메뉴 건너뛰기




Volumn 46, Issue , 2008, Pages 397-416

Chapter 6 Viktor Mutt: A Giant in the Field of Bioactive Peptides

Author keywords

Antibacterial peptides; Central nervous system peptides; Gastrointestinal peptides; Gut brain skin bioactive peptides; Innate immunity; Large scale native preparations; Secretin

Indexed keywords

ANIMALIA;

EID: 45849148952     PISSN: 00698032     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0069-8032(08)00006-5     Document Type: Review
Times cited : (8)

References (54)
  • 1
    • 8344224149 scopus 로고
    • On the preparation of secretin
    • Mutt V. On the preparation of secretin. Ark. Kemi. 15 (1959) 75-95
    • (1959) Ark. Kemi. , vol.15 , pp. 75-95
    • Mutt, V.1
  • 7
    • 53049109816 scopus 로고
    • "Bound" chlorine in casein and in tissue proteins
    • Mutt V. "Bound" chlorine in casein and in tissue proteins. Acta Orthopaed. Scand. 19 (1949) 300
    • (1949) Acta Orthopaed. Scand. , vol.19 , pp. 300
    • Mutt, V.1
  • 8
    • 36949085801 scopus 로고
    • Purification of secretin by freezing out of impurities from methanolic solution at -80°C
    • Jorpes E., and Mutt V. Purification of secretin by freezing out of impurities from methanolic solution at -80°C. Nature 172 (1953) 124
    • (1953) Nature , vol.172 , pp. 124
    • Jorpes, E.1    Mutt, V.2
  • 9
    • 84944484435 scopus 로고
    • The mechanism of pancreatic secretion
    • Bayliss W.M., and Starling E.H. The mechanism of pancreatic secretion. J. Physiol. 28 (1902) 325-353
    • (1902) J. Physiol. , vol.28 , pp. 325-353
    • Bayliss, W.M.1    Starling, E.H.2
  • 10
    • 0000702050 scopus 로고
    • Structure of porcine secretin. I. Degradation with trypsin and thrombin. Sequence of the tryptic peptides. The C-terminal residue
    • Mutt V., Magnusson S., Jorpes J.E., and Dahl E. Structure of porcine secretin. I. Degradation with trypsin and thrombin. Sequence of the tryptic peptides. The C-terminal residue. Biochemistry 4 (1965) 2358-2362
    • (1965) Biochemistry , vol.4 , pp. 2358-2362
    • Mutt, V.1    Magnusson, S.2    Jorpes, J.E.3    Dahl, E.4
  • 11
    • 0014847513 scopus 로고
    • Structure of porcine secretin. The amino acid sequence
    • Mutt V., Jorpes J.E., and Magnusson S. Structure of porcine secretin. The amino acid sequence. Eur. J. Biochem. 15 (1970) 513-519
    • (1970) Eur. J. Biochem. , vol.15 , pp. 513-519
    • Mutt, V.1    Jorpes, J.E.2    Magnusson, S.3
  • 13
    • 0013862039 scopus 로고
    • Cholecystokinin and pancreozymin, one single hormone?
    • Jorpes J.E., and Mutt V. Cholecystokinin and pancreozymin, one single hormone?. Acta Physiol. Scand. 66 (1966) 196-202
    • (1966) Acta Physiol. Scand. , vol.66 , pp. 196-202
    • Jorpes, J.E.1    Mutt, V.2
  • 14
    • 0029558178 scopus 로고
    • Two alternative processing pathways for a preprohormone: A bioactive form of secretin
    • Bonetto V., Jörnvall H., Mutt V., and Sillard R. Two alternative processing pathways for a preprohormone: A bioactive form of secretin. Proc. Natl. Acad. Sci. USA 92 (1995) 11985-11989
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11985-11989
    • Bonetto, V.1    Jörnvall, H.2    Mutt, V.3    Sillard, R.4
  • 17
    • 0015765676 scopus 로고
    • Immunohistochemical studies on monoamine-containing cell systems
    • Hökfelt T., Fuxe K., and Goldstein M. Immunohistochemical studies on monoamine-containing cell systems. Brain Res. 62 (1973) 461-469
    • (1973) Brain Res. , vol.62 , pp. 461-469
    • Hökfelt, T.1    Fuxe, K.2    Goldstein, M.3
  • 18
    • 0000536330 scopus 로고
    • Fluorescence of catecholamines and related compounds with formaldehyde
    • Falck B., Hillarp N.-A., Thieme G., and Torp A. Fluorescence of catecholamines and related compounds with formaldehyde. J. Histochem. Cytochem. 10 (1962) 348-354
    • (1962) J. Histochem. Cytochem. , vol.10 , pp. 348-354
