The Interaction(s) between Calf-Skin Hyaluronic Acid (Hyaluronan) and Dermal Type I Calf-Skin Collagen under 254 nm UV Radiation: Ability of Hyaluronan to Alter Qualitative and Quantitative Dimerization of Collagen Tyrosine Residues

• 作者: Julian M. Menter La Toya Freeman Ortega Edukye
• 来源期刊: 物理化学期刊(英文)
• 学科: 医学
• 关键词: Extracellular Matrix (ECM) PROTEOGLYCAN Type I COLLAGEN Tyrosine DITYROSINE Fluorescence UV Radiation Rate of DITYROSINE Formation PHOTODIMERIZATION
• 年，卷（期）: 2019,（2）
• 页码范围: 51-59
• 页数: 9页
• 分类号: R73

摘要

The extracellular matrix (ECM) is the non-cellular component present within all tissues and organs, providing not only essential physical scaffolding for the cellular constituents and initiating crucial biochemical and biomechanical cues, required for tissue morphogenesis, differentiation and homeostasis. Roughly divided into two groups, these are 1) the main fibrous ECM proteins: collagens, elastins, fibronectins and laminins. 2) Classification of proteoglycans (PGs) is based on their location and binding. Although many different molecular interactions are possible, they depend on the cells’ condition (i.e. “Normal”, Aged, Wounded/Fibrotic, and cancerous). There is little or no data that addresses the influence of the surrounding ECM on dityrosine formation. As a simpler model, we have replaced total PG with hyaluronan (HA) and have used purified calf-skin collagen tyrosine, which forms dityrosine (A2) under 254 nm UV in buffered solution and (near) physiological temperatures. Our results reveal a complicated temperature dependence involving factors relating to collagen HA structure, and collagen’s photochemical activation parameters.