메뉴 건너뛰기




Volumn 73, Issue 1, 1999, Pages 12-20

Molecular cloning of testican-2: Defining a novel calcium-binding proteoglycan family expressed in brain

Author keywords

Calcium; Central nervous system; Follistatin; Modular protein; Proteoglycan; Testican

Indexed keywords

BRAIN PROTEIN; CALCIUM BINDING PROTEIN; FOLLISTATIN; MESSENGER RNA; TESTICAN 2; UNCLASSIFIED DRUG;

EID: 0344326341     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0730012.x     Document Type: Article
Times cited : (60)

References (50)
  • 1
    • 0027269935 scopus 로고
    • Testican, a multidomain testicular proteoglycan resembling modulators of cell social behavior
    • Alliel P. M., Perin J. P., Jolles P., and Bonnet F. J. (1993) Testican, a multidomain testicular proteoglycan resembling modulators of cell social behavior. Eur. J. Biochem. 214, 347-350.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 347-350
    • Alliel, P.M.1    Perin, J.P.2    Jolles, P.3    Bonnet, F.J.4
  • 2
    • 0031834148 scopus 로고    scopus 로고
    • A theory of cortical neuron-astrocyte interaction
    • Antanitus D. S. (1998) A theory of cortical neuron-astrocyte interaction. Neuroscience 4, 154-159.
    • (1998) Neuroscience , vol.4 , pp. 154-159
    • Antanitus, D.S.1
  • 3
    • 0029083530 scopus 로고
    • The turning point in genome research
    • Boguski M. S. (1995) The turning point in genome research. Trends Biochem. Sci. 20, 295-296.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 295-296
    • Boguski, M.S.1
  • 4
    • 0026476388 scopus 로고
    • Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide
    • Bonnet F., Perin J. P., Maillet P., Jolles P., and Alliel P. M. (1992) Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide. Biochem. J. 288, 565-569.
    • (1992) Biochem. J. , vol.288 , pp. 565-569
    • Bonnet, F.1    Perin, J.P.2    Maillet, P.3    Jolles, P.4    Alliel, P.M.5
  • 5
    • 0029927851 scopus 로고    scopus 로고
    • Structure and cellular distribution of mouse brain testican. Association with the postsynaptic area of hippocampus pyramidal cells
    • Bonnet F., Perin J. P., Charbonnier F., Camuzat A., Roussel G., Nussbaum J. L., and Alliel P. M. (1996) Structure and cellular distribution of mouse brain testican. Association with the postsynaptic area of hippocampus pyramidal cells. J. Biol. Chem. 271, 4373-4380.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4373-4380
    • Bonnet, F.1    Perin, J.P.2    Charbonnier, F.3    Camuzat, A.4    Roussel, G.5    Nussbaum, J.L.6    Alliel, P.M.7
  • 6
    • 0029665769 scopus 로고    scopus 로고
    • QR1, a retina-specific gene, encodes an extracellular matrix protein exclusively expressed during neural retina differentiation
    • Casado F. J., Pouponnot C., Jeanny J. C., Lecoq O., Calothy G., and Pierani A. (1996) QR1, a retina-specific gene, encodes an extracellular matrix protein exclusively expressed during neural retina differentiation. Mech. Dev. 54, 237-250.
    • (1996) Mech. Dev. , vol.54 , pp. 237-250
    • Casado, F.J.1    Pouponnot, C.2    Jeanny, J.C.3    Lecoq, O.4    Calothy, G.5    Pierani, A.6
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 10
    • 0031023262 scopus 로고    scopus 로고
    • Expression of agrin in the developing and adult rat brain
    • Cohen N. A., Kaufmann W. E., Worley P. F., and Rupp F. (1997) Expression of agrin in the developing and adult rat brain. Neuroscience 76, 581-596.
