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Volumn 34, Issue 6, 2009, Pages 853-872

A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen synthesis

Author keywords

Collagen; Collagen synthesis; Collagen turnover; Essential amino acid; Glycine; Glycine metabolism; Osteoarthritis; Osteoporosis

Indexed keywords

CARBON; COLLAGEN; GLUTATHIONE; GLYCINE; GLYCINE HYDROXYMETHYLTRANSFERASE; GLYOXYLIC ACID; GLYOXYLIC ACID DERIVATIVE; PORPHYRIN; SERINE;

EID: 77949890874     PISSN: 02505991     EISSN: 09737138     Source Type: Journal    
DOI: 10.1007/s12038-009-0100-9     Document Type: Article
Times cited : (111)

References (118)
  • 2
    • 33750948078 scopus 로고    scopus 로고
    • Insights into early extracellular matrix evolution: Spongin short chain collagen-related proteins are homologous to basement membrane type IV collagens and form a novel family widely distributed in invertebrates
    • Aouacheria A, Geourjon C, Aghajari N, Navratil V, Deléage G, Lethias C and Exposito J-Y 2006 Insights into early extracellular matrix evolution: spongin short chain collagen-related proteins are homologous to basement membrane type IV collagens and form a novel family widely distributed in invertebrates; Mol. Biol. Evol. 23 2288-2302
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 2288-2302
    • Aouacheria, A.1    Geourjon, C.2    Aghajari, N.3    Navratil, V.4    Deléage, G.5    Lethias, C.6    Exposito, J.-Y.7
  • 8
    • 33644756678 scopus 로고    scopus 로고
    • Reconstruction of human hepatocyte glyoxylate metabolic pathways in stably transformed Chinese-hamster ovary cells
    • Behnam J T, Williams E L, Brink S, Rumsby G and Danpure C J 2006 Reconstruction of human hepatocyte glyoxylate metabolic pathways in stably transformed Chinese-hamster ovary cells; Biochem. J. 394 409-416
    • (2006) Biochem. J. , vol.394 , pp. 409-416
    • Behnam, J.T.1    Williams, E.L.2    Brink, S.3    Rumsby, G.4    Danpure, C.J.5
  • 9
    • 0019050844 scopus 로고
    • Regulation of the production of secretory proteins: Intracellular degradation of newly synthesized 'defective' collagen
    • Berg R A, Schwartz M L and Crystal R G 1980 Regulation of the production of secretory proteins: intracellular degradation of newly synthesized 'defective' collagen; Proc. Natl. Acad. Sci. USA 77 4746-4750
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4746-4750
    • Berg, R.A.1    Schwartz, M.L.2    Crystal, R.G.3
  • 11
    • 0020566215 scopus 로고
    • Intracellular degradation of newly synthesized secretory proteins
    • Bienkowski R S 1983 Intracellular degradation of newly synthesized secretory proteins; Biochem. J. 214 1-10
    • (1983) Biochem. J. , vol.214 , pp. 1-10
    • Bienkowski, R.S.1
  • 12
    • 0019843288 scopus 로고
    • Measurement of intracellular collagen degradation
    • Bienkowski R S and Engels C J 1981 Measurement of intracellular collagen degradation; Anal. Biochem. 116 414-424
    • (1981) Anal. Biochem. , vol.116 , pp. 414-424
    • Bienkowski, R.S.1    Engels, C.J.2
  • 13
    • 0018275598 scopus 로고
    • Fibroblasts degrade newly synthesised collagen within the cell before secretion
    • (London)
    • Bienkowski R S, Baum B J and Crystal R G 1978a Fibroblasts degrade newly synthesised collagen within the cell before secretion; Nature (London) 276 413-416
    • (1978) Nature , vol.276 , pp. 413-416
    • Bienkowski, R.S.1    Baum, B.J.2    Crystal, R.G.3
  • 15
    • 0036606746 scopus 로고    scopus 로고
    • Mechanisms balancing skeletal matrix synthesis and degradation
