コラーゲン分解性の、膠原溶解性の

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English Journal

Regeneration of human dermis by a multi-headed Peptide.

Attia-Vigneau J1, Terryn C2, Lorimier S3, Sandre J4, Antonicelli F3, Hornebeck W3.Author information 1Regentis-International, University of Reims-Champagne Ardenne (URCA), Faculty of Medicine, SFR CAP Santé, Reims, France.2Faculty of Medicine, Tissular and Cellular Imaging Center (URCA), Reims, France.3University of Reims-Champagne Ardenne (URCA)-FRE 3481 CNRS, MEdyc, SFR CAP Santé, Reims, France.4Plastic Surgery Department, Courlancy Clinic, Reims, France.AbstractSkin aging is characterized by deterioration of the dermal collagen fiber network due to both decreased collagen expression and increased collagenolytic activity. We designed and evaluated in vitro and ex vivo the efficacy of a trifunctional peptide (TFP) to restore collagen and elastin fibers. TFP was constituted of an elastokine motif (VGVAPG)3, able to increase matrix constituent expression through the stimulation of the elastin-binding protein receptor, a GIL tripeptide occupying matrix metalloproteinase-1 subsites, and a RVRL linker domain acting as a competitive substrate for urokinase. The effects of TFP on type I, type III collagens, and elastin expression in dermal fibroblasts were determined by quantitative real-time reverse-transcriptase-PCR and western blotting. TFP's inhibitory capacity against MMP-1, plasmin, and urokinase was assessed using synthetic substrates, immunohistochemistry, and skin tissue sections as natural substrates. A skin explant model was used to recapitulate aging-induced dermal changes along culture extent. Collagen and elastin fiber structure was analyzed by two-photon fluorescence, second harmonic generation, and confocal microscopies. Compared with the different sections constituting the full peptide, we found that TFP activated the production of matrix constituents while inhibiting MMP-1 in vitro and ex vivo. It also induced a proper fiber network organization, reflecting the potency of TFP in skin remodeling and regeneration.
The Journal of investigative dermatology.J Invest Dermatol.2014 Jan;134(1):58-67. doi: 10.1038/jid.2013.290. Epub 2013 Jun 28.
Skin aging is characterized by deterioration of the dermal collagen fiber network due to both decreased collagen expression and increased collagenolytic activity. We designed and evaluated in vitro and ex vivo the efficacy of a trifunctional peptide (TFP) to restore collagen and elastin fibers. TFP
PMID 23812301

Carbodiimide Inactivation of MMPs and Effect on Dentin Bonding.

Mazzoni A, Apolonio FM, Saboia VP, Santi S, Angeloni V, Checchi V, Curci R, Di Lenarda R, Tay FR, Pashley DH, Breschi L.Author information Department of Biomedicine, Unit of Dental Sciences and Biomaterials, University of Trieste, Trieste, Italy.AbstractThe use of protein cross-linking agents during bonding procedures has been recently proposed to improve bond durability. This study aimed to use zymography and in situ zymography techniques to evaluate the ability of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) cross-linker to inhibit matrix metalloproteinase (MMP) activity. The hypotheses tested were that: (1) bonding procedures increase dentin gelatinolytic activity and (2) EDC pre-treatment prevents this enzymatic activity. The zymographic assay was performed on protein extracts obtained from dentin powder treated with Optibond FL or Scotchbond 1XT with or without 0.3M EDC pre-treatment. For in situ zymography, adhesive/dentin interfaces were created with the same adhesives applied to acid-etched dentin slabs pre-treated or not with EDC conditioner. Zymograms revealed increased expression of dentin endogenous MMP-2 and -9 after adhesive application, while the use of EDC as a primer inactivated dentin gelatinases. Results of in situ zymograpy showed that hybrid layers of tested adhesives exhibited intense collagenolytic activity, while almost no fluorescence signal was detected when specimens were pre-treated with EDC. The correlative analysis used in this study demonstrated that EDC could contribute to inactivate endogenous dentin MMPs within the hybrid layer created by etch-and-rinse adhesives.
Journal of dental research.J Dent Res.2013 Dec 11. [Epub ahead of print]
The use of protein cross-linking agents during bonding procedures has been recently proposed to improve bond durability. This study aimed to use zymography and in situ zymography techniques to evaluate the ability of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) cross-linker to inhibit matrix
PMID 24334409

Dermal Damage Promoted by Repeated Low-Level UV-A1 Exposure Despite Tanning Response in Human Skin.