    • (1997) Neuroscience , vol.76 , pp. 581-596
    • Cohen, N.A.1    Kaufmann, W.E.2    Worley, P.F.3    Rupp, F.4
  • 11
    • 0028805976 scopus 로고
    • Activin a and follistatin expression in developing targets of ciliary ganglion neurons suggests a role in regulating neurotransmitter phenotype
    • Darland D. C., Link B. A., and Nishi R. (1995) Activin A and follistatin expression in developing targets of ciliary ganglion neurons suggests a role in regulating neurotransmitter phenotype. Neuron 15, 857-866.
    • (1995) Neuron , vol.15 , pp. 857-866
    • Darland, D.C.1    Link, B.A.2    Nishi, R.3
  • 12
    • 0030872564 scopus 로고    scopus 로고
    • Molecular tuning of an EF-hand-like calcium binding loop. Contributions of the coordinating side chain at loop position 3
    • Drake S. K., Zimmer M. A., Kundrot C., and Falke J. F. (1997) Molecular tuning of an EF-hand-like calcium binding loop. Contributions of the coordinating side chain at loop position 3. J. Gen. Physiol. 110, 173-184.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 173-184
    • Drake, S.K.1    Zimmer, M.A.2    Kundrot, C.3    Falke, J.F.4
  • 13
    • 0029820952 scopus 로고    scopus 로고
    • A novel transmembrane protein with epidermal growth factor and follistatin domains expressed in the hypothalamo-hypophysial axis of Xenopus laevis
    • Eib D. W., and Martens G. J. (1996) A novel transmembrane protein with epidermal growth factor and follistatin domains expressed in the hypothalamo-hypophysial axis of Xenopus laevis. J. Neurochem. 67, 1047-1055.
    • (1996) J. Neurochem. , vol.67 , pp. 1047-1055
    • Eib, D.W.1    Martens, G.J.2
  • 15
    • 0030340041 scopus 로고    scopus 로고
    • Functions of brain chondroitin sulfate proteoglycans during developments: Interactions with adhesion molecules
    • Grumet M., Friedlander D. R., and Sakurai T. (1996) Functions of brain chondroitin sulfate proteoglycans during developments: interactions with adhesion molecules. Perspect. Dev. Neurobiol. 3, 319-330.
    • (1996) Perspect. Dev. Neurobiol. , vol.3 , pp. 319-330
    • Grumet, M.1    Friedlander, D.R.2    Sakurai, T.3
  • 16
    • 0028297870 scopus 로고
    • Inhibition of activin receptor signaling promotes neuralization in Xenopus
    • Hemmati-Brivanlou A. and Melton D. A. (1994) Inhibition of activin receptor signaling promotes neuralization in Xenopus. Cell 77, 273-281.
    • (1994) Cell , vol.77 , pp. 273-281
    • Hemmati-Brivanlou, A.1    Melton, D.A.2
  • 17
    • 0028270311 scopus 로고
    • Follistatin, an antagonist of activin, is expressed in the Spemann organizer and displays direct neuralizing activity
    • Hemmati-Brivanlou A., Kelly O. G., and Melton D. A. (1994) Follistatin, an antagonist of activin, is expressed in the Spemann organizer and displays direct neuralizing activity. Cell 77, 283-295.
    • (1994) Cell , vol.77 , pp. 283-295
    • Hemmati-Brivanlou, A.1    Kelly, O.G.2    Melton, D.A.3
  • 19
    • 0030995856 scopus 로고    scopus 로고
    • Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40
    • Hohenester E., Maurer P., and Timpl R. (1997) Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. EMBO J. 16, 3778-3786.
    • (1997) EMBO J. , vol.16 , pp. 3778-3786
    • Hohenester, E.1    Maurer, P.2    Timpl, R.3
  • 20
    • 0032482928 scopus 로고    scopus 로고
    • Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo
    • Iemura S. I., Yamamoto T. S., Takagi C., Uchiyama H., Natsume T., Shimasaki S., Sugino H., and Ueno N. (1998) Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo. Proc. Natl. Acad. Sci. USA 95, 9337-9342.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9337-9342
    • Iemura, S.I.1    Yamamoto, T.S.2    Takagi, C.3    Uchiyama, H.4    Natsume, T.5    Shimasaki, S.6    Sugino, H.7    Ueno, N.8
  • 21
    • 0030986608 scopus 로고    scopus 로고
    • The family of the small leucine-rich proteoglycans: Key regulators of matrix assembly and cellular growth
    • Iozzo R. V. (1997) The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth. Crit. Rev. Biochem. Mol. Biol. 32, 141-174.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 141-174
    • Iozzo, R.V.1
  • 22
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo R. V. and Murdoch A. D. (1996) Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J, 10, 598-614.
