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Y. Kamiya, F. Oyama, R. Oyama, F. Sakakibara, K. Nitta, H. Kawauchi, Y. Takayanagi, K. Titani (1990)
Amino acid sequence of a lectin from Japanese frog (Rana japonica) eggs.Journal of biochemistry, 108 1
H. Kawauchi, F. Sakakibara, K. Watanabe (1975)
Agglutinins of frog eggs: A new class of proteins causing preferential agglutination of tumor cellsExperientia, 31
K. Nitta, G. Takayanagi, H. Kawauchi, S. Hakomori (1987)
Isolation and characterization of Rana catesbeiana lectin and demonstration of the lectin-binding glycoprotein of rodent and human tumor cell membranes.Cancer research, 47 18
Thalia Becker, F. Hartl, F. Wieland (2002)
CD40, an extracellular receptor for binding and uptake of Hsp70–peptide complexesThe Journal of Cell Biology, 158
M. Bausero, D. Page, E. Osinaga, A. Asea (2004)
Surface Expression of Hsp25 and Hsp72 Differentially Regulates Tumor Growth and MetastasisTumor Biology, 25
L. Snoeckx, R. Cornelussen, F. Nieuwenhoven, R. Reneman, G. Vusse (2001)
Heat shock proteins and cardiovascular pathophysiology.Physiological reviews, 81 4
K. Titani, K. Takio, M. Kuwada, K. Nitta, F. Sakakibara, H. Kawauchi, G. Takayanagi, S. Hakomori (1987)
Amino acid sequence of sialic acid binding lectin from frog (Rana catesbeiana) eggs.Biochemistry, 26 8
Hosokawa (1992)
Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoidsMol Cell Biol, 12
K. Nitta, K. Ozaki, Yoshimasa Tsukamoto, S. Furusawa, Y. Ohkubo, H. Takimoto, R. Murata, M. Hosono, N. Hikichi, K. Sasaki, H. Kawauchi, Y. Takayanagi, S. Tsuiki, S. Hakomori (1994)
Characterization of a Rana catesbeiana lectin-resistant mutant of leukemia P388 cells.Cancer research, 54 4
Nitta (1996)
Catalytic lectin (leczyme) from bullfrog (Rana catesbeiana) eggs: Mechanism of tumoricidal activityInt J Oncol, 9
K. Nitta, K. Ozaki, Y. Tsukamoto, M. Hosono, Y. Ogawakonno, H. Kawauchi, Y. Takayanagi, S. Tsuiki, S. Hakomori (1996)
Catalytic lectin (leczyme) from bullfrog (Rana catesbeiana) eggs.International journal of oncology, 9 1
K. Nitta, Kouichi Ozaki, M. Ishikawa, S. Furusawa, M. Hosono, H. Kawauchi, K. Sasaki, Y. Takayanagi, S. Tsuiki, S. Hakomori (1994)
Inhibition of cell proliferation by Rana catesbeiana and Rana japonica lectins belonging to the ribonuclease superfamily.Cancer research, 54 4
Guerrero Ca, Moreno Lp (2012)
Rotavirus receptor proteins Hsc70 and integrin αvβ3 are located in the lipid microdomains of animal intestinal cells.Acta Virologica, 56
W. Welch (1992)
Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease.Physiological reviews, 72 4
Sheng Chen, D. Bawa, S. Besshoh, J. Gurd, I. Brown (2005)
Association of heat shock proteins and neuronal membrane components with lipid rafts from the rat brainJournal of Neuroscience Research, 81
S. Sugawara, T. Kawano, Takashi Omoto, M. Hosono, T. Tatsuta, K. Nitta (2009)
Binding of Silurus asotus lectin to Gb3 on Raji cells causes disappearance of membrane-bound form of HSP70.Biochimica et biophysica acta, 1790 2
A. Asea, S. Kraeft, E. Kurt-Jones, M. Stevenson, L. Chen, R. Finberg, G. Koo, S. Calderwood (2000)
HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokineNature Medicine, 6
D. Mosser, A. Caron, L. Bourget, Claude Denis-Larose, B. Massie (1997)
Role of the human heat shock protein hsp70 in protection against stress-induced apoptosisMolecular and Cellular Biology, 17
K. Nitta, F. Oyama, R. Oyama, K. Sekiguchi, H. Kawauchi, Y. Takayanagi, S. Hakomori, K. Titani (1993)
Ribonuclease activity of sialic acid-binding lectin from Rana catesbeiana eggs.Glycobiology, 3 1
