 643–650

MeSH term(s)	Cell Death ; Cellular Senescence ; Erythrocyte Membrane/chemistry ; Erythrocyte Membrane/metabolism ; Erythrocytes/cytology ; Erythrocytes/metabolism ; Humans ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism
Chemical Substances	Membrane Proteins
Language	Japanese
Publishing date	2014-06
Publishing country	Japan
Document type	Journal Article
ZDB-ID	390900-1
ISSN	0485-1439
ISSN	0485-1439
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Zs.A 1175: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 535: Show issues

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