    • Blair H C, Zaidi M and Schlesinger P H 2002 Mechanisms balancing skeletal matrix synthesis and degradation; Biochem. J. 364 329-341
    • (2002) Biochem. J. , vol.364 , pp. 329-341
    • Blair, H.C.1    Zaidi, M.2    Schlesinger, P.H.3
  • 17
    • 0019800423 scopus 로고
    • Stimulation of the elastolytic activity of leukocyte elastase by leukocyte cathepsin G
    • Boudier C, Holle C and Bieth J G 1981 Stimulation of the elastolytic activity of leukocyte elastase by leukocyte cathepsin G; J. Biol. Chem. 256 10256-10258
    • (1981) J. Biol. Chem. , vol.256 , pp. 10256-10258
    • Boudier, C.1    Holle, C.2    Bieth, J.G.3
  • 18
    • 0014735858 scopus 로고
    • Dietary protein level and uric acid metabolism in normal man
    • Bowering J, Calloway D H, Margen S and Kaufmann N A 1970 Dietary protein level and uric acid metabolism in normal man; J. Nutr. 100 249-261
    • (1970) J. Nutr. , vol.100 , pp. 249-261
    • Bowering, J.1    Calloway, D.H.2    Margen, S.3    Kaufmann, N.A.4
  • 19
    • 0016608835 scopus 로고
    • Collagen in the human lung. Quantitation of rates of synthesis and partial characterization of composition
    • Bradley K, McConnell-Breul D and Crystal R G 1975 Collagen in the human lung. Quantitation of rates of synthesis and partial characterization of composition; J. Clin. Invest. 55 543-550
    • (1975) J. Clin. Invest. , vol.55 , pp. 543-550
    • Bradley, K.1    McConnell-Breul, D.2    Crystal, R.G.3
  • 22
    • 0020201899 scopus 로고
    • Interorgan amino acid nutrition
    • Christensen H N 1982 Interorgan amino acid nutrition; Physiol. Rev. 62 1193-1233
    • (1982) Physiol. Rev. , vol.62 , pp. 1193-1233
    • Christensen, H.N.1
  • 23
    • 0021233378 scopus 로고
    • Glycine N-methyltransferase is a folate binding protein of rat liver cytosol
    • Cook R J and Wagner C 1984 Glycine N-methyltransferase is a folate binding protein of rat liver cytosol; Proc. Natl. Acad. Sci. USA 81 3631-3634
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3631-3634
    • Cook, R.J.1    Wagner, C.2
  • 24
  • 25
    • 84878085969 scopus 로고
    • The metabolism of glyoxylate by human- and rat-liver mitochondria
    • Crawhall J C and Watts R W 1962 The metabolism of glyoxylate by human- and rat-liver mitochondria; Biochem. J. 85 163-171
    • (1962) Biochem. J. , vol.85 , pp. 163-171
    • Crawhall, J.C.1    Watts, R.W.2
  • 26
    • 73049165895 scopus 로고
    • The formation of free hydroxyproline by rat cartilage in vitro
    • Daughaday W H and Mariz I K 1962 The formation of free hydroxyproline by rat cartilage in vitro; J. Biol. Chem. 237 2831-2835
    • (1962) J. Biol. Chem. , vol.237 , pp. 2831-2835
    • Daughaday, W.H.1    Mariz, I.K.2
  • 28
    • 0016920764 scopus 로고
    • The blood-brain barrier
    • Davson 1976 The blood-brain barrier; J. Physiol. 255 1-28
    • (1976) J. Physiol. , vol.255 , pp. 1-28
    • Davson1
  • 30
    • 25444454330 scopus 로고    scopus 로고
    • The end-product method of measuring whole-body protein turnover: A review of published results and a comparison with those obtained by leucine infusion
    • Duggleby S L and Waterlow J C 2005 The end-product method of measuring whole-body protein turnover: a review of published results and a comparison with those obtained by leucine infusion; Br. J. Nutr. 94 141-153
    • (2005) Br. J. Nutr. , vol.94 , pp. 141-153
    • Duggleby, S.L.1    Waterlow, J.C.2
  • 32
    • 33845442764 scopus 로고    scopus 로고
    • Articular cartilage collagen: An irreplaceable framework?
