鮭皮コラーゲンペプチドの牛蹄冠部周囲真皮への影響と効果
牛に飼料とともに鮭皮由来コラーゲンペプチド（MCP）を8週間摂取させ，前肢蹄冠の背側，外側，指間の真皮を解析した． MCP群の背側と外側の蹄冠皮膚は真皮の厚さ，線維芽細胞数，コラーゲン細線維の直径が増加，上昇した． MCP群の指間真皮の線維芽細胞数は増加したが，厚さは低下し，コラーゲン細線維直径は減少した． 線維径を調整するデルマタン硫酸とⅤ型コラーゲンはMCP群のすべての部位で増加し，特に指間での増加が顕著であった． 結合組織の強さの指数MADは背側と外側で増加したが指間では減少した． MCP投与による指間真皮のユニークな応答は細いコラーゲン細線維を集めて柔軟な結合組織を形成し，着地時の衝撃...
Saved in:
| Published in | Nippon Juishikai zasshi Vol. 63; no. 1; pp. 38 - 43 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | Japanese |
| Published |
公益社団法人 日本獣医師会
01.01.2010
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 0446-6454 2186-0211 |
| DOI | 10.12935/jvma.63.38 |
Cover
| Abstract | 牛に飼料とともに鮭皮由来コラーゲンペプチド（MCP）を8週間摂取させ，前肢蹄冠の背側，外側，指間の真皮を解析した． MCP群の背側と外側の蹄冠皮膚は真皮の厚さ，線維芽細胞数，コラーゲン細線維の直径が増加，上昇した． MCP群の指間真皮の線維芽細胞数は増加したが，厚さは低下し，コラーゲン細線維直径は減少した． 線維径を調整するデルマタン硫酸とⅤ型コラーゲンはMCP群のすべての部位で増加し，特に指間での増加が顕著であった． 結合組織の強さの指数MADは背側と外側で増加したが指間では減少した． MCP投与による指間真皮のユニークな応答は細いコラーゲン細線維を集めて柔軟な結合組織を形成し，着地時の衝撃を緩衝するためと考察した． MCPは線維芽細胞に作用し蹄冠の各部位に即した太さのコラーゲン細線維を産生させ，真皮構造を強化する効果があると考えられた． |
|---|---|
| AbstractList | 牛に飼料とともに鮭皮由来コラーゲンペプチド（MCP）を8週間摂取させ，前肢蹄冠の背側，外側，指間の真皮を解析した． MCP群の背側と外側の蹄冠皮膚は真皮の厚さ，線維芽細胞数，コラーゲン細線維の直径が増加，上昇した． MCP群の指間真皮の線維芽細胞数は増加したが，厚さは低下し，コラーゲン細線維直径は減少した． 線維径を調整するデルマタン硫酸とⅤ型コラーゲンはMCP群のすべての部位で増加し，特に指間での増加が顕著であった． 結合組織の強さの指数MADは背側と外側で増加したが指間では減少した． MCP投与による指間真皮のユニークな応答は細いコラーゲン細線維を集めて柔軟な結合組織を形成し，着地時の衝撃を緩衝するためと考察した． MCPは線維芽細胞に作用し蹄冠の各部位に即した太さのコラーゲン細線維を産生させ，真皮構造を強化する効果があると考えられた． 牛に飼料とともに鮭皮由来コラーゲンペプチド（MCP）を8週間摂取させ、前肢蹄冠の背側、外側、指間の真皮を解析した。MCP群の背側と外側の蹄冠皮膚は真皮の厚さ、線維芽細胞数、コラーゲン細線維の直径が増加、上昇した。MCP群の指間真皮の線維芽細胞数は増加したが、厚さは低下し、コラーゲン細線維直径は減少した。線維径を調整するデルマタン硫酸とV型コラーゲンはMCP群のすべての部位で増加し、特に指間での増加が顕著であった。結合組織の強さの指数MADは背側と外側で増加したが指間では減少した。MCP投与による指間真皮のユニークな応答は細いコラーゲン細線維を集めて柔軟な結合組織を形成し、着地時の衝撃を緩衝するためと考察した。MCPは線維芽細胞に作用し蹄冠の各部位に即した太さのコラーゲン細線維を産生させ、真皮構造を強化する効果があると考えられた。 |
| Author | 保坂, 善真 阿部, 敬 竹花, 一成 永易, 彩 植田, 弘美 後藤, 千尋 |
| Author_xml | – sequence: 1 fullname: 植田, 弘美 organization: 酪農学園大学獣医学部 – sequence: 1 fullname: 竹花, 一成 organization: 酪農学園大学獣医学部 – sequence: 1 fullname: 後藤, 千尋 organization: 酪農学園大学獣医学部 – sequence: 1 fullname: 阿部, 敬 organization: 酪農学園大学獣医学部 – sequence: 1 fullname: 永易, 彩 organization: 酪農学園大学獣医学部 – sequence: 1 fullname: 保坂, 善真 organization: 鳥取大学農学部 |
| BackLink | https://agriknowledge.affrc.go.jp/RN/2010791084$$DView record in AgriKnowledge |
| BookMark | eNo9kE1Lw0AQhhdRsH6c_B2pu9mPZA8epPgFBRG8L5NkUxNrU9KieGwjQr15EmxRj_VgQb0oKP6YJdb-C1MqXmaGeed5X5glNN9IGhqhNYLLxJaUr8enJ1AWtEzdOVSyiSssbBMyj0qYMWEJxtkiWm21Ig9jx3W4dNwSOpiMnsa3I9N9NdmjyT5M98VkxXxrshuTdUzWM53RuNf_eb_ILx8m2TC_Hub9l_Hgfkp13go1_3ye3H-ZzjC_ev--G6yghRDqLb3615fR4fbWYWXXqu7v7FU2qxbYRbbFHUE5k4Eb-hhz7dk49ABCaUsumU-AYB6C1h6lQkoNEnMWuBx7AWcgGKPLyJnZQhimUVtBLY2OG8lZXQc1rRKI1FTwVS1RcVNhoooUISmTBbkxI-NWG4rbZhqdQHquIG1Hfl2r6RuVoIpMC3X_9_4RpCoG-gsuNowX |
