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Collagen and elastin are the fundamental structural proteins of the extracellular matrix (ECM), providing the essential framework for connective tissues throughout the body [1]. Collagen, the most abundant protein in mammals, exists in multiple types (primarily Type I, II, and III) and provides tensile strength and structural integrity to skin, bones, tendons, and ligaments [3]. Elastin is a highly resilient protein that allows tissues such as the lungs, large arteries, and skin to recoil after stretching, maintaining physiological elasticity [2]. Pathological alterations in these proteins, such as excessive collagen deposition or elastin degradation, are central to diseases like systemic fibrosis, emphysema, and cardiovascular stiffening [4]. Therapeutic interventions include the use of collagenase enzymes to break down pathological collagen in conditions like Dupuytren's contracture, and retinoids to stimulate new protein synthesis in aging skin [5]. Additionally, inhibitors of elastase are explored to prevent tissue destruction in inflammatory lung diseases. Because these proteins are distinct in structure, genetic origin, and function, they are typically addressed as separate therapeutic targets in clinical practice.
Enzymatic degradation of collagen fibers; Stimulation of fibroblast-mediated protein synthesis; Inhibition of proteolytic degradation by elastases.
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