    • Falck, B.1    Hillarp, N.-A.2    Thieme, G.3    Torp, A.4
  • 19
    • 0001989283 scopus 로고
    • Evidence for the existence of monoamine neurons in the central nervous system. I. Demonstration of monoamines in the cell bodies of brainstem neurons
    • Dahlström A., and Fuxe K. Evidence for the existence of monoamine neurons in the central nervous system. I. Demonstration of monoamines in the cell bodies of brainstem neurons. Acta Physiol. Scand. 62 Suppl. 232 (1964) 1-55
    • (1964) Acta Physiol. Scand. , vol.62 , Issue.SUPPL. 232 , pp. 1-55
    • Dahlström, A.1    Fuxe, K.2
  • 20
    • 0017412243 scopus 로고
    • Occurrence of somatostatin-like immunoreactivity in some peripheral sympathetic noradrenergic neurons
    • Hökfelt T., Elfvin L.G., Elde R., Schultzberg M., Goldstein M., and Luft R. Occurrence of somatostatin-like immunoreactivity in some peripheral sympathetic noradrenergic neurons. Proc. Natl. Acad. Sci. USA 74 (1977) 3587-3591
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3587-3591
    • Hökfelt, T.1    Elfvin, L.G.2    Elde, R.3    Schultzberg, M.4    Goldstein, M.5    Luft, R.6
  • 21
    • 84979112113 scopus 로고
    • On the biological assay of cholecystokinin and its dosage in cholecystography
    • Jorpes E., Mutt V., and Olbe L. On the biological assay of cholecystokinin and its dosage in cholecystography. Acta Physiol. Scand. 47 (1959) 109-114
    • (1959) Acta Physiol. Scand. , vol.47 , pp. 109-114
    • Jorpes, E.1    Mutt, V.2    Olbe, L.3
  • 22
    • 0014212851 scopus 로고
    • Isolation of aspartyl-phenylalanine amide from cholecystokinin-pancreozymin
    • Mutt V., and Jorpes J.E. Isolation of aspartyl-phenylalanine amide from cholecystokinin-pancreozymin. Biochem. Biophys. Res. Commun. 26 (1967) 392-397
    • (1967) Biochem. Biophys. Res. Commun. , vol.26 , pp. 392-397
    • Mutt, V.1    Jorpes, J.E.2
  • 23
    • 0014811685 scopus 로고
    • Further purification of a polypeptide demonstrating enterogastrone activity
    • Brown J.C., Mutt V., and Pedersen R.A. Further purification of a polypeptide demonstrating enterogastrone activity. J. Physiol. 209 (1970) 57-64
    • (1970) J. Physiol. , vol.209 , pp. 57-64
    • Brown, J.C.1    Mutt, V.2    Pedersen, R.A.3
  • 24
    • 0014965359 scopus 로고
    • Potent peripheral and splanchnic vasodilator peptide from normal gut
    • Said S.I., and Mutt V. Potent peripheral and splanchnic vasodilator peptide from normal gut. Nature 225 (1970) 863-864
    • (1970) Nature , vol.225 , pp. 863-864
    • Said, S.I.1    Mutt, V.2
  • 25
    • 0014954352 scopus 로고
    • Polypeptide with broad biological activity: Isolation from small intestine
    • Said S.I., and Mutt V. Polypeptide with broad biological activity: Isolation from small intestine. Science 169 (1970) 1217-1218
    • (1970) Science , vol.169 , pp. 1217-1218
    • Said, S.I.1    Mutt, V.2
  • 26
    • 0018837330 scopus 로고
    • N-terminally extended somatostatin: The primary structure of somatostatin-28
    • Pradayrol L., Jörnvall H., Mutt V., and Ribet A. N-terminally extended somatostatin: The primary structure of somatostatin-28. FEBS Lett. 109 (1980) 55-58
    • (1980) FEBS Lett. , vol.109 , pp. 55-58
    • Pradayrol, L.1    Jörnvall, H.2    Mutt, V.3    Ribet, A.4
  • 28
    • 0012664686 scopus 로고
    • Chemical determination of polypeptide hormones
    • Tatemoto K., and Mutt V. Chemical determination of polypeptide hormones. Proc. Natl. Acad. Sci. USA 75 (1978) 4115-4119
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4115-4119
    • Tatemoto, K.1    Mutt, V.2
  • 29
    • 0019310264 scopus 로고
    • Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides
    • Tatemoto K., and Mutt V. Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides. Nature 285 (1980) 417-418
    • (1980) Nature , vol.285 , pp. 417-418
    • Tatemoto, K.1    Mutt, V.2