| ContentType | Journal Article |
| Copyright | 2010 公益社団法人 日本獣医師会 |
| Copyright_xml | – notice: 2010 公益社団法人 日本獣医師会 |
| DBID | N5S |
| DOI | 10.12935/jvma.63.38 |
| DatabaseName | AgriKnowledge（アグリナレッジ）AGROLib |
| DatabaseTitleList | |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Veterinary Medicine |
| EISSN | 2186-0211 |
| EndPage | 43 |
| ExternalDocumentID | oai_affrc_go_jp_01_00569349 article_jvma_63_1_63_38_article_char_ja |
| GroupedDBID | 5GY ALMA_UNASSIGNED_HOLDINGS JSF KQ8 RJT N5S |
| ID | FETCH-LOGICAL-a2759-5763549d8fc005eb20fbaaf929594c1a105faeeb33699ea9054d850bd54a6443 |
| ISSN | 0446-6454 |
| IngestDate | Fri Sep 19 12:27:56 EDT 2025 Wed Sep 03 06:03:12 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | false |
| IsScholarly | true |
| Issue | 1 |
| Language | Japanese |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-a2759-5763549d8fc005eb20fbaaf929594c1a105faeeb33699ea9054d850bd54a6443 |
| Notes | ZZ00014801 791084 |
| OpenAccessLink | https://agriknowledge.affrc.go.jp/RN/2010791084 |
| PageCount | 6 |
| ParticipantIDs | affrit_agriknowledge_oai_affrc_go_jp_01_00569349 jstage_primary_article_jvma_63_1_63_38_article_char_ja |
| PublicationCentury | 2000 |
| PublicationDate | 20100100 |
| PublicationDateYYYYMMDD | 2010-01-01 |
| PublicationDate_xml | – month: 01 year: 2010 text: 20100100 |
| PublicationDecade | 2010 |
| PublicationTitle | Nippon Juishikai zasshi |
| PublicationTitleAlternate | 日獣会誌 |
| PublicationYear | 2010 |
| Publisher | 公益社団法人 日本獣医師会 |
| Publisher_xml | – name: 公益社団法人 日本獣医師会 |
| References | [19] Hardingham TE, Fosang AJ : Proteoglycans : many forms and many functions, FASEB J, 6, 861-870 (1992) [14] Sykes B, Francis MJ, Smith R : Altered relation of two collagen types in osteogenesis imperfecta, N Engl J Med, 296, 1200-1203 (1977) [16] Zhang G, Ezura Y, Chervoneva I, Robinson PS, Beason DP, Carine ET, Soslowsky LJ, Iozzo RV, Birk DE :Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development, J Cell Biochem, 98, 1436-1449 (2006) [8] Yang CM, Russell BJ : Resistance of proline-containing peptides to ruminal degradation in vitro, Appl Environ Microbiol, 58, 3954-3958 (1992) [20] Watanabe T, Imamura Y, Hosaka Y, Ueda H, Takehana K : Graded arrangement of collagen fibrils in the equine superficial digital flexor tendon, Connect Tissue Res, 48, 332-337 (2007) [1] Matsuda N, Koyama Y, Hosaka Y, Ueda H, Watanabe T, Araya T, Irie S, Takehana K : Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis, J Nutr Sci Vitaminol (Tokyo), 52, 211-215 (2006) [13] Flint MH, Craig AS, Reilly HC, Gillard GC, Parry DA : Collagen fibril diameters and glycosaminoglycan content of skins-indices of tissue maturity and function, Connect Tissue Res, 13, 69-81 (1984) [7] Shigemura Y, Iwai K, Morimatsu F, Iwamoto T, Mori T, Oda C, Taira T, Park EY, Nakamura Y, Sato K :Effect of Prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin, J Agric Food Chem,57, 444-449 (2009) [18] Birk DE, Nurminskaya MV, Zycband EI : Collagen fibrillogenesis in situ : fibril segments undergo postdepositional modifications resulting in linear and lateral growth during matrix development, Dev Dyn, 202, 229-243 (1995) [4] Lischer ChJ, Ossent P, Raber M, Geyer H : Suspensory structures and supporting tissues of the third phalanx of cows and their relevance to the development of typical sole ulcers (Rusterholz ulcers), Vet Rec, 151, 694-698 (2002) [2] Minaguchi J, Koyama Y, Meguri N, Hosaka Y, Ueda H, Kusubata M, Hirota A, Irie S, Mafune N, Takehana K : Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in Achilles tendon, J Nutr Sci Vitaminol (Tokyo), 51, 169-174 (2005) [9] Erasmus LJ, Botha PM, Cruywagen CW, Meissner HH : Amino acid profile and intestinal digestibility in dairy cows of rumen-undegradable protein from various feedstuffs, J Dairy Sci, 77, 541-551 (1994) [5] Koyama Y, Hirota A, Mori H, Takahara H, Kuwaba K, Kusubata M, Matsubara Y, Kasugai S, Itoh M, Irie S : Ingestion of gelatin has differential effect on bone mineral density and body weight in protein undernutrition, J Nutr Sci Vitaminol (Tokyo), 47, 84-86 (2001) [11] Iwai K, Hasegawa T, Taguchi Y, Morimatsu F, Sato K, Nakamura Y, Higashi A, Kido Y, Nakabo Y, Ohtsuki K : Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates, J Agric Food Chem, 53, 6531-6536 (2005) [3] Yunoki S, Nagai N, Suzuki T, Munekata M : Novel biomaterial from reinforced salmon collagen gel prepared by fibril formation and cross-linking, J Biosci Bioeng, 98, 40-47 (2004) [6] Moskowitz RW : Role of collagen hydrolysate in bone and joint disease, Semin Arthritis Rheum, 30, 87-99 (2000) [17] Robinson PS, Huang TF, Kazam E, Iozzo RV, Birk DE, Soslowsky LJ : Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice, J Biomech Eng, 127, 181-185 (2005) [10] O'Mara FP, Murphy JJ, Rath M : The amino acid composition of protein feedstuffs before and after ruminal incubation and