Bm Regenerate Anti-Ageing Serum

Bm Regenerate Anti-Ageing Serum

Bm Regenerate Anti-Ageing Serum is a single plant ingredient serum setting new standards in anti-ageing skincare. Australian grown Mountain Pepper Berry enhances collagen production, repairs barrier function and increases hydration to gently defy visible signs of ageing.

Recent research has demonstrated the importance of the dermal-epidermal junction (DEJ) in skin aging. Since the BM proteins laminins and nidogen are expressed in epidermal keratinocytes, modulation of their expression seems an attractive approach for anti-aging ingredients.

Anti-wrinkle activity

Skin wrinkling is a result of a substantial deterioration of extracellular matrix molecules. This includes a reduced number of collagen fibers and disorganized collagen and laminin matrix proteins. MB has been shown to promote the proliferation of dermal fibroblasts and inhibit their enzymatic degradation of these proteins. Therefore, the use of BM can prevent ageing and reduce wrinkles.

BM is also known to have a mitochondrial-protective effect, which may contribute to the energy supply in cell proliferation and maintenance of the dermis. This was also confirmed aesthetic skin care in this study where MB increased the expression of several ECM proteins, including collagen XVII, laminin and nidogen. A mixture of peptide derivatives with stimulating activities on BM proteins was used as an anti-aging ingredient and showed an anti-wrinkle activity in ex vivo human skin and clinical studies.

The safety of MB was also evaluated using an in vitro skin irritation test and a long term cell viability assay on a 3D reconstructed human skin model. Both tests showed that MB does not cause irritation at any concentration tested and is safe for long-term topical application. This is particularly important as this ingredient is very soluble in water and can easily penetrate the epidermis and reach the underlying dermal tissues. This is in contrast to some popular cosmeceuticals that are irritating even at low concentrations.

Collagen XVII expression

The COL17A1 gene encodes collagen XVII, a multifunctional protein that is part of the hemidesmosomal structure in basal keratinocytes. Hemidesmosomes connect the epidermis to the dermis and anchor it to underlying tissues. The protein also binds with other components of the skin, such as plectin, laminin 332, and type VII collagen. Loss-of-function mutations in this gene result in a subtype of junctional epidermolysis bullosa (JEB) that shows more severe blistering and a milder overall phenotype than the other types of JEB.

COL17A1 is involved in the formation of hemidesmosomes and regulates a number of other cell functions, including cell migration, proliferation, and differentiation. It is also required for the proper cellular attachment of the epidermis to the dermis. In addition, hemidesmosomes form the primary site of the interaction between skin and bacterial pathogens.

In cancer biology, the differential expression of hemidesmosomal versus non-hemidesmosomal COL17 affects various characteristics of cell migration. Hemidesmosomal COL17 is located in the cell body and around the nucleus, whereas non-hemidesmosomal COL17 is localized to growing epithelial tongues.

We have shown that the expression of hemidesmosomal COL17 is correlated with the survival of lung cancer patients. In a cohort of 79 patients who underwent surgical resection, those with tumors that expressed hemidesmosomal COL17, Oct4, and HK2 had a better prognosis than those who did not express these markers.

Laminin expression

The laminin family of proteins are a major component of basement membranes (BM) and form heterotrimers consisting of three distinct subunits (a, b, and g). Laminins self-assemble into a cross-shaped matrix that interacts with cell-surface receptors and other ECM molecules. They are thought to be a crucial factor in the control of cell polarity and cell-matrix interactions during development, wound healing, and disease.

In mouse embryos (E15.5 and neonatal), the BM of the ureteric bud contains laminins a1 and a5. The first-formed BL of the nephron, that of the vesicle, also contained a5 and a1. Laminin a5 transcripts were also detectable in liver and meninges. Laminin a2 expression was confined to mesodermally derived tissues such as skeletal muscle and heart, whereas a3 expression was restricted to epithelial tissues including skin, lung, and olfactory epithelium.

Antibodies to the a5 and a2 chains of laminin reacted with sections from both tissues in qualitatively similar patterns. However, neither anti-a5 nor anti-a2 reacted with the 400 kD a1 chain of laminin-1. This result suggests that the antibodies used in these experiments reacted with a different form of laminin than the immunologically defined molecule. This may be due to a cross-reaction with other, unidentified binders or fragments of laminin. The reactivity of the a1 chain is further supported by a recent study in which apical-basal polarity of mammalian cells was disrupted by silencing a gene encoding for the a5 chain of laminin.

Nidogen expression

The Nidogen-perlecan interaction is essential for BM assembly and epithelial morphogenesis. Recombinant Nidogen promotes aesthetic skin care shop the formation of ternary complexes with laminins and perlecans, and blocking this interaction by antibodies results in defects in BM structure and epithelial morphogenesis. However, in vivo experiments suggest that the requirement for this interaction is tissue-specific. For example, loss of a nidogen gene in Caenorhabditis elegans leads to aberrant axonal migration but no obvious phenotype affecting BM assembly. This demonstrates that conclusions drawn from cell culture and in vitro experiments must be interpreted cautiously.

The G2 domain of nidogen-1 has been shown to form high-affinity binding sites for both collagen IV and perlecan. These interactions have been shown to be important for BM assembly and branching epithelial morphogenesis (Fox et al., 1991). Moreover, mutations in the G2 domain cause abnormal accumulation of Col IV and perlecan in the basement membrane of mouse tissues.

A crystal structure has been solved of the nidogen-1 G2 domain in complex with the IG3 domain of perlecan (Fig. 2). The structure shows that the perlecan binding site is located on a relatively flat region of the nidogen-1 b-barrel and forms an extensive interface. The main contact is centered on the side chain of Tyr1801 (perlecan) and involves two hydrogen bonds and the guanidinium group of Arg620 (nidogen). The interface is packed with water molecules, forming a hydrophobic pocket.