  • 30
    • 0019944850 scopus 로고
    • Neuropeptide Y: A novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide (PP)
    • Tatemoto K., Carlquist M., and Mutt V. Neuropeptide Y: A novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide (PP). Nature 296 (1982) 659-660
    • (1982) Nature , vol.296 , pp. 659-660
    • Tatemoto, K.1    Carlquist, M.2    Mutt, V.3
  • 33
    • 0021871961 scopus 로고
    • Neuropeptide K: Isolation, structure and biological activities of a novel brain tachykinin
    • Tatemoto K., Lundberg J.M., Jörnvall H., and Mutt V. Neuropeptide K: Isolation, structure and biological activities of a novel brain tachykinin. Biochem. Biophys. Res. Commun. 128 (1985) 947-953
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 947-953
    • Tatemoto, K.1    Lundberg, J.M.2    Jörnvall, H.3    Mutt, V.4
  • 34
    • 0023035470 scopus 로고
    • Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion
    • Tatemoto K., Efendic S., Mutt V., Makk G., Feistner G.J., and Barchas J.D. Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion. Nature 324 (1986) 476-478
    • (1986) Nature , vol.324 , pp. 476-478
    • Tatemoto, K.1    Efendic, S.2    Mutt, V.3    Makk, G.4    Feistner, G.J.5    Barchas, J.D.6
  • 35
    • 0024853901 scopus 로고
    • Isolation and characterization of a 60-residue intestinal peptide structurally related to the pancreatic secretory type of trypsin inhibitor: Influence on insulin secretion
    • Agerberth B., Söderling-Barros J., Jörnvall H., Chen Z.-W., Östenson C.-G., Efendic S., and Mutt V. Isolation and characterization of a 60-residue intestinal peptide structurally related to the pancreatic secretory type of trypsin inhibitor: Influence on insulin secretion. Proc. Natl. Acad. Sci. USA 86 (1989) 8590-8594
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8590-8594
    • Agerberth, B.1    Söderling-Barros, J.2    Jörnvall, H.3    Chen, Z.-W.4    Östenson, C.-G.5    Efendic, S.6    Mutt, V.7
  • 36
    • 0030050233 scopus 로고    scopus 로고
    • Endosulfine, endogenous ligand for the sulphonylurea receptor: Isolation from porcine brain and partial structural determination of the alpha form
    • Virsolvy-Vergine A., Salazar G., Sillard R., Denoroy L., Mutt V., and Bataille D. Endosulfine, endogenous ligand for the sulphonylurea receptor: Isolation from porcine brain and partial structural determination of the alpha form. Diabetologia 39 (1996) 135-141
    • (1996) Diabetologia , vol.39 , pp. 135-141
    • Virsolvy-Vergine, A.1    Salazar, G.2    Sillard, R.3    Denoroy, L.4    Mutt, V.5    Bataille, D.6
  • 38
    • 0031441884 scopus 로고    scopus 로고
    • Identification, isolation and characterization of daintain (allograft inflammatory factor-1), a macrophage polypeptide with effects on insulin secretion and abundantly present in the pancreas of prediabetic BB rats
    • Chen Z.-W., Ahren B., Östenson C.-G., Cintra A., Bergman T., Möller C., Fuxe V., Jörnvall H., and Efendic S. Identification, isolation and characterization of daintain (allograft inflammatory factor-1), a macrophage polypeptide with effects on insulin secretion and abundantly present in the pancreas of prediabetic BB rats. Proc. Natl. Acad. Sci. USA 94 (1997) 13879-13884
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13879-13884
    • Chen, Z.-W.1    Ahren, B.2    Östenson, C.-G.3    Cintra, A.4    Bergman, T.5    Möller, C.6    Fuxe, V.7    Jörnvall, H.8    Efendic, S.9
  • 39
    • 0029051333 scopus 로고
    • Cloning and characterization of allograft inflammatory factor-1: A novel macrophage factor identified in rat cardiac allografts with chronic rejection
    • Utans U., Arceci R.J., Yamashita Y., and Russell M.E. Cloning and characterization of allograft inflammatory factor-1: A novel macrophage factor identified in rat cardiac allografts with chronic rejection. J. Clin. Invest. 95 (1995) 2954-2962