    • (1996) FASEB J , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 23
    • 0028866994 scopus 로고
    • Nonsynaptic modulation of neuronal activity in the brain: Electric currents and extracellular ions
    • Jefferys J. G. R. (1995) Nonsynaptic modulation of neuronal activity in the brain: electric currents and extracellular ions. Physiol. Rev. 75, 689-723.
    • (1995) Physiol. Rev. , vol.75 , pp. 689-723
    • Jefferys, J.G.R.1
  • 24
    • 0030804282 scopus 로고    scopus 로고
    • Properties of the extracellular calcium binding module of the proteoglycan testican
    • Kohfeldt E., Maurer P., Vannahme C., and Timpl R. (1997) Properties of the extracellular calcium binding module of the proteoglycan testican. FEBS Lett. 414, 557-561.
    • (1997) FEBS Lett. , vol.414 , pp. 557-561
    • Kohfeldt, E.1    Maurer, P.2    Vannahme, C.3    Timpl, R.4
  • 25
    • 0030213227 scopus 로고    scopus 로고
    • Interpreting cDNA sequences: Some insights from studies on translation
    • Kozak M. (1996) Interpreting cDNA sequences: some insights from studies on translation. Mamm. Genome 7, 563-574.
    • (1996) Mamm. Genome , vol.7 , pp. 563-574
    • Kozak, M.1
  • 26
    • 0027420339 scopus 로고
    • Proteoglycans in the nervous system
    • Lander A. D. (1993) Proteoglycans in the nervous system. Curr. Opin. Neurobiol. 3, 716-723.
    • (1993) Curr. Opin. Neurobiol. , vol.3 , pp. 716-723
    • Lander, A.D.1
  • 27
    • 23444459571 scopus 로고
    • The biology of SPARC, a protein that modulates cell-matrix interactions
    • Lane T. F. and Sage E. H. (1994) The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J. 8, 163-173.
    • (1994) FASEB J. , vol.8 , pp. 163-173
    • Lane, T.F.1    Sage, E.H.2
  • 28
    • 0023686881 scopus 로고
    • Cloning and complete amino acid sequence of human and murine basement membrane protein BM-40 (SPARC, osteonectin)
    • Lankat-Buttgereit B., Mann K., Deutzmann R., Timpl R., and Krieg T. (1988) Cloning and complete amino acid sequence of human and murine basement membrane protein BM-40 (SPARC, osteonectin). FEBS Lett. 236, 352-356.
    • (1988) FEBS Lett. , vol.236 , pp. 352-356
    • Lankat-Buttgereit, B.1    Mann, K.2    Deutzmann, R.3    Timpl, R.4    Krieg, T.5
  • 29
    • 0027211820 scopus 로고
    • Nervous tissue proteoglycans
    • Margolis R. K. and Margolis R. U. (1993) Nervous tissue proteoglycans. Experientia 49, 429-446.
    • (1993) Experientia , vol.49 , pp. 429-446
    • Margolis, R.K.1    Margolis, R.U.2
  • 30
    • 0030730256 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans as mediators of axon growth and path finding
    • Margolis R. U. and Margolis R. K. (1997) Chondroitin sulfate proteoglycans as mediators of axon growth and path finding. Cell Tissue Res. 290, 343-348.
