Protein-glutamine gamma-glutamyltransferase K is an enzyme that in humans is encoded by the TGM1 gene.
Keratinocyte transglutaminase is a transglutaminase enzyme.
Keratinocyte transglutaminase enzymes serve to specifically catalyze the development of the cornified cell envelope, a defining characteristic of epidermal keratinocytes that have undergone the termination of differentiation. [1] [2]The specific cross linkages formed by keratinocyte transglutaminase are between n^ε-(γ-glutamyl)lysine residues which develop into isopeptide protein-protein linkages that adds to the stabilization of the cornified cell envelope. [3] [4]In terminally differentiated stratified squamous epithelia, the cornified cell envelope protein linkages allow for a structurally fortified, yet flexible(15 nm thick) layer to the place of the cell membrane, acting as a highly insoluble barrier. [5] [2] The expression of the enzyme is most highly exhibited along the biological membrane of these fully formed epithelial cells, preventing the cell from undergoing chemical and or physical damages. [2] [6]A lesser amount of enzymatic activity, of the TGK genes (5-10%), lies within the cytoplasmic fraction of such cells, allowing for finalization of the cross-linkaging necessary for the full functionality of the cornified cell envelope. [7]
Pathology
A deficiency is associated with ichthyosis lamellaris. Epidermal transglutaminase is the autoantigen, in humans, of dermatitis herpetiformis.
A study on the mutation of Keratinocyte transglutaminase (TGK) came to conclude that those affected with ichthyosis lamellaris, present a substantial deficit in keratinocyte transglutaminase activity. [2]It was concluded that those afflicted, display a decrease in activity of the enzyme, as a result of a lessened amount of transcription of the human TGK gene. [2] This lack of protein stems from a common mutation of the TGK gene, which exists in two possible variants, found at the TGM1 locus on the 14q11 chromosome, as exhibited amongst all the subjects of the study. [2] Such mutations were of the compound heterozygous or homozygous variety, which leads to the expression of lamellar ichthyosis as a result of abnormal cross-linkaging of the cornified cell envelope. [2]
- ^ Eckert, Richard L.; Sturniolo, Michael T.; Broome, Ann-Marie; Ruse, Monica; Rorke, Ellen A. (March 2005). "Transglutaminase function in epidermis". The Journal of Investigative Dermatology. 124 (3): 481–492. doi: 10.1111/j.0022-202X.2005.23627.x. ISSN 0022-202X. PMID 15737187.
- ^ a b c d e f g Huber, M.; Rettler, I.; Bernasconi, K.; Frenk, E.; Lavrijsen, S.; Ponec, M.; Bon, A.; Lautenschlager, S.; Schorderet, D.; Hohl, D. (1995-01-27). "Mutations of keratinocyte transglutaminase in lamellar ichthyosis". Science. 267 (5197): 525–528. doi: 10.1126/science.7824952. ISSN 0036-8075.
- ^ "Protein Glutamine Gamma Glutamyltransferase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2020-04-29.
- ^ "Protein Glutamine Gamma Glutamyltransferase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2020-04-29.
- ^ Kim, Soo Youl; Jeitner, Thomas M.; Steinert, Peter M. (January 2002). "Transglutaminases in disease". Neurochemistry International. 40 (1): 85–103. doi: 10.1016/s0197-0186(01)00064-x. ISSN 0197-0186. PMID 11738475.
- ^ "Protein Glutamine Gamma Glutamyltransferase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2020-04-29.
-
^
{{ cite web}}: Empty citation ( help)
Protein-glutamine gamma-glutamyltransferase K is an enzyme that in humans is encoded by the TGM1 gene.
Keratinocyte transglutaminase is a transglutaminase enzyme.
Keratinocyte transglutaminase enzymes serve to specifically catalyze the development of the cornified cell envelope, a defining characteristic of epidermal keratinocytes that have undergone the termination of differentiation. [1] [2]The specific cross linkages formed by keratinocyte transglutaminase are between n^ε-(γ-glutamyl)lysine residues which develop into isopeptide protein-protein linkages that adds to the stabilization of the cornified cell envelope. [3] [4]In terminally differentiated stratified squamous epithelia, the cornified cell envelope protein linkages allow for a structurally fortified, yet flexible(15 nm thick) layer to the place of the cell membrane, acting as a highly insoluble barrier. [5] [2] The expression of the enzyme is most highly exhibited along the biological membrane of these fully formed epithelial cells, preventing the cell from undergoing chemical and or physical damages. [2] [6]A lesser amount of enzymatic activity, of the TGK genes (5-10%), lies within the cytoplasmic fraction of such cells, allowing for finalization of the cross-linkaging necessary for the full functionality of the cornified cell envelope. [7]
Pathology
A deficiency is associated with ichthyosis lamellaris. Epidermal transglutaminase is the autoantigen, in humans, of dermatitis herpetiformis.
A study on the mutation of Keratinocyte transglutaminase (TGK) came to conclude that those affected with ichthyosis lamellaris, present a substantial deficit in keratinocyte transglutaminase activity. [2]It was concluded that those afflicted, display a decrease in activity of the enzyme, as a result of a lessened amount of transcription of the human TGK gene. [2] This lack of protein stems from a common mutation of the TGK gene, which exists in two possible variants, found at the TGM1 locus on the 14q11 chromosome, as exhibited amongst all the subjects of the study. [2] Such mutations were of the compound heterozygous or homozygous variety, which leads to the expression of lamellar ichthyosis as a result of abnormal cross-linkaging of the cornified cell envelope. [2]
- ^ Eckert, Richard L.; Sturniolo, Michael T.; Broome, Ann-Marie; Ruse, Monica; Rorke, Ellen A. (March 2005). "Transglutaminase function in epidermis". The Journal of Investigative Dermatology. 124 (3): 481–492. doi: 10.1111/j.0022-202X.2005.23627.x. ISSN 0022-202X. PMID 15737187.
- ^ a b c d e f g Huber, M.; Rettler, I.; Bernasconi, K.; Frenk, E.; Lavrijsen, S.; Ponec, M.; Bon, A.; Lautenschlager, S.; Schorderet, D.; Hohl, D. (1995-01-27). "Mutations of keratinocyte transglutaminase in lamellar ichthyosis". Science. 267 (5197): 525–528. doi: 10.1126/science.7824952. ISSN 0036-8075.
- ^ "Protein Glutamine Gamma Glutamyltransferase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2020-04-29.
- ^ "Protein Glutamine Gamma Glutamyltransferase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2020-04-29.
- ^ Kim, Soo Youl; Jeitner, Thomas M.; Steinert, Peter M. (January 2002). "Transglutaminases in disease". Neurochemistry International. 40 (1): 85–103. doi: 10.1016/s0197-0186(01)00064-x. ISSN 0197-0186. PMID 11738475.
- ^ "Protein Glutamine Gamma Glutamyltransferase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2020-04-29.
-
^
{{ cite web}}: Empty citation ( help)