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Article: Identification of endothelial cell surface carbohydrate-binding receptors by carbohydrate ligand mimicry peptides.

Fukuda, Michiko N

Advances in experimental medicine and biology

2012 Volume 749, Page(s) 57–66

MeSH term(s)	Amino Acid Sequence ; Animals ; Apoptosis ; Carbohydrates/chemistry ; Endothelium/chemistry ; Endothelium/cytology ; Lung/chemistry ; Lung/cytology ; Mice ; Molecular Mimicry ; Molecular Sequence Data ; Peptides/chemistry ; Receptors, Cell Surface/chemistry
Chemical Substances	Carbohydrates ; Peptides ; Receptors, Cell Surface
Language	English
Publishing date	2012
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-1-4614-3381-1_5
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Peptide-displaying phage technology in glycobiology.

Fukuda, Michiko N

Glycobiology

2011 Volume 22, Issue 3, Page(s) 318–325

Abstract: Phage display technology is an emerging drug discovery tool. Using that approach, short peptides that mimic part of a carbohydrate's conformation are selected by screening a peptide-displaying phage library with anti-carbohydrate antibodies. Chemically ... ...

Abstract	Phage display technology is an emerging drug discovery tool. Using that approach, short peptides that mimic part of a carbohydrate's conformation are selected by screening a peptide-displaying phage library with anti-carbohydrate antibodies. Chemically synthesized peptides with an identified sequence have been used as an alternative ligand to carbohydrate-binding proteins. These peptides represent research tools useful to assay the activities of glycosyltransferases and/or sulfotransferases or to inhibit the carbohydrate-dependent binding of proteins in vitro and in vivo. Peptides can also serve as immunogens to raise anti-carbohydrate antibodies in vivo in animals. Phage display has also been used in single-chain antibody technology by inserting an immunoglobulin's variable region sequence into the phage. A single-chain antibody library can then be screened with a carbohydrate antigen as the target, resulting in a recombinant anti-carbohydrate antibody with high affinity to the antigen. This review provides examples of successful applications of peptide-displaying phage technology to glycobiology. Such an approach should benefit translational research by supplying carbohydrate-mimetic peptides and carbohydrate-binding polypeptides.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antigens/chemistry ; Biomimetic Materials ; Glycomics ; Humans ; Immobilized Proteins ; Peptide Library ; Peptides/chemistry ; Peptides/immunology ; Polysaccharides/immunology ; Protein Binding ; Single-Chain Antibodies/isolation & purification
Chemical Substances	Antigens ; Immobilized Proteins ; Peptide Library ; Peptides ; Polysaccharides ; Single-Chain Antibodies
Language	English
Publishing date	2011-09-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwr140
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Article ; Online: Efficient antigen delivery by dendritic cell-targeting peptide via nucleolin confers superior vaccine effects in mice.

Matsuda, Teppei / Misato, Kazuki / Tamiya, Shigeyuki / Akeda, Yasuhiro / Nakase, Ikuhiko / Kuroda, Etsushi / Takahama, Shokichi / Nonaka, Motohiro / Yamamoto, Takuya / Fukuda, Michiko N / Yoshioka, Yasuo

iScience

2022 Volume 25, Issue 11, Page(s) 105324

Abstract: Efficient delivery of subunit vaccines to dendritic cells (DCs) is necessary to improve vaccine efficacy, because the vaccine antigen alone cannot induce sufficient protective immunity. Here, we identified DC-targeting peptides using a phage display ... ...

Abstract	Efficient delivery of subunit vaccines to dendritic cells (DCs) is necessary to improve vaccine efficacy, because the vaccine antigen alone cannot induce sufficient protective immunity. Here, we identified DC-targeting peptides using a phage display system and demonstrated the potential of these peptides as antigen-delivery carriers to improve subunit vaccine effectiveness in mice. The fusion of antigen proteins and peptides with DC-targeting peptides induced strong antigen-specific IgG responses, even in the absence of adjuvants. In addition, the DC-targeting peptide improved the distribution of antigens to DCs and antigen presentation by DCs. The combined use of an adjuvant with a DC-targeting peptide improved the effectiveness of the vaccine. Furthermore, nucleolin, located on the DC surface, was identified as the receptor for DC-targeting peptide, and nucleolin was indispensable for the vaccine effect of the DC-targeting peptide. Overall, the findings of this study could be useful for developing subunit vaccines against infectious diseases.
Language	English
Publishing date	2022-10-10
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2022.105324
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Article ; Online: Correction to: Tumor vasculature-targeted 10B delivery by an Annexin A1-binding peptide boosts effects of boron neutron capture therapy.

