Serpins in the Human Hair Follicle
| Autor: | Tien Yang, Tung-Tien Sun, Barbara Risse, Mark S. Baker, Da Wen Yu, Pamela J. Jensen, Robert M. Lavker |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Cellular differentiation
Population Apoptosis Receptors Cell Surface In situ hybridization Dermatology Biology Outer root sheath Biochemistry Amyloid beta-Protein Precursor Follicular phase Serpin E2 medicine Plasminogen Activator Inhibitor 2 Humans RNA Messenger education programmed cell death Molecular Biology In Situ Hybridization Serpins education.field_of_study integumentary system Cell Biology Hair follicle Molecular biology Immunohistochemistry Protease Nexins plasminogen activator inhibitor type 2 follicular papilla medicine.anatomical_structure protease nexin-1 Plasminogen activator inhibitor-2 follicular epithelial differentiation Carrier Proteins Plasminogen activator Hair Follicle |
| Zdroj: | Journal of Investigative Dermatology. 114(5):917-922 |
| ISSN: | 0022-202X |
| DOI: | 10.1046/j.1523-1747.2000.00945.x |
| Popis: | Proteinases and their inhibitors are very likely to function as mediators or regulators of the hair growth cycle. Very little information is currently available, however, regarding the specific inhibitors present in human hair follicles at defined stages of their growth cycle. In this study we have analyzed two proteinase inhibitors, plasminogen activator inhibitor type 2 and protease nexin 1, in human hair follicles using in situ hybridization and/or immunohistochemistry. Protease nexin 1 mRNA was found only in the mesenchymal population of the hair follicle, i.e., the follicular papilla cells, during the anagen but not the catagen phase. In contrast, plasminogen activator inhibitor type 2 was localized to several epithelial populations in the follicle: the more differentiated cells of the infundibulum; the companion layer in anagen follicles; and the single layer of outer root sheath cells directly abutting the club hair in telogen follicles. At least some of the plasminogen activator inhibitor type 2 in human follicles appears to be in the relaxed form, as evidenced by strong staining with an antibody that is specific for this form of the inhibitor. This suggests that plasminogen activator inhibitor type 2 interacts with and is cleaved by an endogenous follicular proteinase and supports a constitutive role for this inhibitor in human follicular epithelia. |
| Databáze: | OpenAIRE |
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