    • Eyre D R, Weis M A and Wu J J 2006 Articular cartilage collagen: an irreplaceable framework? Eur. Cell. Mater. 12 57-63
    • (2006) Eur. Cell. Mater. , vol.12 , pp. 57-63
    • Eyre, D.R.1    Weis, M.A.2    Wu, J.J.3
  • 33
    • 0003526098 scopus 로고
    • Energy and protein requirements
    • FAO/WHO/UNU
    • FAO/WHO/UNU 1985 Energy and protein requirements; FAO/WHO/UNU Tech. Rep. Ser. 724 1-206
    • (1985) FAO/WHO/UNU Tech. Rep. Ser , vol.724 , pp. 1-206
  • 35
    • 0015791633 scopus 로고
    • The specific radioactivity of the precursor pool for estimates of the rate of protein synthesis
    • Fern E B and Garlick P J 1973 The specific radioactivity of the precursor pool for estimates of the rate of protein synthesis; Biochem. J. 134 1127-1130
    • (1973) Biochem. J. , vol.134 , pp. 1127-1130
    • Fern, E.B.1    Garlick, P.J.2
  • 38
    • 0014497563 scopus 로고
    • Bone matrix turnover and balance in vitro II, the effects of ageing
    • Flanagan B and Nichols G 1969 Bone matrix turnover and balance in vitro II, the effects of ageing; J. Clin. Invest. 48 607-612
    • (1969) J. Clin. Invest. , vol.48 , pp. 607-612
    • Flanagan, B.1    Nichols, G.2
  • 39
    • 0029991011 scopus 로고    scopus 로고
    • Plasma methionine and cysteine kinetics in response to an intravenous glutathione infusion in adult humans
    • Fukagawa N K, Ajami A M and Young V R 1996 Plasma methionine and cysteine kinetics in response to an intravenous glutathione infusion in adult humans; Am. J. Physiol. 270 E209-E214
    • (1996) Am. J. Physiol. , vol.270
    • Fukagawa, N.K.1    Ajami, A.M.2    Young, V.R.3
  • 40
    • 0036178069 scopus 로고    scopus 로고
    • Endogenous glycine and tyrosine production is maintained in adults consuming a marginal-protein diet
    • Gibson N R, Jahoor F, Ware L and Jackson A A 2002 Endogenous glycine and tyrosine production is maintained in adults consuming a marginal-protein diet; Am. J. Clin. Nutr. 75 511-518
    • (2002) Am. J. Clin. Nutr. , vol.75 , pp. 511-518
    • Gibson, N.R.1    Jahoor, F.2    Ware, L.3    Jackson, A.A.4
  • 41
    • 0017237086 scopus 로고
    • Lung collagen heterogeneity. Synthesis of type I and type III collagen by rabbit and human lung cells in culture
    • Hance A J, Bradley K and Crystal R G 1976 Lung collagen heterogeneity. Synthesis of type I and type III collagen by rabbit and human lung cells in culture; J. Clin. Invest. 57 102-111
    • (1976) J. Clin. Invest. , vol.57 , pp. 102-111
    • Hance, A.J.1    Bradley, K.2    Crystal, R.G.3
  • 42
    • 0034733820 scopus 로고    scopus 로고
    • Regulating the cellular economy of supply and demand
    • Hofmeyr J-H S and Cornish-Bowden A 2000 Regulating the cellular economy of supply and demand; FEBS Lett. 476 47-51
    • (2000) FEBS Lett. , vol.476 , pp. 47-51
    • Hofmeyr, J.-H.S.1    Cornish-Bowden, A.2
  • 43
    • 0035658518 scopus 로고    scopus 로고
    • Threonine metabolism in isolated rat hepatocytes
    • House J D, Hall B N and Brosnan J T 2001 Threonine metabolism in isolated rat hepatocytes; Am. J. Physiol. 281 E1300-E1307
    • (2001) Am. J. Physiol. , vol.281
    • House, J.D.1    Hall, B.N.2    Brosnan, J.T.3
  • 44
    • 0017360262 scopus 로고
    • Chemical and histochemical studies of human alveolar collagen fibers
    • Huang W 1977 Chemical and histochemical studies of human alveolar collagen fibers; Am. J. Pathol. 86 81-97
    • (1977) Am. J. Pathol. , vol.86 , pp. 81-97
    • Huang, W.1
  • 47
    • 0023622455 scopus 로고
    • Urinary excretion of 5-oxoproline (pyroglutamic aciduria) as an index of glycine insufficiency in normal man
    • Jackson A A, Badaloo A V, Forrester T, Hibbert J M and Persaud C 1987 Urinary excretion of 5-oxoproline (pyroglutamic aciduria) as an index of glycine insufficiency in normal man; Br. J Nutr. 58 207-214
    • (1987) Br. J Nutr. , vol.58 , pp. 207-214
    • Jackson, A.A.1    Badaloo, A.V.2    Forrester, T.3    Hibbert, J.M.4    Persaud, C.5
  • 48
    • 0029909031 scopus 로고    scopus 로고
    • Urinary excretion of 5-L-oxoproline (pyroglutamic acid) is increased in normal adults consuming vegetarian or low protein diets