Yoneyama, Tohru / Hatakeyama, Shingo / Sutoh Yoneyama, Mihoko / Yoshiya, Taku / Uemura, Tsuyoshi / Ishizu, Takehiro / Suzuki, Minoru / Hachinohe, Shingo / Ishiyama, Shintaro / Nonaka, Motohiro / Fukuda, Michiko N / Ohyama, Chikara

BMC cancer

2021 Volume 21, Issue 1, Page(s) 105

Language	English
Publishing date	2021-01-29
Publishing country	England
Document type	Published Erratum
ISSN	1471-2407
ISSN (online)	1471-2407
DOI	10.1186/s12885-021-07815-7
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Article: Screening of peptide-displaying phage libraries to identify short peptides mimicking carbohydrates.

Fukuda, Michiko N

Methods in enzymology

2006 Volume 416, Page(s) 51–60

Abstract: Peptide-displaying phage technology has numerous applications. Using a specificity-defined monoclonal anti-carbohydrate antibody, we can identify a series of short peptides that mimic the binding specificity of a specific carbohydrate. This chapter ... ...

Abstract	Peptide-displaying phage technology has numerous applications. Using a specificity-defined monoclonal anti-carbohydrate antibody, we can identify a series of short peptides that mimic the binding specificity of a specific carbohydrate. This chapter introduces pioneering work applying phage display technology to the glycobiology field, presents a step-by-step protocol for phage library screening, and provides useful hints for evaluating results including false positives, all of which should contribute to successful cloning. Thus, biopanning using a monoclonal antibody as the target is described in detail. Because peptides are useful alternatives to carbohydrate ligands, their potential use as structural or functional mimics of carbohydrate-binding proteins is discussed.
MeSH term(s)	Antibodies, Monoclonal/chemistry ; Bacteriophages ; Base Sequence ; Binding Sites, Antibody ; Carbohydrates/chemistry ; Molecular Mimicry ; Molecular Sequence Data ; Peptide Library ; Peptides/chemistry
Chemical Substances	Antibodies, Monoclonal ; Carbohydrates ; Peptide Library ; Peptides
Language	English
Publishing date	2006
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/S0076-6879(06)16004-8
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Article ; Online: Trophinin in cell adhesion and signal transduction.

Fukuda, Michiko N / Sugihara, Kazuhiro

Frontiers in bioscience (Elite edition)

2012 Volume 4, Issue 1, Page(s) 342–350

Abstract: The process of human embryo implantation is mediated not only by evolutionarily conserved mechanisms but by activities unique to humans. Among the latter, evidence suggests that the cell adhesion molecule trophinin plays a unique role in human embryo ... ...

Abstract	The process of human embryo implantation is mediated not only by evolutionarily conserved mechanisms but by activities unique to humans. Among the latter, evidence suggests that the cell adhesion molecule trophinin plays a unique role in human embryo implantation. Here, we describe characteristics of trophinin protein and of the trophinin-associated proteins bystin and tastin. We then describe trophinin-mediated signal transduction in trophectoderm cells during human embryo implantation and events related to human sperm tail motility. We also report dual roles for trophinin in human cancers in terms of promoting malignancy in some tumor types and suppressing it in others.
MeSH term(s)	Amino Acid Sequence ; Cell Adhesion Molecules/chemistry ; Cell Adhesion Molecules/metabolism ; Cell Adhesion Molecules/physiology ; Humans ; Molecular Sequence Data ; Neoplasms/metabolism ; Protein Binding ; Proteins/metabolism ; Sequence Homology, Amino Acid ; Signal Transduction/physiology ; Structure-Activity Relationship
Chemical Substances	BYSL protein, human ; Cell Adhesion Molecules ; Proteins ; TRO protein, human ; TROAP protein, human
Language	English
Publishing date	2012-01-01
Publishing country	Singapore
Document type	Journal Article ; Review
ZDB-ID	2565080-4
ISSN	1945-0508 ; 1945-0494
ISSN (online)	1945-0508
ISSN	1945-0494
DOI	10.2741/381
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Article: Cell adhesion molecules in human embryo implantation.

Fukuda, Michiko N / Sugihara, Kazuhiro

Sheng li xue bao : [Acta physiologica Sinica

2012 Volume 64, Issue 3, Page(s) 247–258

Abstract: The process of human embryo implantation is mediated not only by evolutionarily conserved mechanisms, but also by a mechanism unique to humans. Evidence suggests that the cell adhesion molecules, L-selectin and trophinin, play a unique role in human ... ...

