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The Journal of Clinical Endocrinology & Metabolism Vol. 83, No. 5 1776-1782
Copyright © 1998 by The Endocrine Society

Original Studies

Luteinizing Hormone and Human Chorionic Gonadotropin Decrease Type 2 5{alpha}-Reductase and Androgen Receptor Protein Levels in Women’s Skin

J. Bird1, X. Li, Z. M. Lei, J. Sanfilippo2, M. A. Yussman and Ch. V. Rao

Laboratory of Molecular Reproductive Biology and Medicine, Department of Obstetrics and Gynecology, University of Louisville Health Sciences Center, Louisville, Kentucky 40292

Address all correspondence and requests for reprints to: Dr. Ch. V. Rao, Department of Obstetrics and Gynecology, 438 MDR Building, University of Louisville Health Sciences Center, Louisville, Kentucky 40292. E-mail: cvrao001{at}ulkyvm.louisville.edu


   Abstract
Top
 Abstract
Introduction
 Materials and Methods
 Results
 Discussion
 References
 
The present study tested the hypothesis that LH/hCG may regulate the type 2 5{alpha}-reductase and androgen receptor protein levels in skin. The skin samples obtained from women undergoing abdominal laparotomy or abdominoplasty were incubated in the presence or absence of hCG. Western blotting was then performed to determine the response of type 2 5{alpha}-reductase and androgen receptors. The results demonstrated that treatment with hCG resulted in a significant time- and dose-dependent, although modest, decrease in 5{alpha}-reductase and androgen receptor levels compared to the controls. These effects were mimicked by LH, but not by other hormones in the glycoprotein hormone family, including {alpha}- and ß-subunits of hCG. Although the biological and clinical importance of this regulation remains to be determined, these findings reaffirm that human skin is among the nongonadal tissues that respond to LH and hCG treatment.


   Introduction
Top
 Abstract
 Introduction
Materials and Methods
 Results
 Discussion
 References
 
LH FROM anterior pituitary and hCG from human placenta are structural and functional homologs that bind to the same receptors (1, 2). The receptors are transmembrane glycoproteins that belong to the family of G protein-coupled receptors (2). It was assumed for a long time that LH and hCG regulated only gonadal tissues because it was thought that only these tissues contained the LH/hCG receptors. Contrary to this assumption, recent studies from several laboratories have demonstrated that LH/hCG receptors are also present in many nongonadal tissues and that exogenous LH and hCG can regulate their functions (reviewed in Ref.3). Human skin is among this group of nongonadal tissues. It contains LH/hCG receptor messenger ribonucleic acid (mRNA) transcripts and receptor protein that can bind [125I]hCG (4). Human skin also contains 5{alpha}-reductase, which catalyzes the conversion of testosterone into hormonally more active dihydrotestosterone (DHT). In addition, human skin contains androgen receptors that mediate the actions of locally formed DHT (4, 5, 6, 7, 8, 9). The local formation and action of androgens play important roles in the growth and differentiation of skin appendages and their secretions, and these contribute to skin changes seen in patients with polycystic ovarian disease and other forms of hirsutism (10, 11, 12, 13, 14, 15, 16, 17). The coincidental distribution of LH/hCG receptors with androgen receptors and 5{alpha}-reductase (Ref. 4 and the present study) suggests a hypothesis that LH and hCG might regulate these molecules. The present study tested this hypothesis in skin samples from premenopausal women.


   Materials and Methods
Top
 Abstract
 Introduction
 Materials and Methods
Results
 Discussion
 References
 
Materials

The following items were obtained from the National Hormone and Pituitary Program supported by the NIDDK, NICHHD, and USDA (Rockville, MD): hCG (CR-127; 14,900 IU/mg), human FSH (AFP-87929B; 1,683 IU/mg), human LH (AFP-0264B; 4,015 IU/mg), human TSH (AFP-4314C; 15 IU/mg), and the {alpha}-subunit (CR-125) and ß-subunit (CR-125; 29 IU/mg) of hCG. A polyclonal antibody raised against the synthetic amino acid sequence of 227–251 of the type 2 human 5{alpha}-reductase (B302) was obtained from Dr. David W. Russell at the University of Texas Southwestern Medical School (Dallas, TX) (5). It recognizes type 2 and weakly cross-reacts with type 1 isozyme. The affinity-purified polyclonal antibody raised against the synthetic peptide corresponding to the N-terminal 21 amino acids of rat and human androgen receptors (clone PG-21) was purchased from Affinity Bioreagents (Golden, CO). This antibody cross-reacts with androgen receptors from various species, but does not cross-react with other members of the steroid receptor superfamily.