after subsequent passage through the intestines of dairy cows, J Anim Sci, 75, 1941-1949 (1997) [12] Martens H, Kudritzki J, Wolf K, Schweigel M : No evidence for active peptide transport in forestomach epithelia of sheep, Anim Physiol Anim Nutr (Berl),85, 314-324 (2001) [15] Chen H, Wong EA, Webb KE Jr : Tissue distribution of a peptide transporter mRNA in sheep, dairy cows,pigs, and chickens, J Anim Sci, 77, 1277-1283 (1999) |
| References_xml | – reference: [8] Yang CM, Russell BJ : Resistance of proline-containing peptides to ruminal degradation in vitro, Appl Environ Microbiol, 58, 3954-3958 (1992) – reference: [11] Iwai K, Hasegawa T, Taguchi Y, Morimatsu F, Sato K, Nakamura Y, Higashi A, Kido Y, Nakabo Y, Ohtsuki K : Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates, J Agric Food Chem, 53, 6531-6536 (2005) – reference: [5] Koyama Y, Hirota A, Mori H, Takahara H, Kuwaba K, Kusubata M, Matsubara Y, Kasugai S, Itoh M, Irie S : Ingestion of gelatin has differential effect on bone mineral density and body weight in protein undernutrition, J Nutr Sci Vitaminol (Tokyo), 47, 84-86 (2001) – reference: [1] Matsuda N, Koyama Y, Hosaka Y, Ueda H, Watanabe T, Araya T, Irie S, Takehana K : Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis, J Nutr Sci Vitaminol (Tokyo), 52, 211-215 (2006) – reference: [12] Martens H, Kudritzki J, Wolf K, Schweigel M : No evidence for active peptide transport in forestomach epithelia of sheep, Anim Physiol Anim Nutr (Berl),85, 314-324 (2001) – reference: [6] Moskowitz RW : Role of collagen hydrolysate in bone and joint disease, Semin Arthritis Rheum, 30, 87-99 (2000) – reference: [10] O'Mara FP, Murphy JJ, Rath M : The amino acid composition of protein feedstuffs before and after ruminal incubation and after subsequent passage through the intestines of dairy cows, J Anim Sci, 75, 1941-1949 (1997) – reference: [13] Flint MH, Craig AS, Reilly HC, Gillard GC, Parry DA : Collagen fibril diameters and glycosaminoglycan content of skins-indices of tissue maturity and function, Connect Tissue Res, 13, 69-81 (1984) – reference: [16] Zhang G, Ezura Y, Chervoneva I, Robinson PS, Beason DP, Carine ET, Soslowsky LJ, Iozzo RV, Birk DE :Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development, J Cell Biochem, 98, 1436-1449 (2006) – reference: [20] Watanabe T, Imamura Y, Hosaka Y, Ueda H, Takehana K : Graded arrangement of collagen fibrils in the equine superficial digital flexor tendon, Connect Tissue Res, 48, 332-337 (2007) – reference: [2] Minaguchi J, Koyama Y, Meguri N, Hosaka