Multicellular living organisms and unmodified parts thereof and – Nonhuman animal – Transgenic nonhuman animal
Reexamination Certificate
2007-01-23
2007-01-23
Crouch, Deborah (Department: 1632)
Multicellular living organisms and unmodified parts thereof and
Nonhuman animal
Transgenic nonhuman animal
C435S354000, C800S003000
Reexamination Certificate
active
11095668
ABSTRACT:
Disclosed are a mouse homozygous or heterozygous for the defect of the Noc2 gene, and a tissue and a cell of the mouse. The Noc2 knockout mice, which exhibit stress-related insulin hyposecretion and accumulation of secretory granules of increased size and irregular shape in exocrine cells, provide a test system used in the development of therapeutic drugs for related disorders.
REFERENCES:
Keri et al, PNAS, 97(1): 383-387, 2000.
Lariviere et al, J Pharm Exp Ther, 297(2): 467-473, 2001.
Kotake et al, JBC, 272(47): 29407-29410, 1997.
Capecchi et al, Scientific American, pp. 52-59, 1994.
Jahn et al., “Membrane Fusion and Exocytosis,” Annu. Rev. Biochem., 1999, vol. 68, pp. 863-911.
Rettig et al, “Emerging Roles of Presynaptic Proteins in Ca++-Triggered Exocytosis,” Science, 2002, vol. 298, pp. 781-785.
Burgoyne et al., “Secretory Granule Exocytosis,” Physiol. Rev., 2003, vol. 83, pp. 581-632.
Burgoyne et al., “Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE Function,” Bioessays, 1998, vol. 20, pp. 328-335.
Lang, “Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion,” Eur. J. Biochem., 1999, vol. 259, pp. 3-17.
Williams, “Intracellular signaling mechanisms activated by cholecytokinin-regulating synthesis and secretion of digestive enzymes in pancreatic acinar cells,” 2001, Annu Rev. Physiol., vol. 63, pp. 77-97.
Takai et al., “Small GTP-Binding Proteins,” Physiol. Rev., 2001, vol. 81, pp. 153-208.
Zerial et al., “RAB proteins as membrane organizers,” Nat. Rev. Mol. Cell Biol., 2001, vol. 2, pp. 107-117.
Castillo et al., “Rab3A is essential for mossy fibre long-term potentiation in the hippocampus,” Nature, 1997, vol. 388, pp. 590-593.
Lledo et al., “Inhibition of Rab3B expression attenuates Ca2+-dependent exocytosis in rat anterior pituitary cells,” Nature, vol. 364, Aug. 5, 1993.
Fischer et al., “Rab3C Is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis,” R. J. Biol. Chem., 1994, vol. 269, No. 15, pp. 10971-10974.
Chen et al., “Dominant negative Rab3D inhibits amylase release from mouse pancreatic acini,” 2002, vol. 277, No. 20, pp. 18002-18009.
Shirataki et al., “Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-Binding protein related to synaptotagmin,” Molecular and Cell Biology, 1993, vol. 13, No. 4, pp. 2061-2068.
Wang et al., “Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion,” Nature, 1997, vol. 388, pp. 593-598.
Ozaki et al., “cAMP-GEFII is a direct target of cAMP in regulated exocytosis,” 2000, Nat Cell Biol., vol. 2, pp. 805-811.
Kotake et al., “Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells,” The Journal of Biological Chemistry, 1997, vol. 272, No. 47, pp. 29407-29410.
Schoch et al., “Rim1α forms a protein scaffold for regulating neurotransmitter release at the active zone,” Nature, 2002, vol. 415, pp. 321-326.
Castillo et al., “Rim1α is required for presynaptic long-term potentiation,” Nature, 2002, vol. 415, pp. 327-330.
Koushika et al., “A post-docking role for active zone protein rim,” Nat Neurosci., 2001, vol. 4, No. 10, pp. 997-1005.
Burns et al., “Rabphilin-3A: A multifunctional regulator of synaptic vesicle traffic,” J Gen Physiol., 1998, vol. 111, pp. 243-255.
Schluter et al., “Rabphilin knock-out mice reveal that rabphilin is not required for Rab3 function in regulatin neurotransmitter release,” The Journal of Neuroscience, Jul. 15, 1999, vol. 19, No. 14, pp. 5834-5846.
Kashima et al., “Critical role of cAMP-GEFII.Rim2 complex in incretin-potentiated insulin secretion,” The Journal of Biological Chemistry, 2001, vol. 276, No. 49, pp. 46046-46053.
Fujimoto et al., “Piccolo, a Ca2+ sensor in pancreatic β-cells,” The Journal of Biological Chemistry, Dec. 2002, vol. 277, No. 52, pp. 50497-50502.
Haynes et al., “A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+- regulated exocytosis in neuroendocrine cells,” The Journal of Biological Chemistry, 2001, vol. 276, No. 13, pp. 9726-9732.
De Boer et al., “Plasma catecholamine, corticosterone and glucose responses to repeated stress in rats: Effect of interstressor interval length,” Physiology and Behavior, 1990, vol. 47, pp. 1117-1124.
Okabe et al., “Green mice' as a source of ubiquitous green cells,” 1997, FEBS Letters, vol. 407, pp. 313-319.
Miki et al., “Defective insulin secretion and enhanced insulin action in KATPchannel-deficient mice,” Proc. Natl. Acad. Sci. USA, Sep. 1998, vol. 95, pp. 10402-10406.
Ohnishi et al., “Overexpression of Rab3D enhances regulated amylase secretion from pancreatic acini of transgenic mice,” 1997, J Clin Invest, vol. 100, No. 12, pp. 3044-3052.
Carrasco et al., “Neuroendocrine pharmacology of stress,” 2003, vol. 463, pp. 235-272.
Lang et al., “Direct control of exocytosis by recptor-mediated activation of the heterotrimeric GTPases Gi and Go or by the expression of their active Gα subunits,” The EMBO Journal, 1995, vol. 14, No. 15, pp. 3635-3644.
Renstroem et al., “Neurotransmitter-Induced inhibition of exocytosis in insulin-secreting β-cells by activation of calcineurin.” Neuron, Sep. 1996, vol. 17, pp. 513-522.
Sharp et al., “Mechanisms of inhibition of insulin release,” Am J. Physiol., 1996, vol. 271, pp. 1781-1799.
Yaekura et al., “Insulin secretory deficiency and glucose intolerance in Rab3A Null mice,” Mar. 14, 2003, vol. 278, No. 11, pp. 9715-9721.
Naya et al., “Diabetes, defective pancreatic morphogenesis, and abnormal enteroendocrine differentiation in BETA2/NeuroD-deficient mice,” Genes & Development, 1997, vol. 11, pp. 2323-2334.
Ohnishi et al., “Rab3D localizes to zymogen granules in rat pancreatic acini and other exocrine glands,” Am J Physiol., vol. 271, G531-538.
Riedel et al., “Rab3D is not required for exocrine exocytosis but for maintenance of normally sized secretory granules,” Molecular and Cellular Biology, Sep. 2002, pp. 6487-6497.
Iwanaga Toshihiko
Matsumoto Masanari
Miki Takashi
Seino Susumu
Crouch Deborah
JCR Pharmaceuticals Co. Ltd.
Millen White Zelano & Branigan P.C.
Seino Susumu
Sgagias Magdalene K.
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