Incubation of human skin tissues

Skin samples were obtained from 18 cycling women undergoing abdominal laparotomy or abdominoplasty for various indications. The use of these abdominal skin samples was approved by our university human studies committee. Immediately after collection, the samples were transported to the laboratory on ice and processed for immunocytochemistry or for incubations. For the latter studies, the skin was cut into 3-mm3 pieces and incubated for varying lengths of time at 37 C in the presence or absence of various hormones in Krebs-Ringer bicarbonate buffer under 5% CO2 and 95% O2. At the end of the incubation, the tissues were extensively washed and processed for Western blotting.

Immunocytochemistry

This procedure was performed by a previously described avidin-biotin immunoperoxidase method (18), using a 1:200 dilution of type 2 5{alpha}-reductase antibody or a 1:25 dilution of androgen receptor antibody. For the procedural controls, either the primary antibodies were omitted, or they were replaced with nonspecific IgG.

Western blotting

After the incubation, the tissues were homogenized at 4 C in 25 mmol/L HEPES buffer, pH 7.4, containing the protease inhibitors, leupeptin and aprotinin (10 µg/mL), and 4-(2-aminoethyl) benzene sulfonyl fluoride hydrochloride (50 µg/mL). The protein content in the homogenates was determined by the Bradford method using a commercial kit. Aliquots of 60 µg protein were separated on a discontinuous 10% SDS-PAGE under reducing conditions and electroblotted to Immobilon P membranes (Millipore Corp., Bedford, MA) (19). The type 2 5{alpha}-reductase and androgen receptors on the membranes were detected using a 1:800 dilution of 5{alpha}-reductase and a 1:100 dilution of androgen receptor antibodies and an enhanced chemiluminescence detection system. Nonspecific IgG was used for a control. The relative optical densities of protein bands on x-ray films were determined using a Z-Gel scanning system (ZAXIS, Hudson, OH).

Repetition of experiments and statistical analysis

Each experiment was performed in triplicate and repeated on skin samples from three to five women. The data were analyzed by one-way ANOVA and Duncan’s multiple range test using a SPSS statistical program (SPSS, Inc., Chicago, IL) (20).


   Results
Top
 Abstract
 Introduction
 Materials and Methods
 Results
Discussion
 References
 
Immunocytochemistry was used to determine the cellular distribution of type 2 5{alpha}-reductase and androgen receptors in skin samples from women. Figure 1Go shows that the immunostaining for type 2 5{alpha}-reductase is present in epidermis (A), sweat glands (B), sebaceous glands (C), and hair follicles (A). This staining was absent in the procedural control (D), suggesting that it was specific. Similarly, androgen receptor immunostaining was present in epidermis (E), hair follicles (F), sweat glands (G), and sebaceous glands (H) and was absent in the procedural controls (I). As expected, nuclei of the cells were immunostained for androgen receptors (E–H), and the perinuclear region was immunostained for type 2 5{alpha}-reductase (A–C). The cellular distribution of type 2 5{alpha}-reductase and androgen receptors is in general agreement with the findings of previous studies (4, 6, 8, 9). More importantly, these distributions are similar to that of LH/hCG receptors (Ref. 4 and the present study).



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  		Figure 1. Cellular distribution of type 2 5{alpha}-reductase (A–D) and androgen receptors (E–I) in human skin as determined by immunocytochemistry. Immunostaining for 5{alpha}-reductase and androgen receptors in epidermis (EP), sweat (SG) and sebaceous (seb) glands, and hair follicles (HF) is shown. D and I are nonspecific IgG immunostaining controls. Magnification, x300.