Y, Ueda H, Kusubata M, Hirota A, Irie S, Mafune N, Takehana K : Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in Achilles tendon, J Nutr Sci Vitaminol (Tokyo), 51, 169-174 (2005) – reference: [18] Birk DE, Nurminskaya MV, Zycband EI : Collagen fibrillogenesis in situ : fibril segments undergo postdepositional modifications resulting in linear and lateral growth during matrix development, Dev Dyn, 202, 229-243 (1995) – reference: [3] Yunoki S, Nagai N, Suzuki T, Munekata M : Novel biomaterial from reinforced salmon collagen gel prepared by fibril formation and cross-linking, J Biosci Bioeng, 98, 40-47 (2004) – reference: [7] Shigemura Y, Iwai K, Morimatsu F, Iwamoto T, Mori T, Oda C, Taira T, Park EY, Nakamura Y, Sato K :Effect of Prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin, J Agric Food Chem,57, 444-449 (2009) – reference: [14] Sykes B, Francis MJ, Smith R : Altered relation of two collagen types in osteogenesis imperfecta, N Engl J Med, 296, 1200-1203 (1977) – reference: [9] Erasmus LJ, Botha PM, Cruywagen CW, Meissner HH : Amino acid profile and intestinal digestibility in dairy cows of rumen-undegradable protein from various feedstuffs, J Dairy Sci, 77, 541-551 (1994) – reference: [19] Hardingham TE, Fosang AJ : Proteoglycans : many forms and many functions, FASEB J, 6, 861-870 (1992) – reference: [17] Robinson PS, Huang TF, Kazam E, Iozzo RV, Birk DE, Soslowsky LJ : Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice, J Biomech Eng, 127, 181-185 (2005) – reference: [4] Lischer ChJ, Ossent P, Raber M, Geyer H : Suspensory structures and supporting tissues of the third phalanx of cows and their relevance to the development of typical sole ulcers (Rusterholz ulcers), Vet Rec, 151, 694-698 (2002) – reference: [15] Chen H, Wong EA, Webb KE Jr : Tissue distribution of a peptide transporter mRNA in sheep, dairy cows,pigs, and chickens, J Anim Sci, 77, 1277-1283 (1999) |
| SSID | ssib007875978 ssib016509427 ssib015835736 ssib002221907 ssib002483650 ssj0000615234 ssib029852152 |
| Score | 1.8142189 |
| Snippet | 牛に飼料とともに鮭皮由来コラーゲンペプチド（MCP）を8週間摂取させ，前肢蹄冠の背側，外側，指間の真皮を解析した． MCP群の背側と外側の蹄冠皮膚は真皮の厚さ，線維芽... 牛に飼料とともに鮭皮由来コラーゲンペプチド（MCP）を8週間摂取させ、前肢蹄冠の背側、外側、指間の真皮を解析した。MCP群の背側と外側の蹄冠皮膚は真皮の厚さ、線維芽細胞... |
| SourceID | affrit jstage |
| SourceType | Open Access Repository Publisher |
| StartPage | 38 |
| SubjectTerms | コラーゲン 牛 真皮 蹄冠 鮭皮由来コラーゲンペプチド |
| Title | 鮭皮コラーゲンペプチドの牛蹄冠部周囲真皮への影響と効果 |
| URI | https://www.jstage.jst.go.jp/article/jvma/63/1/63_38/_article/-char/ja https://agriknowledge.affrc.go.jp/RN/2010791084 |