    • Jackson A A, Persaud C, Meakins T S and Bundy R 1996 Urinary excretion of 5-L-oxoproline (pyroglutamic acid) is increased in normal adults consuming vegetarian or low protein diets; J. Nutr. 126 2813-2822
    • (1996) J. Nutr. , vol.126 , pp. 2813-2822
    • Jackson, A.A.1    Persaud, C.2    Meakins, T.S.3    Bundy, R.4
  • 49
    • 0036907143 scopus 로고    scopus 로고
    • Increased systolic blood pressure in rats induced by a maternal low-protein diet is reversed by dietary supplementation with glycine
    • Jackson A A, Dunn R L, Marchand MC and Langley-Evans S C 2002 Increased systolic blood pressure in rats induced by a maternal low-protein diet is reversed by dietary supplementation with glycine; Clin. Sci. (London). 103 633-639
    • (2002) Clin. Sci. (London). , vol.103 , pp. 633-639
    • Jackson, A.A.1    Dunn, R.L.2    Marchand, M.C.3    Langley-Evans, S.C.4
  • 50
    • 0032981639 scopus 로고    scopus 로고
    • A model of whole-body protein turnover based on leucine kinetics in rodents
    • Johnson H A, Baldwin R L, France J and Calvert C C 1999 A model of whole-body protein turnover based on leucine kinetics in rodents; J. Nutr. 129 728-739
    • (1999) J. Nutr. , vol.129 , pp. 728-739
    • Johnson, H.A.1    Baldwin, R.L.2    France, J.3    Calvert, C.C.4
  • 52
    • 0021081492 scopus 로고
    • Measurement of the absolute synthesis of soluble and insoluble elastin by chick aortic tissue
    • Keeley F W and Johnson D J 1983 Measurement of the absolute synthesis of soluble and insoluble elastin by chick aortic tissue; Can. J. Biochem. Cell. Biol. 61 1079-1084
    • (1983) Can. J. Biochem. Cell. Biol. , vol.61 , pp. 1079-1084
    • Keeley, F.W.1    Johnson, D.J.2
  • 53
    • 84957355538 scopus 로고
    • Body size and metabolic rate
    • Kleiber M 1947 Body size and metabolic rate; Physiol. Rev. 27 511-541
    • (1947) Physiol. Rev. , vol.27 , pp. 511-541
    • Kleiber, M.1
  • 54
    • 0016750884 scopus 로고
    • Evidence that histidine is an essential amino acid in normal and chronically uremic man
    • Kopple J D and Swendseid M E 1975 Evidence that histidine is an essential amino acid in normal and chronically uremic man; J. Clin. Invest. 55 881-891
    • (1975) J. Clin. Invest. , vol.55 , pp. 881-891
    • Kopple, J.D.1    Swendseid, M.E.2
  • 56
    • 0017073669 scopus 로고
    • The regulation of folate and methionine metabolism
    • Krebs H A, Hems R and Tyler B 1976 The regulation of folate and methionine metabolism; Biochem. J. 158 341-353
    • (1976) Biochem. J. , vol.158 , pp. 341-353
    • Krebs, H.A.1    Hems, R.2    Tyler, B.3
  • 58
    • 15944411011 scopus 로고    scopus 로고
    • Low serine hydroxy-methyltransferase activity in the human placenta has important implications for fetal glycine supply
    • Lewis R M, Godfrey K M, Jackson A A, Cameron I T and Hanson M A 2005 Low serine hydroxy-methyltransferase activity in the human placenta has important implications for fetal glycine supply; J. Clin. Endocrinol. Metab. 90 1594-1598
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 1594-1598
    • Lewis, R.M.1    Godfrey, K.M.2    Jackson, A.A.3    Cameron, I.T.4    Hanson, M.A.5
  • 59
    • 0032488780 scopus 로고    scopus 로고
    • Precambrian sponges with cellular structures
    • Li C W, Chen J Y and Hua T E 1998 Precambrian sponges with cellular structures; Science 279 879-882
    • (1998) Science , vol.279 , pp. 879-882
    • Li, C.W.1    Chen, J.Y.2    Hua, T.E.3
  • 60
    • 0034871510 scopus 로고    scopus 로고
    • Dietary glycine prevents peptidoglycan polysaccharide-induced reactive arthritis in the rat: Role for glycine-gated chloride channel
    • Li X, Bradford B U, Wheeler M D, Stimpson S A, Pink, H M, Brodie T A, Schwab J H and Thurman R G 2001 Dietary glycine prevents peptidoglycan polysaccharide-induced reactive arthritis in the rat: role for glycine-gated chloride channel; Infect. Immun. 69 5883-5891
    • (2001) Infect. Immun. , vol.69 , pp. 5883-5891
    • Li, X.1    Bradford, B.U.2    Wheeler, M.D.3    Stimpson, S.A.4    Pink, H.M.5    Brodie, T.A.6    Schwab, J.H.7    Thurman, R.G.8
  • 61
    • 10244234102 scopus 로고    scopus 로고
    • Procollagen II C-propeptide in joint fluid: Changes in concentration with age, time after knee injury, and osteoarthritis