    • (1997) Cell Tissue Res. , vol.290 , pp. 343-348
    • Margolis, R.U.1    Margolis, R.K.2
  • 31
    • 0030919445 scopus 로고    scopus 로고
    • Activins, inhibins, and follistatins: Further thoughts on a growing family of regulators
    • Mather J. P., Moore A., and Li R. H. (1997) Activins, inhibins, and follistatins: further thoughts on a growing family of regulators. Proc. Soc. Exp. Biol. Med. 215, 209-222.
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.215 , pp. 209-222
    • Mather, J.P.1    Moore, A.2    Li, R.H.3
  • 32
    • 0028839859 scopus 로고
    • The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV
    • Maurer P., Hohenadl C., Hohenester E., Göhring W., Timpl R., and Engel J. (1995) The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV. J. Mol. Biol. 253, 347-357.
    • (1995) J. Mol. Biol. , vol.253 , pp. 347-357
    • Maurer, P.1    Hohenadl, C.2    Hohenester, E.3    Göhring, W.4    Timpl, R.5    Engel, J.6
  • 34
    • 0030070883 scopus 로고    scopus 로고
    • SC1: A marker for astrocytes in the adult rodent brain is upregulated during reactive astrocytosis
    • McKinnon P. J. and Margolskee R. F. (1996) SC1: a marker for astrocytes in the adult rodent brain is upregulated during reactive astrocytosis. Brain Res. 709, 27-36.
    • (1996) Brain Res. , vol.709 , pp. 27-36
    • McKinnon, P.J.1    Margolskee, R.F.2
  • 35
    • 0028123375 scopus 로고
    • Developmental expression in the rat cerebellum of SC1, a putative brain extracellular matrix glycoprotein related to SPARC
    • Mendis D. B., Shahin S., Gurd J. W., and Brown I. R. (1994) Developmental expression in the rat cerebellum of SC1, a putative brain extracellular matrix glycoprotein related to SPARC. Brain Res. 633, 197-205.
    • (1994) Brain Res. , vol.633 , pp. 197-205
    • Mendis, D.B.1    Shahin, S.2    Gurd, J.W.3    Brown, I.R.4
  • 36
    • 0028915961 scopus 로고
    • SPARC, an extracellular matrix glycoprotein containing the follistatin module, is expressed by astrocytes in synaptic enriched regions of the adult brain
    • Mendis D. B., Malaval L., and Brown I. R. (1995) SPARC, an extracellular matrix glycoprotein containing the follistatin module, is expressed by astrocytes in synaptic enriched regions of the adult brain. Brain Res. 676, 69-79.
    • (1995) Brain Res. , vol.676 , pp. 69-79
    • Mendis, D.B.1    Malaval, L.2    Brown, I.R.3
  • 37
    • 0029797002 scopus 로고    scopus 로고
    • Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families
    • Molina F., Bouanani M., Pau B., and Granier C. (1996) Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families. Eur. J. Biochem. 240, 125-133.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 125-133
    • Molina, F.1    Bouanani, M.2    Pau, B.3    Granier, C.4
  • 38
    • 0030608273 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. VI. the coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain
    • Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., and Nomura N. (1996) Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 3, 321-329.
    • (1996) DNA Res. , vol.3 , pp. 321-329
    • Nagase, T.1    Seki, N.2    Ishikawa, K.3    Ohira, M.4    Kawarabayasi, Y.5    Ohara, O.6    Tanaka, A.7    Kotani, H.8    Miyajima, N.9    Nomura, N.10
  • 39
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and van Heijne O. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Van Heijne, O.4
  • 40
    • 0028031129 scopus 로고
    • Brain development and multiple molecular species of proteoglycan
    • Oohira A., Katoh-Semba R., Watanabe E., and Matsui F. (1994) Brain development and multiple molecular species of proteoglycan. Neurosci. Res. 20, 195-207.
    • (1994) Neurosci. Res. , vol.20 , pp. 195-207
    • Oohira, A.1    Katoh-Semba, R.2    Watanabe, E.3    Matsui, F.4
  • 41
    • 0030587604 scopus 로고    scopus 로고
    • Cloning and early dorsal axial expression of Flik, a chick follistatin-related gene: Evidence for involvement in dorsalization/neural induction
    • Patel K., Connolly D. J., Amthor H., Nose K., and Cooke J. (1996) Cloning and early dorsal axial expression of Flik, a chick follistatin-related gene: evidence for involvement in dorsalization/neural induction. Dev. Biol. 178, 327-342.
