Hormonal Effects on Fascia in Women
David Lesondak, Angeli Maun Akey in Fascia, Function, and Medical Applications, 2020
Not only does estrogen stimulate type I collagen,5 it also slows down the breakdown of collagen and elastin. Elastin is a connective tissue molecule that gives the tissue its property of resilience, allowing it to extend/recoil with ease and form elastic fibers.5 Collagen and elastin breakdown is slowed by downregulating MMPs.5 These MMPs are zinc-dependent endopeptidases that have been shown to denature endopelvic connective tissue.5,10 Postmenopausal women have lower estrogen levels. As a result, they have relatively increased activity of these MMPs compared with their premenopausal states. Hence, diminished levels of collagen in postmenopausal women results in increased myofascial issues and rapid fascial sagging. Moreover, tissues derived from prolapsed organs show lower levels of elastin, stiffer extracellular matrices (ECMs), and decreased tissue strength.5
Natural Products and Stem Cells and Their Commercial Aspects in Cosmetics
Heather A.E. Benson, Michael S. Roberts, Vânia Rodrigues Leite-Silva, Kenneth A. Walters in Cosmetic Formulation, 2019
Proteins have been used for cosmetic purposes since ancient times. One such protein, collagen, is found in all multicellular organisms and is the main protein found in skin. Collagen is also present in connective tissues, tendons and bones. With skin aging, the molecular structure of collagen is modified and causes skin to look wrinkled and dry and have reduced elasticity. Several types of collagen are marketed that are extracted from animal waste produced after preparing animals for dietary consumption. Soluble collagen, also known as native collagen, is generally the type used in skin and hair care products. This collagen can be hydrolyzed with free amino acids, resulting in no residue on skin and hair. Collagen is known for its moisturizing properties and can be used in creams to increase the skin penetration of formulation ingredients. However, there is some controversy over the effectiveness of collagen for use in hair products. Collagen can also be hydrolyzed and denatured to obtain gelatin. Elastin is a protein that is often found in the body together with collagen and, as the name implies, elastin contributes to the skin’s elasticity. This protein is used in creams, lotions, shampoos and conditioners, face masks, and other cosmetic formulations. Non-animal–derived options are available for collagen and elastin, including plant and synthetic sources (Corbeil et al., 2000).
Exploring the Plant Kingdom for Sources of Skincare Cosmeceuticals
Mahendra Rai, Shandesh Bhattarai, Chistiane M. Feitosa in Wild Plants, 2020
Eighty percent of the dry weight of skin is considered to be collagen and is responsible for the tensile strength of the skin. Collagenases are a type of metalloproteinase that can cleave molecules in the extracellular matrix. Elastase is a proteolytic enzyme involved in the degradation of the extracellular matrix that contains elastin. Elastin provides much of the elastic recoil properties of skin, arteries, lungs, and ligaments. Loss of elastin is a major part of what causes visible signs of aging in the skin. Hyaluronic acid has a role in retaining the moisture, structure, and elasticity of the skin while facilitating rapid tissue proliferation, regeneration, and repair. The levels of collagen, elastin, and hyaluronic acid would decrease with aging, and this could lead to a loss of strength and flexibility in the skin, causing the emergence of wrinkles (Ndlovu et al. 2013). Moreover, the high levels of ROS induce the action of collagenase, elastase, and hyaluronidase, which can further contribute to skin aging (Labat-Robert et al. 2000, Ndlovu et al. 2013). However, natural materials with anti-collagenase, anti-elastase, and anti-hyaluronidase properties can help to prevent the undesirable age-associated destruction of collagen, elastin, and hyaluronic acid (Thring et al. 2009, Ndlovu et al. 2013).
Bilaminar Mechanics of the Human Optic Nerve Sheath
Published in Current Eye Research, 2020
Andrew Shin, Joseph Park, Alan Le, Vadims Poukens, Joseph L. Demer
Examination of mechanical and anatomical characteristics in two of the same specimens suggests that the IL might be stiffer, at least in part, because it has denser elastin. Elastin is a protein with reversible extensibility preventing dynamic tissue creep and permitting tissues to resume their shapes after loading.32 Elastin is abundant in artery, lung, elastic ligament, cartilage, and skin,33,34 as well as in the lamina cribrosa,35-37 the peripapillary scleral ring,36 and the connective pulley tissue system of the orbit at sites of concentrated mechanical stress.38 Elastin resists tissue deformation and has a memory permitting it to return to its undeformed shape after low stress loading.32,39 Elastin and collagen fibers comprise parallel mechanical elements when tissue undergoes strain: at low strain, collagen fibers extend easily with most of the load borne by elastic fibers, but at high strain, collagen fibers become limiting.40 For example, in rat aorta, collagen digestion has little effect on stress levels at up to about 30% strain, implicating a major role for elastin in this loading regime41 that is most relevant to the strains used in the current paper. We describe in detail elsewhere the laminar differences in elastin abundance and fiber orientation in the human ON sheath.24 Cross linking and absence of elastin turnover with age leads to tissue stiffening.40 The higher elastin density in the ON sheath IL is consistent with its stiffer mechanical properties than the OL.
The role of kallikreins in inflammatory skin disorders and their potential as therapeutic targets
Published in Critical Reviews in Clinical Laboratory Sciences, 2021
Caitlin T. Di Paolo, Eleftherios P. Diamandis, Ioannis Prassas
The dermis is comprised of a dense thick layer of connective tissue and contains sensory cells, sweat glands, and blood vessels. Via its vascular structures, the dermis provides the avascular epidermis with the nutrients required for the development of a functional barrier. These blood vessels are also involved in the thermoregulation of the body by constricting or dilating to conserve or release heat. Fibroblasts secrete collagen, which is the main structural component of the dermis and gives the skin flexibility and strength through its mesh-like framework. Elastin is also abundant, resulting in the skin’s elastic nature following stretching. Within the dermis there are glycosaminoglycans, such as hyaluronic acid, which provide hydration and moisture to the epidermis. Mast cells located in the dermis are involved in the immune function of the skin, as they can trigger an inflammatory response to microorganisms, allergens, and physical injury.
Current advances in cell therapeutics: a biomacromolecules application perspective
Published in Expert Opinion on Drug Delivery, 2022
Samson A. Adeyemi, Yahya E. Choonara
Elastin is a bio-synthetic biomacromolecule synthesized from human elastin sequences as the backbone[105]. Elastin-Like Polypeptides (ELPs) are produced from a plasmid-borne gene in Escherichia coli [106] which are then extracted by purifying the cell lysates and characterized by large monomers with repeating units. Based on this bio-engineering technique Rodriguez-Cabello and co-workers [107] coined the term elastin-like ‘recombinamer’ (ELR). The VPGVG pentapeptide repeat is a widely investigated ELR family and represents the most ubiquitous sequence found in human elastin naturally. Several other ELRs have been manufactured from the VPGVG repeat by replacing the fourth amino acid with other naturally occurring amino acids, except proline. When heated, ELRs respond to heat and show a reversible sol-gel transition interphase. At transition temperature, they form a random-coil conformation and when heated, the chain folds hydrophobically to form a uniform b-spiral stabilized structure. The polymer molecular weight, its concentration in solution and composition of the amino acids control the transition temperature and can be monitored to stabilize between room and body temperature. In addition, it is possible to engineer this biomacromolecule to accommodate biodegradation sequences [108] or add specific cell adhesion motifs [109]. For instance, Costa and co-workers [110,111] added chitosan as a polycation to a negatively charged ELR having the RGD motifs to synthesize microcapsules using a layer-by-layer technique for application in the transport of bioactive agents and cells in tissue engineering.