Post by skyship on Feb 5, 2016 17:56:59 GMT -5
2. Hair follicle
Recent advances in molecular genetics have led to the identification of numerous genes that are expressed in the HF. Furthermore, mutations in some of these genes have been shown to underlie hereditary hair diseases in humans [2]. Causative genes for the diseases encode various proteins with different functions, such as structural proteins, transcription factors, and signaling molecules. This chapter aims to update recent findings regarding the molecular basis of genetic hair diseases.
Wymore is not looking at keratin and its signalling properties........ this was the way in. whether outside CTs or inside GMOs or breathing in the protofilaments.
3. Keratin disorders
Keratins are one of the major structural components of the HF, and are largely divided into type I (acidic) and type II (neutral to basic) keratins. The type I and type II keratins undergo heterodimerization, which leads to form keratin intermediate filaments (KIFs) in the cytoplasm [5]. Based on the amino acid composition, keratins are further classified into two groups: epithelial (soft) keratins and hair (hard) keratins. As compared to the epithelial keratins, the hair keratins show higher sulfur content in their N- and C-terminus, which plays an important role in interacting with hair keratin-associated proteins via disulfide bindings [6, 7]. All the keratin proteins are composed of an N-terminal rod domain, a central rod domain, and a C-terminal tail domain. Importantly, the N-terminal and the C-terminal regions of the rod domain are highly conserved in amino acid sequences, which are called helix initiation motif (HIM) and helix termination motif (HTM), respectively (Figure 4). It is believed that the HIM and the HTM play essential roles in heterodimerization between the keratins. In humans, gene clusters for the type I and type II keratin genes are mapped on chromosomes 17q21 [8] and 12q13 [9], respectively. To date, a total of 54 functional keratin genes (28 type I and 26 type II) have been identified and characterized in humans. It has been shown that during differentiation of the HF, various keratin genes are abundantly and differentially expressed, and contribute to HF keratinization, leading to the formation of a rigid structure [10]. In general, epithelial keratins are mainly expressed in the ORS, the companion layer, the IRS, while hair keratins are predominantly expressed in the hair shaft. In addition, it has recently been reported that some epithelial keratins are expressed in the hair shaft medulla as well [11]. It is noteworthy that mutations in several keratin genes have been reported to underlie hereditary hair disorders in humans (Table 1).
www.intechopen.com/books/current-genetics-in-dermatology/current-genetics-in-hair-diseases
......best way to post things.....sorry Facebook does not do it! Too many EGOS in the way!
Recent advances in molecular genetics have led to the identification of numerous genes that are expressed in the HF. Furthermore, mutations in some of these genes have been shown to underlie hereditary hair diseases in humans [2]. Causative genes for the diseases encode various proteins with different functions, such as structural proteins, transcription factors, and signaling molecules. This chapter aims to update recent findings regarding the molecular basis of genetic hair diseases.
Wymore is not looking at keratin and its signalling properties........ this was the way in. whether outside CTs or inside GMOs or breathing in the protofilaments.
3. Keratin disorders
Keratins are one of the major structural components of the HF, and are largely divided into type I (acidic) and type II (neutral to basic) keratins. The type I and type II keratins undergo heterodimerization, which leads to form keratin intermediate filaments (KIFs) in the cytoplasm [5]. Based on the amino acid composition, keratins are further classified into two groups: epithelial (soft) keratins and hair (hard) keratins. As compared to the epithelial keratins, the hair keratins show higher sulfur content in their N- and C-terminus, which plays an important role in interacting with hair keratin-associated proteins via disulfide bindings [6, 7]. All the keratin proteins are composed of an N-terminal rod domain, a central rod domain, and a C-terminal tail domain. Importantly, the N-terminal and the C-terminal regions of the rod domain are highly conserved in amino acid sequences, which are called helix initiation motif (HIM) and helix termination motif (HTM), respectively (Figure 4). It is believed that the HIM and the HTM play essential roles in heterodimerization between the keratins. In humans, gene clusters for the type I and type II keratin genes are mapped on chromosomes 17q21 [8] and 12q13 [9], respectively. To date, a total of 54 functional keratin genes (28 type I and 26 type II) have been identified and characterized in humans. It has been shown that during differentiation of the HF, various keratin genes are abundantly and differentially expressed, and contribute to HF keratinization, leading to the formation of a rigid structure [10]. In general, epithelial keratins are mainly expressed in the ORS, the companion layer, the IRS, while hair keratins are predominantly expressed in the hair shaft. In addition, it has recently been reported that some epithelial keratins are expressed in the hair shaft medulla as well [11]. It is noteworthy that mutations in several keratin genes have been reported to underlie hereditary hair disorders in humans (Table 1).
www.intechopen.com/books/current-genetics-in-dermatology/current-genetics-in-hair-diseases
......best way to post things.....sorry Facebook does not do it! Too many EGOS in the way!