Abstract	The process of human embryo implantation is mediated not only by evolutionarily conserved mechanisms, but also by a mechanism unique to humans. Evidence suggests that the cell adhesion molecules, L-selectin and trophinin, play a unique role in human embryo implantation. Here, we describe the dual roles of mucin carbohydrate ligand for L-selectin and trophinin protein and of the trophinin-associated proteins bystin and tastin. We then describe trophinin-mediated signal transduction in trophectoderm cells and endometrial epithelial cells. This review also covers cadherin and integrin in human embryo implantation.
MeSH term(s)	Cadherins/physiology ; Cell Adhesion Molecules/physiology ; Embryo Implantation ; Epithelial Cells/metabolism ; Humans ; Integrins/physiology ; L-Selectin/physiology ; Signal Transduction
Chemical Substances	BYSL protein, human ; Cadherins ; Cell Adhesion Molecules ; Integrins ; TRO protein, human ; TROAP protein, human ; L-Selectin (126880-86-2)
Language	English
Publishing date	2012-06-25
Publishing country	China
Document type	Journal Article ; Review
ZDB-ID	604308-2
ISSN	0371-0874
ISSN	0371-0874
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Article ; Online: Tumor vasculature-targeted

BMC cancer

2021 Volume 21, Issue 1, Page(s) 72

Abstract: Background: p-Boronophenylalanine (: Methods: (1) IF7 conjugates of either : Results: Intravenous injection of IF7C conjugates of either : Conclusions: We conclude that IF7 serves as an ... ...

Abstract	Background: p-Boronophenylalanine ( Methods: (1) IF7 conjugates of either Results: Intravenous injection of IF7C conjugates of either Conclusions: We conclude that IF7 serves as an efficient
MeSH term(s)	Animals ; Annexin A1/metabolism ; Apoptosis ; Boron Compounds/administration & dosage ; Boron Compounds/chemistry ; Boron Compounds/metabolism ; Boron Neutron Capture Therapy/methods ; Cell Proliferation ; Female ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Nude ; Neovascularization, Pathologic/metabolism ; Neovascularization, Pathologic/pathology ; Neovascularization, Pathologic/radiotherapy ; Peptide Fragments/metabolism ; Phenylalanine/administration & dosage ; Phenylalanine/analogs & derivatives ; Phenylalanine/chemistry ; Phenylalanine/metabolism ; Tumor Cells, Cultured ; Urinary Bladder Neoplasms/metabolism ; Urinary Bladder Neoplasms/pathology ; Urinary Bladder Neoplasms/radiotherapy ; Xenograft Model Antitumor Assays
Chemical Substances	Annexin A1 ; Boron Compounds ; Peptide Fragments ; Phenylalanine (47E5O17Y3R) ; 4-boronophenylalanine (UID84303EL)
Language	English
Publishing date	2021-01-15
Publishing country	England
Document type	Journal Article
ISSN	1471-2407
ISSN (online)	1471-2407
DOI	10.1186/s12885-020-07760-x
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Article ; Online: Development of an orally-administrable tumor vasculature-targeting therapeutic using annexin A1-binding D-peptides.

Nonaka, Motohiro / Mabashi-Asazuma, Hideaki / Jarvis, Donald L / Yamasaki, Kazuhiko / Akama, Tomoya O / Nagaoka, Masato / Sasai, Toshio / Kimura-Takagi, Itsuko / Suwa, Yoichi / Yaegashi, Takashi / Huang, Chun-Teng / Nishizawa-Harada, Chizuko / Fukuda, Michiko N

PloS one

2021 Volume 16, Issue 1, Page(s) e0241157

Abstract: We previously reported that IF7 peptide, which binds to the annexin A1 (ANXA1) N-terminus ... the ANXA1 N-terminus as target. We then identified peptide sequences, synthesized them as D-amino acids, and ... designated the resulting peptide dTIT7, which we showed bound to the ANXA1 N-terminus. Whole body imaging ...