    • Lohmander L S, Yoshihara Y, Roos H, Kobayashi T, Yamada H and Shinmei M 1996 Procollagen II C-propeptide in joint fluid: changes in concentration with age, time after knee injury, and osteoarthritis; J. Rheumatol. 23 1765-1769
    • (1996) J. Rheumatol. , vol.23 , pp. 1765-1769
    • Lohmander, L.S.1    Yoshihara, Y.2    Roos, H.3    Kobayashi, T.4    Yamada, H.5    Shinmei, M.6
  • 62
    • 0242663609 scopus 로고    scopus 로고
    • The release of crosslinked peptides from type II collagen into human synovial fluid is increased soon after joint injury and in osteoarthritis
    • Lohmander L S, Atley L M, Pietka T A and Eyre D R 2003 The release of crosslinked peptides from type II collagen into human synovial fluid is increased soon after joint injury and in osteoarthritis; Arthr. Rheum. 48 3130-3139
    • (2003) Arthr. Rheum. , vol.48 , pp. 3130-3139
    • Lohmander, L.S.1    Atley, L.M.2    Pietka, T.A.3    Eyre, D.R.4
  • 64
    • 0000754558 scopus 로고
    • The determination of collagen and elastin in tissues with results obtained in various normal tissues from different species
    • Lowry O H, Gilligan D R and Katersky E M 1941 The determination of collagen and elastin in tissues with results obtained in various normal tissues from different species; J. Biol. Chem. 139 795-804
    • (1941) J. Biol. Chem. , vol.139 , pp. 795-804
    • Lowry, O.H.1    Gilligan, D.R.2    Katersky, E.M.3
  • 66
    • 0023709126 scopus 로고
    • In vivo oxidation of the methyl group of hepatic 5-methyltetrahydrofolate
    • Lumb M, Chanarin I, Deacon R and Perry J 1988 In vivo oxidation of the methyl group of hepatic 5-methyltetrahydrofolate; J. Clin. Pathol. 41 1158-1162
    • (1988) J. Clin. Pathol. , vol.41 , pp. 1158-1162
    • Lumb, M.1    Chanarin, I.2    Deacon, R.3    Perry, J.4
  • 68
    • 0024513871 scopus 로고
    • Oxidation of 5-methyltetrahydrofolate in cobalamin-inactivated rats
    • Lumb M, Deacon R, Perry J and Chanarin I 1989b Oxidation of 5-methyltetrahydrofolate in cobalamin-inactivated rats; Biochem. J. 258 907-910
    • (1989) Biochem. J. , vol.258 , pp. 907-910
    • Lumb, M.1    Deacon, R.2    Perry, J.3    Chanarin, I.4
  • 69
    • 0017990701 scopus 로고
    • Osteoarthrosis in a coyote × dog hybrid from nebraska
    • Mahan B R 1978 Osteoarthrosis in a coyote × dog hybrid from Nebraska; J. Wildl. Dis. 14 395-398
    • (1978) J. Wildl. Dis. , vol.14 , pp. 395-398
    • Mahan, B.R.1
  • 70
    • 2642555594 scopus 로고    scopus 로고
    • The intracellular free amino acid pool represents tracer precursor enrichment for calculation of protein synthesis in cultured fibroblasts and myocytes
    • Martini W Z, Chinkes D L and Wolfe R R 2004 The intracellular free amino acid pool represents tracer precursor enrichment for calculation of protein synthesis in cultured fibroblasts and myocytes; J. Nutr. 134 1546-1550
    • (2004) J. Nutr. , vol.134 , pp. 1546-1550
    • Martini, W.Z.1    Chinkes, D.L.2    Wolfe, R.R.3
  • 71
    • 0025822677 scopus 로고
    • Age-related changes in collagen synthesis and degradation in rat tissues. Importance of degradation of newly synthesized collagen in regulating collagen production
    • Mays P K, McAnulty R J, Campa J S and Laurent G J 1991 Age-related changes in collagen synthesis and degradation in rat tissues. Importance of degradation of newly synthesized collagen in regulating collagen production; Biochem. J. 276 307-313
    • (1991) Biochem. J. , vol.276 , pp. 307-313
    • Mays, P.K.1    McAnulty, R.J.2    Campa, J.S.3    Laurent, G.J.4
  • 73
    • 59449102307 scopus 로고    scopus 로고
    • Branch-point stoichiometry can generate weak links in metabolism: The case of glycine biosynthesis
    • Meléndez-Hevia E and de Paz-Lugo P 2008 Branch-point stoichiometry can generate weak links in metabolism: the case of glycine biosynthesis; J. Biosci. 33 771-780
    • (2008) J. Biosci. , vol.33 , pp. 771-780
    • Meléndez-Hevia, E.1    De Paz-Lugo, P.2
  • 75
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A 1988 Glutathione metabolism and its selective modification; J. Biol. Chem. 263 17205-17208
    • (1988) J. Biol. Chem. , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 77