    • (1996) Dev. Biol. , vol.178 , pp. 327-342
    • Patel, K.1    Connolly, D.J.2    Amthor, H.3    Nose, K.4    Cooke, J.5
  • 42
    • 0021931832 scopus 로고
    • Stimulus- And amino acid-induced calcium and potassium changes in rat neocortex
    • Pumain R. and Heinemann U. (1985) Stimulus- and amino acid-induced calcium and potassium changes in rat neocortex. J. Neurophysiol. 53, 1-16.
    • (1985) J. Neurophysiol. , vol.53 , pp. 1-16
    • Pumain, R.1    Heinemann, U.2
  • 43
    • 0002791951 scopus 로고    scopus 로고
    • Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction
    • Ruegg M. A. and Bixby J. L. (1998) Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction. Trends Neurosci. 21, 22-27.
    • (1998) Trends Neurosci. , vol.21 , pp. 22-27
    • Ruegg, M.A.1    Bixby, J.L.2
  • 44
    • 0029823181 scopus 로고    scopus 로고
    • Brain extracellular matrix
    • Ruoslahti E. (1996) Brain extracellular matrix. Glycobiology 6, 489-492.
    • (1996) Glycobiology , vol.6 , pp. 489-492
    • Ruoslahti, E.1
  • 45
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Ruoslahti E. and Yamaguchi Y. (1991) Proteoglycans as modulators of growth factor activities. Cell 64, 867-869.
    • (1991) Cell , vol.64 , pp. 867-869
    • Ruoslahti, E.1    Yamaguchi, Y.2
  • 46
    • 0032536897 scopus 로고    scopus 로고
    • Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/ osteonectin
    • Sasaki T., Hohenester E., Göhring W., and Timpl R. (1998) Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/ osteonectin. EMBO J. 17, 1625-1634.
    • (1998) EMBO J. , vol.17 , pp. 1625-1634
    • Sasaki, T.1    Hohenester, E.2    Göhring, W.3    Timpl, R.4
  • 47
    • 0029669991 scopus 로고    scopus 로고
    • The SlOO family of EF-hand calcium-binding proteins; functions and pathology
    • Schäfer B. W. and Heizmann C. W. (1996) The SlOO family of EF-hand calcium-binding proteins; functions and pathology. Trends Biochem. 21, 134-140.
    • (1996) Trends Biochem. , vol.21 , pp. 134-140
    • Schäfer, B.W.1    Heizmann, C.W.2
  • 48
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?
    • Schlessinger J., Lax I., and Lemmon M. (1995) Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors? Cell 83, 357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 49
    • 0031002390 scopus 로고    scopus 로고
    • The revised 8,307 basepair coding sequence of human thyroglobulin transiently expressed in eukaryotic cells
    • van de Graaf S. A. R., Pauws E., de Vijlder J. J. M., and Ris-Stalpers C. (1997) The revised 8,307 basepair coding sequence of human thyroglobulin transiently expressed in eukaryotic cells. Eur. J. Endocrinol. 136, 508-515.
    • (1997) Eur. J. Endocrinol. , vol.136 , pp. 508-515
    • Van De Graaf, S.A.R.1    Pauws, E.2    De Vijlder, J.J.M.3    Ris-Stalpers, C.4
  • 50
    • 0031910476 scopus 로고    scopus 로고
    • The role of the insulin-like growth factor system in the developing brain
    • Werther G. A., Russo V., Baker N., and Butler G. (1998) The role of the insulin-like growth factor system in the developing brain. Horm. Res. 1, 37-40.
    • (1998) Horm. Res. , vol.1 , pp. 37-40
    • Werther, G.A.1    Russo, V.2    Baker, N.3    Butler, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.