| Volume | 63 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| ispartofPNX | 日本獣医師会雑誌, 2010/01/20, Vol.63(1), pp.38-43 |
| journalDatabaseRights | – providerCode: PRVAFT databaseName: Open Access Digital Library customDbUrl: eissn: 2186-0211 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0000615234 issn: 0446-6454 databaseCode: KQ8 dateStart: 19510101 isFulltext: true titleUrlDefault: http://grweb.coalliance.org/oadl/oadl.html providerName: Colorado Alliance of Research Libraries |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnR1NT9RAdAJ48WIUNeJXODgnU-zHdHbm2O6WEAwkJGi4NdPdFneJsCHggdtSY4I3TyZAxCMeJBEvkmj8Mc2K_Avfm7a7NRgjXprXmTdv3nsznXlvOvOGkAdcsUiwpm0owbkB87FjCCVdo2WDedFkKrIknh2em-czT9jskrs0MupXT5dsRFPNrT-eK_mfVoU0aFc8JXuBlh0QhQSAoX3hCS0Mz39qYxpI6gXUa9CgRqWHcOBQYVPf0QD-Ay8Av15m2WVKiQMFC6BWAMIqgby4pSnX8FX6NBDUl1QwGrhUcOqZyAbWJTBFWiXg67qAsTqV079zaFFfVCi71G9Q30I6gOlPl1majvCwuoBTGQCpqjE93-52ofPObuI62opqP9wCT-BZu-xDNGBISzY0Nw0UHvqTfuGa_YK1IT7wEVBRRwlBFx4r8UUD5cNskwp_iA_sCs1uKb_GB05dOgxpiQlQDgXmiI9xtXKyILQnq8suevdeueySj87gRxsYDq06lRRjdfWTyeeFPIJNYWHkcanOzV1geGGcj86L52qKO1NlkfPBwJNkvRkur4WdbmhaIQZzlQ6To-SSXeMcb_F4vFBxIW2Yk6ouPhMOr_zJhgEbfMoBvuWCSV5zBiaqpSMs2oPythQuXoU8WMdEk9jWmzcGGimOwaI8j4bSgImHnLfRgeuA51PumtSG3OJVcqXwwCa9_HO6RkY6apyMP8VtYfps-uRcsd3kOlk4O_p4unuUbX_O0g9Z-jXbPs5SgHez9G2W9rJ0J-sdne7s_Tx52X_1_iw97L857O8dn-4fYKneF8jtf_t0dvA96x32X5_8eLd_gyxOB4v1GaO4g8RQNijGcDFgI5MtkTRB0XFkm0mkVAJOhStZ01LgniQqjiPH4VLGSoIH1BKuGbVcpsDVcG6SsdW11fgWmeRmLCOucAcFWPGJkIwxGQvJuUyclm1OEDPXT6iW14cr6uFfmnyC8FyTYTcPTRMWQ1GIag-5E1r4cMQgHY9yhh11--J13SGXh5_BXTK2sb4Z3wN7fCO6rzvcLxLIwQk |
| linkProvider | Colorado Alliance of Research Libraries |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=%E9%AE%AD%E7%9A%AE%E3%82%B3%E3%83%A9%E3%83%BC%E3%82%B2%E3%83%B3%E3%83%9A%E3%83%97%E3%83%81%E3%83%89%E3%81%AE%E7%89%9B%E8%B9%84%E5%86%A0%E9%83%A8%E5%91%A8%E5%9B%B2%E7%9C%9F%E7%9A%AE%E3%81%B8%E3%81%AE%E5%BD%B1%E9%9F%BF%E3%81%A8%E5%8A%B9%E6%9E%9C&rft.jtitle=Nippon+Juishikai+zasshi&rft.au=%E4%BF%9D%E5%9D%82%2C+%E5%96%84%E7%9C%9F&rft.au=%E5%BE%8C%E8%97%A4%2C+%E5%8D%83%E5%B0%8B&rft.au=%E9%98%BF%E9%83%A8%2C+%E6%95%AC&rft.au=%E6%B0%B8%E6%98%93%2C+%E5%BD%A9&rft.date=2010-01-01&rft.issn=0446-6454&rft.volume=63&rft.issue=1&rft.spage=38&rft.epage=43&rft_id=info:doi/10.12935%2Fjvma.63.38&rft.externalDocID=oai_affrc_go_jp_01_00569349 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0446-6454&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0446-6454&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0446-6454&client=summon |