    • 0041355216 scopus 로고    scopus 로고
    • Hydroxylation-induced stabilization of the collagen triple helix. Further characterization of peptides with 4(R)-hydroxyproline in the xaa position
    • Mizuno K, Hayashi T and Bachinger H P 2003 Hydroxylation-induced stabilization of the collagen triple helix. Further characterization of peptides with 4(R)-hydroxyproline in the Xaa position; J. Biol. Chem. 278 32373-32379
    • (2003) J. Biol. Chem. , vol.278 , pp. 32373-32379
    • Mizuno, K.1    Hayashi, T.2    Bachinger, H.P.3
  • 78
    • 0016722112 scopus 로고
    • Labile methyl balances for normal humans on various dietary regimens
    • Mudd S H and Poole J R 1975 Labile methyl balances for normal humans on various dietary regimens; Metabolism 24 721-735
    • (1975) Metabolism , vol.24 , pp. 721-735
    • Mudd, S.H.1    Poole, J.R.2
  • 79
    • 0018934312 scopus 로고
    • Labile methyl group balances in the human: The role of sarcosine
    • Mudd S H, Ebert M H and Scriver C R 1980 Labile methyl group balances in the human: the role of sarcosine; Metabolism 29 707-720
    • (1980) Metabolism , vol.29 , pp. 707-720
    • Mudd, S.H.1    Ebert, M.H.2    Scriver, C.R.3
  • 82
    • 0019153325 scopus 로고
    • Methionine synthesis aminoimidazole carboxamide excretion and folate levels in pregnant rats
    • N'Diaye F, Hitier Y, Courcy G P d, Goubern M and Bourdel G 1980 Methionine synthesis aminoimidazole carboxamide excretion and folate levels in pregnant rats; J. Nutr. 110 522-531
    • (1980) J. Nutr. , vol.110 , pp. 522-531
    • N'Diaye, F.1    Hitier, Y.2    Courcy, G.P.D.3    Goubern, M.4    Bourdel, G.5
  • 83
    • 76549214686 scopus 로고
    • The determination of collagen and elastin in tissues
    • Neuman R E and Logan M A 1950 The determination of collagen and elastin in tissues; J. Biol. Chem. 186 549-556
    • (1950) J. Biol. Chem. , vol.186 , pp. 549-556
    • Neuman, R.E.1    Logan, M.A.2
  • 84
    • 0018547050 scopus 로고
    • Plasma amino acid turnover rates and pools in rabbits: In vivo studies using stable isotopes
    • Nissim I and Lapidot A 1979 Plasma amino acid turnover rates and pools in rabbits: in vivo studies using stable isotopes; Am. J. Physiol. 237 E418-E427
    • (1979) Am. J. Physiol. , vol.237
    • Nissim, I.1    Lapidot, A.2
  • 86
    • 0019380807 scopus 로고
    • Whole body protein synthesis and turnover in normal man and malnourished patients with and without known cancer
    • Norton J A, Stein T P and Brennan M F 1981 Whole body protein synthesis and turnover in normal man and malnourished patients with and without known cancer; Ann. Surg. 194 123-128
    • (1981) Ann. Surg. , vol.194 , pp. 123-128
    • Norton, J.A.1    Stein, T.P.2    Brennan, M.F.3
  • 87
    • 0019165604 scopus 로고
    • Measurement of the synthesis rates of collagens and total protein in rabbit muscle
    • Palmer R M, Robins S P and Lobley G E 1980 Measurement of the synthesis rates of collagens and total protein in rabbit muscle; Biochem. J. 192 631-636
    • (1980) Biochem. J. , vol.192 , pp. 631-636
    • Palmer, R.M.1    Robins, S.P.2    Lobley, G.E.3
  • 90
    • 0035941338 scopus 로고    scopus 로고
    • Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation
    • Perret S, Merle C, Bernocco S, Berland P, Garrone R, Hulmes D J, Theisen M and Ruggiero F 2001 Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation; J. Biol. Chem. 276 43693-43698
    • (2001) J. Biol. Chem. , vol.276 , pp. 43693-43698
    • Perret, S.1    Merle, C.2    Bernocco, S.3    Berland, P.4    Garrone, R.5    Hulmes, D.J.6    Theisen, M.7    Ruggiero, F.8
  • 91
    • 0029910652 scopus 로고    scopus 로고
    • Urinary excretion of 5-L-oxoproline (pyroglutamic acid) is increased during recovery from severe childhood malnutrition and responds to supplemental glycine
    • Persaud C, Forrester T and Jackson A A 1996 Urinary excretion of 5-L-oxoproline (pyroglutamic acid) is increased during recovery from severe childhood malnutrition and responds to supplemental glycine; J. Nutr. 126 2823-2830
    • (1996) J. Nutr. , vol.126 , pp. 2823-2830
    • Persaud, C.1    Forrester, T.2    Jackson, A.A.3
  • 92
    • 0001988920 scopus 로고
