Noc2 knockout mouse

Multicellular living organisms and unmodified parts thereof and – Nonhuman animal – Transgenic nonhuman animal

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

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.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Noc2 knockout mouse does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Noc2 knockout mouse, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Noc2 knockout mouse will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3784269

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.