Abstract	We previously reported that IF7 peptide, which binds to the annexin A1 (ANXA1) N-terminus, functions as a tumor vasculature-targeted drug delivery vehicle after intravenous injection. To enhance IF7 stability in vivo, we undertook mirror-image peptide phage display using a synthetic D-peptide representing the ANXA1 N-terminus as target. We then identified peptide sequences, synthesized them as D-amino acids, and designated the resulting peptide dTIT7, which we showed bound to the ANXA1 N-terminus. Whole body imaging of mouse brain tumor models injected with near infrared fluorescent IRDye-conjugated dTIT7 showed fluorescent signals in brain and kidney. Furthermore, orally-administered dTIT7/geldanamycin (GA) conjugates suppressed brain tumor growth. Ours is a proof-of-concept experiment showing that ANXA1-binding D-peptide can be developed as an orally-administrable tumor vasculature-targeted therapeutic.
MeSH term(s)	Administration, Oral ; Animals ; Annexin A1/antagonists & inhibitors ; Annexin A1/metabolism ; Brain Neoplasms/blood supply ; Brain Neoplasms/drug therapy ; Brain Neoplasms/metabolism ; Brain Neoplasms/pathology ; Drug Delivery Systems ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Neoplasm Proteins/antagonists & inhibitors ; Neoplasm Proteins/metabolism ; Neovascularization, Pathologic/drug therapy ; Neovascularization, Pathologic/metabolism ; Neovascularization, Pathologic/pathology ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/pharmacology ; Xenograft Model Antitumor Assays
Chemical Substances	ANXA1 protein, human ; Annexin A1 ; Neoplasm Proteins ; Peptides
Language	English
Publishing date	2021-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0241157
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Article ; Online: Annexin A1 expression is correlated with malignant potential of renal cell carcinoma.

Yamanoi, Mariko / Yamanoi, Kazuhiro / Fujii, Chifumi / Fukuda, Michiko N / Nakayama, Jun

International journal of urology : official journal of the Japanese Urological Association

2018 Volume 26, Issue 2, Page(s) 284–290

Abstract: Objectives: To evaluate the expression of annexin A1 protein in patients with renal cell carcinoma.: Methods: Annexin A1 expression was examined in renal cell carcinoma specimens from 27 patients, and their disease-free survival was analyzed using ... ...

Abstract	Objectives: To evaluate the expression of annexin A1 protein in patients with renal cell carcinoma. Methods: Annexin A1 expression was examined in renal cell carcinoma specimens from 27 patients, and their disease-free survival was analyzed using the log-rank test. Annexin A1 knockdown in the human renal cell carcinoma cell line Caki-1 was carried out, and its proliferation, invasion, motility and adhesion were compared with those of control cells. Results: In 13 out of 27 patients, annexin A1 was highly expressed in the membrane of renal cell carcinoma tumor cells, whereas in the rest of the patients, annexin A1 expression was weak or negligible in the membrane of those cells. Patients with high annexin A1 expression had significantly poorer disease-free survival than those with weak or negligible annexin A1 expression (P = 0.031). In the renal cell carcinoma cell line, annexin A1 knockdown cells showed significantly decreased proliferation, invasion, motility and adhesion relative to control cells, and expressed lower relative levels of membrane-type 1 matrix metalloproteinase and hypoxia-inducible factor 1-alpha transcripts, showing a potential pathway regulated by annexin A1. Conclusion: Annexin A1 is associated with renal cell carcinoma malignant potential and could serve as a marker of poor prognosis.
MeSH term(s)	Aged ; Aged, 80 and over ; Annexin A1/genetics ; Annexin A1/metabolism ; Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Carcinoma, Renal Cell/genetics ; Carcinoma, Renal Cell/mortality ; Carcinoma, Renal Cell/pathology ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Disease-Free Survival ; Female ; Gene Expression Regulation, Neoplastic ; Gene Knockdown Techniques ; Humans ; Hypoxia-Inducible Factor 1, alpha Subunit/metabolism ; Kidney Neoplasms/genetics ; Kidney Neoplasms/mortality ; Kidney Neoplasms/pathology ; Male ; Matrix Metalloproteinase 14/metabolism ; Middle Aged ; Neoplasm Invasiveness/pathology ; Prognosis ; Survival Analysis
Chemical Substances	ANXA1 protein, human ; Annexin A1 ; Biomarkers, Tumor ; HIF1A protein, human ; Hypoxia-Inducible Factor 1, alpha Subunit ; MMP14 protein, human (EC 3.4.24.80) ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2018-12-02
Publishing country	Australia
Document type	Journal Article
ZDB-ID	1328401-0
ISSN	1442-2042 ; 0919-8172
ISSN (online)	1442-2042
ISSN	0919-8172
DOI	10.1111/iju.13869
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Zs.A 4460: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 278: Show issues

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