    • Studies on the collagen and elastin content of the human lung
    • Pierce J A and Hocott J B 1960 Studies on the collagen and elastin content of the human lung; J. Clin. Invest. 39 8-14
    • (1960) J. Clin. Invest. , vol.39 , pp. 8-14
    • Pierce, J.A.1    Hocott, J.B.2
  • 93
    • 0021362187 scopus 로고
    • Kinetic compartmental analysis of carnitine metabolism in the human carnitine deficiency syndromes. Evidence for alterations in tissue carnitine transport
    • Rebouche C J and Engel A G 1984 Kinetic compartmental analysis of carnitine metabolism in the human carnitine deficiency syndromes. Evidence for alterations in tissue carnitine transport; J. Clin. Invest. 73 857-867
    • (1984) J. Clin. Invest. , vol.73 , pp. 857-867
    • Rebouche, C.J.1    Engel, A.G.2
  • 94
    • 0031816464 scopus 로고    scopus 로고
    • Carnitine metabolism and its regulation in microorganisms and mammals
    • Rebouche C J and Seim H 1998 Carnitine metabolism and its regulation in microorganisms and mammals; Annu. Rev. Nutr. 18 39-61
    • (1998) Annu. Rev. Nutr. , vol.18 , pp. 39-61
    • Rebouche, C.J.1    Seim, H.2
  • 96
    • 0015111666 scopus 로고
    • Collagen synthesis in mature articular cartilage of the rabbit
    • Repo R U and Mitchell N 1971 Collagen synthesis in mature articular cartilage of the rabbit; J. Bone Joint Surg. 53 541-548
    • (1971) J. Bone Joint Surg. , vol.53 , pp. 541-548
    • Repo, R.U.1    Mitchell, N.2
  • 97
    • 0008505655 scopus 로고
    • The allometric relationship of skeleton weight to body weight in teleost fishes: A preliminary comparison with birds and mammals
    • Reynolds W W and Karlotski W J 1977 The allometric relationship of skeleton weight to body weight in teleost fishes: a preliminary comparison with birds and mammals; Copeia 1977 160-163
    • (1977) Copeia 1977 , pp. 160-163
    • Reynolds, W.W.1    Karlotski, W.J.2
  • 98
    • 0343317519 scopus 로고
    • Studies on the skeletal tissues. II. The collagen content of bones from rabbits oxen and humans
    • Rogers H J, Weidmann S M and Parkinson A 1952 Studies on the skeletal tissues. II. The collagen content of bones from rabbits oxen and humans; Biochem. J. 50 537-542
    • (1952) Biochem. J. , vol.50 , pp. 537-542
    • Rogers, H.J.1    Weidmann, S.M.2    Parkinson, A.3
  • 99
    • 0027422979 scopus 로고
    • Extracellular matrix 4: The elastic fiber
    • Rosenbloom J, Abrams W R and Mecham R 1993 Extracellular matrix 4: the elastic fiber; FASEB. J. 7 1208-1218
    • (1993) FASEB. J. , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 100
    • 0021646130 scopus 로고
    • Elastin metabolism and chemistry: Potential roles in lung development and structure
    • Rucker R B and Dubick M A 1984 Elastin metabolism and chemistry: potential roles in lung development and structure; Environ. Health Perspect. 55 179-191
    • (1984) Environ. Health Perspect. , vol.55 , pp. 179-191
    • Rucker, R.B.1    Dubick, M.A.2
  • 101
    • 0017185407 scopus 로고
    • Is there a recycling of hydroxyproline?
    • Ruiz-Torres A and Kürten I 1976 Is there a recycling of hydroxyproline?; Experientia 32 555-656
    • (1976) Experientia , vol.32 , pp. 555-656
    • Ruiz-Torres, A.1    Kürten, I.2
  • 103
    • 0025780051 scopus 로고
    • Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon
    • Shapiro S D, Endicott S K, Province M A, Pierce J A and Campbell E J 1991 Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon; J. Clin. Invest. 87 1828-1834
    • (1991) J. Clin. Invest. , vol.87 , pp. 1828-1834
    • Shapiro, S.D.1    Endicott, S.K.2    Province, M.A.3    Pierce, J.A.4    Campbell, E.J.5
  • 104
    • 0021306610 scopus 로고
    • Extensive degradation of recently synthesized collagen in gingiva of normal and streptozotocin-induced diabetic rats
    • Schneir M L, Ramamurthy N S and Golub L M 1984 Extensive degradation of recently synthesized collagen in gingiva of normal and streptozotocin-induced diabetic rats; J. Dent. Res. 63 23-27
    • (1984) J. Dent. Res. , vol.63 , pp. 23-27
    • Schneir, M.L.1    Ramamurthy, N.S.2    Golub, L.M.3
  • 106
    • 0015293064 scopus 로고
    • Is histidine an essential amino acid in man?