F. Sakakibara, H. Kawauchi, G. Takayanagi, H. Ise (1979)
Egg lectin of Rana japonica and its receptor glycoprotein of Ehrlich tumor cells.Cancer research, 39 4
S. Calderwood, S. Mambula, P. Gray, Jimmy Thériault (2007)
Extracellular heat shock proteins in cell signalingFEBS Letters, 581
M. Haigis, Erin Kurten, R. Raines (2003)
Ribonuclease inhibitor as an intracellular sentry.Nucleic acids research, 31 3
Yukie Okabe, Naoko Katayama, M. Iwama, Hideaki Watanabe, K. Ohgi, Masachika Irie, K. Nitta, H. Kawauchi, Y. Takayanagi, Fumitaka Oyama, Koichl Abe, Taro Okazaki, N. Inokuchi, Takashi Koyama (1991)
Comparative base specificity, stability, and lectin activity of two lectins from eggs of Rana catesbeiana and R. japonica and liver ribonuclease from R. catesbeiana.Journal of biochemistry, 109 5
A. Asea, M. Rehli, E. Kabingu, J. Boch, Olivia Baré, P. Auron, M. Stevenson, S. Calderwood (2002)
Novel Signal Transduction Pathway Utilized by Extracellular HSP70The Journal of Biological Chemistry, 277
H. Beere, B. Wolf, K. Cain, D. Mosser, A. Mahboubi, T. Kuwana, P. Tailor, R. Morimoto, G. Cohen, D. Green (2000)
Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosomeNature Cell Biology, 2
A. Broquet, G. Thomas, J. Masliah, G. Trugnan, M. Bachelet (2003)
Expression of the Molecular Chaperone Hsp70 in Detergent-resistant Microdomains Correlates with Its Membrane Delivery and Release*Journal of Biological Chemistry, 278
T. Tatsuta, M. Hosono, S. Sugawara, Yukiko Kariya, Y. Ogawa, S. Hakomori, K. Nitta (2013)
Sialic acid-binding lectin (leczyme) induces caspase-dependent apoptosis-mediated mitochondrial perturbation in Jurkat cellsInternational Journal of Oncology, 43
S. Liossis, X. Ding, J. Kiang, G. Tsokos (1997)
Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells.Journal of immunology, 158 12
N. Hosokawa, K. Hirayoshi, H. Kudo, H. Takechi, A. Aoike, K. Kawai, K. Nagata (1992)
Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoidsMolecular and Cellular Biology, 12
Heat shock proteins (Hsps) are molecular chaperones that maintain homeostasis of organisms. In regards to the Hsps, many studies have investigated the structure, expression, localization and functions of Hsp70 and Hsc70 including expression in the glycosphingolipid-enriched microdomain (GEM) on the cell surface and involvement in cell death. Sialic acid-binding lectin (SBL) isolated from oocytes of Rana catesbeiana is a multifunctional protein which has lectin activity, ribonuclease activity and antitumor activity. SBL has potential as a new type of anticancer drug, since it causes cancer-selective induction of apoptosis by multiple signaling pathways in which RNA is its target; and the participation of the mitochondrial pathway and the endoplasmic reticulum (ER) stress-mediated pathway has been suggested. It has also been suggested that receptor(s) for SBL (SBLR) may exist in the GEM on the cell surface. In the present study, we studied the possible involvement of Hsp70 and Hsc70 in SBL-induced apoptosis. We showed that Hsp70 and Hsc70 were expressed on the P388 cell surface similar to SBLR, and their distribution in cells dramatically changed immediately prior to the execution of apoptosis following stimulation of SBL. Functional study of Hsp70 revealed that decreased expression of Hsp70 diminished the apoptosis induced by SBL. It is suggested that Hsp70 participates in the antitumor effect of SBL.
Oncology Reports – Spandidos Publications
Published: Jan 1, 2014
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