Шаштың және тырнақтың кератин түрі

Type of keratin found in hair and nails

Hair keratin is a type of keratin found in hair and the nails.

Originating from the embryonic epidermis, the hair follicle evolves into one of the most complex structures in the human body, comprising 7–8 distinct tissue sections. The base of the hair follicle contains the bulb, housing dermal fibroblasts known as the dermal papilla, crucial for morphogenesis and the hair follicle's cyclic activity. Encircling these cells is the matrix cell region, the hair follicle's proliferative compartment, responsible for the formation of different follicle compartments (except the ORS) and the production of crucial structural elements of hair hair keratins and associated proteins known as KAPs. Keratins belong to two types acidic Type I and neutral basic Type II, further categorized into Type I a and b, and Type II a and b. The initial step in forming keratin is the alignment of type I and type II keratin polypeptides to create a heterodimer, which then aggregates into higher order structural units.

Due to their role as structural stabilizers in epithelial cells, keratin filaments have garnered significant interest across biology, embryology, pathology, and dermatology. This fundamental cytoskeletal function extends beyond individual cell levels. Typically, keratin filaments are integrated into desmosomes (see Fig. 1b, d) and hemidesmosomes, contributing not only to cell to cell stability but also to the attachment to the basement membrane and the connective tissue within a particular epithelium. In non stratified (simple) epithelia of internal organs experiencing minimal mechanical stress, only a few keratin types form sparsely distributed filaments within the cytoplasm. However, a more substantial number of keratin types participate in the intermediate filament cytoskeletal framework of squamous epithelia, which becomes more prominent in cornified stratified epithelia like the epidermis covering the body's outer surface. Here, keratins are abundant and densely packed, forming tonofilaments. It has been revealed that RKNPs significantly boosted cell proliferation and migration in laboratory settings. Moreover, when applied to dermal wounds in vivo, RKNPs facilitated improved wound healing, leading to enhanced epithelialization, vascularization, collagen deposition, and remodeling. Importantly, tests for in vivo biocompatibility showed no signs of systemic toxicity. RKNPs have potential as a promising approach for advancing wound healing and suggests new avenues for developing keratin based biomaterials. Furthermore, in the femoral artery injury model, the recombinant keratin proteins significantly reduced bleeding time compared to the control group (approximately 50 s vs. 270 s). Notably, K37 and K81 exhibited stronger haemostatic effects than extracted keratins (approximately 80 s) in treating rat liver injury. Additionally, the recombinant keratin proteins demonstrated a robust capacity to promote the formation of a fibrin clot at the injury site, effectively stopping the bleeding. Consequently, recombinant human hair keratins offer potential for developing novel haemostatic products based on keratin biomaterials. Hair keratins form intermediate filaments (KIFs) within trichocytes, specialized cells that contribute to hair formation. As these cells move upward in the cortex, KIFs aggregate, surrounded by a space called the matrix. KRTAPs, also known as KAPs, are a significant part of this matrix between KIFs. It's suggested that KRTAPs play a role in establishing a cross linked network with KIFs, contributing to the creation of the rigid hair shaft. However, this intricate process can be simplified into a few highly preserved gene families. In cortical keratinocytes, distinct patterns of keratin gene expression are evident, indicating the presence of different hierarchical transcription processes among various cell types. Examination of keratin gene promoter regions reveals conserved sequence motifs that might govern these cell specific traits. The intermediate filament network is formed by the necessary pairing of equal amounts of type I and type II keratins. While hair keratins, such as KRT81, are typical in hard keratinized structures like hair and nails, they are thought to serve as structural proteins specific to these organs without expression elsewhere, such as the mammary gland. KRT81, a type II hair keratin, is a major hair protein expressed in the hair cortex. Interestingly, despite being typically associated with hair structures, KRT81 expression has been observed in the SKBR3 human breast cancer cell line and metastatic lymph nodes of breast carcinomas, but not in normal breast epithelial cells. Moreover, the expressed KRT81 was found to be a 5′ truncated isoform (ΔHb1), with the full length protein not being expressed. However, the exact function of this truncated form in breast cancer cells remains unclear. Western blot analysis detected the presence of the complete 55 kDa KRT81 in various human breast cancer cell lines (MCF7, SKBR3, MDA MB 231), normal human mammary epithelial cells (HMEC), and non neoplastic cells (MCF10A). Reverse transcription polymerase chain reaction confirmed the expression of the full length KRT81, encompassing its 5' region, in breast cells. Immunohistochemical and immunofluorescence examinations located KRT81 within the cytoplasm. Additionally, in KRT81 knockdown MDA MB231 cells, zymography illustrated decreased MMP9 activity, while scratch and invasion assays demonstrated diminished cell migration and invasion capabilities. This presents the first evidence of complete KRT81 expression in both normal breast epithelial cells and breast cancer cells. Furthermore, the findings suggest that KRT81 plays a role in the migration and invasion of breast cancer cells.