    • Stifel F B and Herman R H 1972 Is histidine an essential amino acid in man? Am. J. Clin. Nutr. 25 182-185
    • (1972) Am. J. Clin. Nutr. , vol.25 , pp. 182-185
    • Stifel, F.B.1    Herman, R.H.2
  • 107
    • 0019462140 scopus 로고
    • Alternative metabolic fates of thymine nucleotides in human cells
    • Taheri M R, Wickremasinghe R G and Hoffbrand A V 1981 Alternative metabolic fates of thymine nucleotides in human cells; Biochem. J. 194 451-461
    • (1981) Biochem. J. , vol.194 , pp. 451-461
    • Taheri, M.R.1    Wickremasinghe, R.G.2    Hoffbrand, A.V.3
  • 108
    • 33644875278 scopus 로고    scopus 로고
    • Biochemistry of human skin - Our brain on the outside
    • Tobin D J 2006 Biochemistry of human skin - our brain on the outside; Chem. Soc. Rev. 35 52-67
    • (2006) Chem. Soc. Rev. , vol.35 , pp. 52-67
    • Tobin, D.J.1
  • 110
    • 0036471216 scopus 로고    scopus 로고
    • Carnitine biosynthesis in mammals
    • Vaz F M and Wanders R J 2002 Carnitine biosynthesis in mammals; Biochem. J. 361 417-429
    • (2002) Biochem. J. , vol.361 , pp. 417-429
    • Vaz, F.M.1    Wanders, R.J.2
  • 111
    • 0021252966 scopus 로고
    • Protein turnover with special reference to man
    • Waterlow J C 1984 Protein turnover with special reference to man; Q. J. Exp. Physiol. 69 409-438
    • (1984) Q. J. Exp. Physiol. , vol.69 , pp. 409-438
    • Waterlow, J.C.1
  • 112
    • 84890207812 scopus 로고    scopus 로고
    • (Wallingford, UK: CABI Publishing)
    • Waterlow J C 2006 Protein turnover (Wallingford, UK: CABI Publishing) pp 270-274
    • (2006) Protein Turnover , pp. 270-274
    • Waterlow, J.C.1
  • 114
    • 9844232492 scopus 로고
    • Rates of reactions involved in phosphatide synthesis in liver and small intestine of intact rats
    • Wise E M Jr and Elwyn D 1965 Rates of reactions involved in phosphatide synthesis in liver and small intestine of intact rats; J. Biol. Chem. 240 1537-1548
    • (1965) J. Biol. Chem. , vol.240 , pp. 1537-1548
    • Wise Jr., E.M.1    Elwyn, D.2
  • 115
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodelling
    • Woessner J F Jr 1991 Matrix metalloproteinases and their inhibitors in connective tissue remodelling; FASEB J. 5 2145-2154
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner Jr., J.F.1
  • 116
    • 0002917420 scopus 로고
    • Formation and breakdown of collagen and elastin in the human uterus during pregnancy and post-partum involution
    • Woessner J F and Brewer T H 1963 Formation and breakdown of collagen and elastin in the human uterus during pregnancy and post-partum involution; Biochem. J. 89 75-82
    • (1963) Biochem. J. , vol.89 , pp. 75-82
    • Woessner, J.F.1    Brewer, T.H.2
  • 117
    • 0022537834 scopus 로고
    • L-threonine aldolase is not a genuine enzyme in rat liver
    • Yeung Y G 1986 L-Threonine aldolase is not a genuine enzyme in rat liver; Biochem. J. 237 187-190
    • (1986) Biochem. J. , vol.237 , pp. 187-190
    • Yeung, Y.G.1
  • 118
    • 0023182795 scopus 로고
    • Protein intake and requirements with reference to diet and health
    • Young V R and Pellett P L 1987 Protein intake and requirements with reference to diet and health; Am. J. Clin. Nutr. 45 1323-1343
    • (1987) Am. J. Clin. Nutr. , vol.45 , pp. 1323-1343
    • Young, V.R.1    Pellett, P.L.2


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