Wang F, Smith NR, Tran BA, Kang S, Voorhees JJ, Fisher GJ.Author information Department of Dermatology, University of Michigan Medical School, Ann Arbor.AbstractIMPORTANCE Solar UV irradiation causes photoaging, characterized by fragmentation and reduced production of type I collagen fibrils that provide strength to skin. Exposure to UV-B irradiation (280-320 nm) causes these changes by inducing matrix metalloproteinase 1 and suppressing type I collagen synthesis. The role of UV-A irradiation (320-400 nm) in promoting similar molecular alterations is less clear yet important to consider because it is 10 to 100 times more abundant in natural sunlight than UV-B irradiation and penetrates deeper into the dermis than UV-B irradiation. Most (approximately 75%) of solar UV-A irradiation is composed of UV-A1 irradiation (340-400 nm), which is also the primary component of tanning beds. OBJECTIVE To evaluate the effects of low levels of UV-A1 irradiation, as might be encountered in daily life, on expression of matrix metalloproteinase 1 and type I procollagen (the precursor of type I collagen). DESIGN, SETTING, AND PARTICIPANTS In vivo biochemical analyses were conducted after UV-A1 irradiation of normal human skin at an academic referral center. Participants included 22 healthy individuals without skin disease. MAIN OUTCOMES AND MEASURES Skin pigmentation was measured by a color meter (chromometer) under the L* variable (luminescence), which ranges from 0 (black) to 100 (white). Gene expression in skin samples was assessed by real-time polymerase chain reaction. RESULTS Lightly pigmented human skin (L* >65) was exposed up to 4 times (1 exposure/d) to UV-A1 irradiation at a low dose (20 J/cm2), mimicking UV-A levels from strong sun exposure lasting approximately 2 hours. A single exposure to low-dose UV-A1 irradiation darkened skin slightly and did not alter matrix metalloproteinase 1 or type I procollagen gene expression. With repeated low-dose UV-A1 irradiation, skin darkened incrementally with each exposure. Despite this darkening, 2 or more exposures to low-dose UV-A1 irradiation significantly induced matrix metalloproteinase 1 gene expression, which increased progressively with successive exposures. Repeated UV-A1 exposures did not suppress type I procollagen expression. CONCLUSIONS AND RELEVANCE A limited number of low-dose UV-A1 exposures, as commonly experienced in daily life, potentially promotes photoaging by affecting breakdown, rather than synthesis, of collagen. Progressive skin darkening in response to repeated low-dose UV-A1 exposures in lightly pigmented individuals does not prevent UV-A1-induced collagenolytic changes. Therefore, for optimal protection against skin damage, sunscreen formulations should filter all UV wavelengths, including UV-A1 irradiation.
JAMA dermatology (Chicago, Ill.).JAMA Dermatol.2013 Dec 4. doi: 10.1001/jamadermatol.2013.8417. [Epub ahead of print]
IMPORTANCE Solar UV irradiation causes photoaging, characterized by fragmentation and reduced production of type I collagen fibrils that provide strength to skin. Exposure to UV-B irradiation (280-320 nm) causes these changes by inducing matrix metalloproteinase 1 and suppressing type I collagen syn
PMID 24305962

Japanese Journal

Cathepsin K-upregulation in fibroblasts promotes matrigel invasive ability of squamous cell carcinoma cells via tumor-derived IL-1α

Xie Lining,Moroi Yoichi,Hayashida Sayaka,Tsuji Gaku,Takeuchi Satoshi,Shan Baoen,Nakahara Takeshi,Uchi Hiroshi,Takahara Masakazu,Furue Masutaka,師井洋一
Journal of dermatological science 61(1), 45-50, 2011-01-01
… Background: Cathepsin K (CTSK), a cysteine protease with strong collagenolytic properties, is involved in extracellular matrix turnover. …
NAID 10030889729

Autoactivation of Proteolytic Activity in Human Whole Saliva

MIYOSHI Yoshitada,WATANABE Makoto,TAKAHASHI Nobuhiro
Journal of oral biosciences 52(4), 402-408, 2010-11-20
NAID 10027626176

Inhibition of Collagenolytic Cathepsins by β-Lactoglobulin in Milk and Its Suppressive Effect on Bone Resorption

Ogawa Naoko,Takahashi Masae,Ishidoh Kazumi [他],KATUNUMA Nobuhiko
Journal of nutritional science and vitaminology 55(3), 264-270, 2009-06-01
… It is well known that the collagenolytic cathepsins play an important role in the degradation of bone matrix. … Furthermore, we demonstrated that β-lactoglobulin B inhibited degradation of type I-collagen by collagenolytic cathepsins. … Therefore, peroral intake of β-lactoglobulin in milk and its digested peptides are expected to help protect osteoclastic bone resorption via inhibition of collagenolytic cathepsins K and L. …
NAID 10025971416

「膠原溶解性」

　　[★]

英: collagenolytic
関: コラーゲン分解性

「コラーゲン分解性」

　　[★]

英: collagenolytic
関: 膠原溶解性

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collagenolytic

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「膠原溶解性」

「コラーゲン分解性」