    • (1995) J. Clin. Invest. , vol.95 , pp. 2954-2962
    • Utans, U.1    Arceci, R.J.2    Yamashita, Y.3    Russell, M.E.4
  • 40
    • 0030296804 scopus 로고    scopus 로고
    • cDNA cloning of human allograft inflammatory factor-1: Tissue distribution, cytokine induction, and mRNA expression in injured rat carotid arteries
    • Autieri M.-V. cDNA cloning of human allograft inflammatory factor-1: Tissue distribution, cytokine induction, and mRNA expression in injured rat carotid arteries. Biochem. Biophys. Res. Commun. 228 (1996) 29-37
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 29-37
    • Autieri, M.-V.1
  • 41
    • 0015055323 scopus 로고
    • The further purification of motilin, a gastric motor activity stimulating polypeptide from the mucosa of the small intestine of hogs
    • Brown J.C., Mutt V., and Dryburgh J.R. The further purification of motilin, a gastric motor activity stimulating polypeptide from the mucosa of the small intestine of hogs. Can. J. Physiol. Pharmacol. 49 (1971) 399-405
    • (1971) Can. J. Physiol. Pharmacol. , vol.49 , pp. 399-405
    • Brown, J.C.1    Mutt, V.2    Dryburgh, J.R.3
  • 42
    • 0027303260 scopus 로고
    • Isolation of three antibacterial peptides from pig intestine: Gastric inhibitory polypeptide (7-42), diazepam-binding inhibitor (32-86) and a novel factor, peptide 3910
    • Agerberth B., Boman A., Andersson M., Jörnvall H., Mutt V., and Boman H.G. Isolation of three antibacterial peptides from pig intestine: Gastric inhibitory polypeptide (7-42), diazepam-binding inhibitor (32-86) and a novel factor, peptide 3910. Eur. J. Biochem. 216 (1993) 623-629
    • (1993) Eur. J. Biochem. , vol.216 , pp. 623-629
    • Agerberth, B.1    Boman, A.2    Andersson, M.3    Jörnvall, H.4    Mutt, V.5    Boman, H.G.6
  • 44
    • 17344379931 scopus 로고
    • An appreciation of the work of Vittorio Erspamer
    • Mutt V. An appreciation of the work of Vittorio Erspamer. Peptides 2 Suppl 2 (1981) 3-6
    • (1981) Peptides , vol.2 , Issue.SUPPL. 2 , pp. 3-6
    • Mutt, V.1
  • 45
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engström A., Bennich H., and Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292 (1981) 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engström, A.3    Bennich, H.4    Boman, H.G.5
  • 46
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84 (1987) 5449-5453
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 48
    • 0037362455 scopus 로고    scopus 로고
    • Ascaris nematodes from pig and human make three antibacterial peptides: Isolation of cecropin P1 and two ASABF peptides
    • Andersson M., Boman A., and Boman H.G. Ascaris nematodes from pig and human make three antibacterial peptides: Isolation of cecropin P1 and two ASABF peptides. Cell. Mol. Life Sci. 60 (2003) 599-606
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 599-606
    • Andersson, M.1    Boman, A.2    Boman, H.G.3
  • 50
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides
    • Agerberth B., Lee J.-Y., Bergman T., Carlquist M., Boman H.G., Mutt V., and Jörnvall H. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur. J. Biochem. 202 (1991) 849-854
    • (1991) Eur. J. Biochem. , vol.202 , pp. 849-854
    • Agerberth, B.1    Lee, J.-Y.2    Bergman, T.3    Carlquist, M.4    Boman, H.G.5    Mutt, V.6    Jörnvall, H.7
  • 52
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov R., and Janeway Jr. C.A. Innate immunity: The virtues of a nonclonal system of recognition. Cell 91 (1997) 295-298
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 53
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R., Preston-Hurlburt P., and Janeway Jr. C.A. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388 (1997) 394-397
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 54


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.