The reduced glutathione to oxidized glutathione levels appear to influence G6PDH and maybe vice versa.But this shows indirectly(I believe) that glutathione levels ARE lower in mpb scalp.There is another study which says alopecic scalp is lower in glutathione also but doesnt state if they meant mpb specifically.
The second abstract suggests glutathione is an important part of androgen signaling.Maybe we become more androgen sensitive because of lower glutathione levels? But just blocking the androgen receptor may not be enough because perhaps it doesnt reverse the redox status? Sometimes when pathways are shut down too long merely reversing the original offender doesnt restore them to back to baseline levels as a new homeostatic setpoint was determined.
We can increase glutathione levels and G6PDH(an energy enzyme) by l-carnitine and alpha lipoic acid and NAC and aged garlic(because of s-allyl cysteine).
If you think about what the cell is attempting to do,it makes sense.If a cell has a poor antioxidant defense system it better shut down energy pathways like G6PDH or it could lead to cancer.
Biosci Biotechnol Biochem 1999 Dec;63(12):2219-21 Related Articles, Books
Activity of glucose-6-phosphate 1-dehydrogenase in hair follicles with male-pattern alopecia.
Adachi K, Watanabe Y, Inouye K
Research and Development Headquarters, Lion Corporation, Kanagawa, Japan.
[Medline record in process]
Activity of glucose-6-phosphate 1-dehydrogenase (G6PDH) in human hair follicles was measured. A good relationship has been demonstrated between the activity and the ratio of the number of the anagen hairs to that of all the plucked hairs in the frontal-parietal region of the scalp with male-pattern alopecia. As the ratio becomes lower so that the advancing degree of alopecia is higher, the G6PDH activity becomes lower.
PMID: 10664855, UI: 20128240
Purification of androgen receptors in human sebocytes and hair. Sawaya ME.
University of Miami School of Medicine, Department of Dermatology and Cutaneous Surgery, FL 33101.
Human sebaceous glands (SG) and hair follicles (HF) are target structures in the skin for androgen action. They contain steroid enzymes, capable of transforming weak androgens into the target-tissue-active androgens testosterone (T) and dihydrotestosterone (DHT), which bind to the androgen receptor (AR) to regulate cellular transcription. The AR from HF and SG from human scalp tissue has been purified greater than 86,000 times by phenyl-sepharose, DEAE-sephacel, gel filtration chromatography, and ultrafiltration. Sucrose density gradient analysis and non-denaturing gradient polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate (SDS)-PAGE revealed two molecular species of AR, an active form called monomer, capable of binding DHT with great specificity (4S, m = 62,000 Da, Kd = 0.6 nM, Bmax 8260 fmol/micrograms protein), and the other, an inactive form of the monomer called tetramer (10.8S, m = 252,000 Da, Kd = 2.9 nM). The two species are interconvertible, and after purification each appeared as a single band on SDS-PAGE. The conversion of the monomer to the tetramer AR form is influenced by reduced and oxidized glutathione, and possibly by an endogenous disulfide converting factor (DCF). Furthermore, biochemical events in the androgenic signal transduction sequence were shown to be stimulated by androgens via the AR. These include the total nuclear AR content, chromatin binding of AR complexes, and stimulation of RNA polymerase II, thus influencing gene expression, which is important in understanding regulation of HF growth and SG proliferation.
L-carnitine and DL-alpha-lipoic acid reverse the age-related deficit in glutathione redox state in skeletal muscle and heart tissues. Kumaran S, Savitha S, Anusuya Devi M, Panneerselvam C.
Department of Medical Biochemistry, Dr. AL Mudaliar Post Graduate Institute of Basic Medical Sciences, Uni