 
The size of type 2 5{alpha}-reductase protein in human skin, as determined by Western blotting, was 29 kDa. This size is in excellent agreement with previously reported values in other tissues (5). Incubation of skin samples with 10 ng/mL hCG resulted in a significant, although modest, decrease in type 2 5{alpha}-reductase protein levels at 4 h compared to its corresponding control value (Fig. 2Go). A shorter or longer duration of incubation with hCG had no effect.



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  		Figure 2. Time dependency of hCG effect on type 2 5{alpha}-reductase protein levels in human skin. In this and the following figures, the means and their SEs of densitometric values from all of the experiments are presented; the inset shows a representative Western blot. The asterisks indicate significant decreases (P < 0.05) compared to control values, which, in the case of time dependency experiments, were run at each time point.

 
Figure 3Go shows that incubation of skin samples for 4 h with increasing concentrations of hCG resulted in a significant, although modest, decrease in 5{alpha}-reductase protein levels at 0.1 ng/mL, which did not further change when the hCG concentrations were increased to 100 ng/mL. The decreasing hCG effect was hormone specific, because LH, but not the other hormones in the same glycoprotein hormone family, such as FSH and TSH, could mimic the hCG action on 5{alpha}-reductase protein levels (Fig. 4Go). The {alpha}- and ß-subunits of hCG had no effect, suggesting that the hCG action requires the conformation of native hormone (Fig. 4Go).



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  		Figure 3. Dose dependency of the effect of hCG on type 2 5-{alpha} reductase protein levels in human skin.

 


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  		Figure 4. Hormone specificity of the effect of hCG on type 2 5 {alpha}-reductase protein levels in human skin.

 
Human skin contains a 63-kDa androgen receptor protein. This size is smaller than those reported in most other androgen target tissues, except chicken oviduct and human foreskin fibroblasts (21, 22). The treatment of skin specimens with 10 ng/mL hCG also resulted in a significant, although modest, decrease in androgen receptor protein levels at 4 h compared to its corresponding control value (Fig. 5Go). A shorter or longer duration of incubation with hCG had no effect.



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  		Figure 5. Time dependency of the effect of hCG on androgen receptor protein levels in human skin.

 
Incubation of skin samples for 4 h with increasing hCG concentrations resulted in a significant, although modest decrease at 0.05 ng/mL hCG, with no further change when the concentrations were increased up to 100 ng/mL hCG (Fig. 6Go). The hCG effect was mimicked by LH, but not by other hormones in the glycoprotein hormone family or the {alpha}- and ß-subunits of hCG (Fig. 7Go).



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  		Figure 6. Dose dependency of the effect of hCG on androgen receptor protein levels in human skin.

 


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  		Figure 7. Hormone specificity of the effect of hCG on androgen receptor protein levels in human skin.

 

   Discussion
Top
 Abstract
 Introduction
 Materials and Methods
 Results
 Discussion
References
 
Besides human skin, LH/hCG receptors have been demonstrated in the skin of nontransgenic and transgenic mice heterozygous or homozygous for human immunodeficiency virus-1 provirus pNL 4–3 and in Kaposi sarcoma, a skin cancer commonly seen in human immunodeficiency virus-infected patients (Shapira A., S. Bao, Z. M. Lei, A. L. Notkins, S. K. De, Ch. V. Rao; unpublished data; Huang Z. H., Z. M. Lei, Ch. V. Rao; unpublished data). Treatment of homozygous transgenic mice with hCG, which protects them from the syndrome characterized by dry, scaly, and hyperkeratotic skin; failure to grow; and early death (23), increases skin LH/hCG receptors (Shapira A., S. Bao, Z. M. Lei, A. L. Notkins, S. K. De, Ch. V. Rao; unpublished data). Although it is controversial (24), hCG has been shown to induce the regression of Kaposi sarcomas by increasing apoptosis (25, 26). All of these findings suggest that LH/hCG receptors could be important in the regulation of skin functions by gonadotropins.

Skin has many functions. For example, it acts as a physical barrier, serves as an immunological organ, and has the potential to react to both external and internal stimuli (27, 28, 29, 30). Skin possibly is the largest androgen-dependent organ in the body. It has the enzymes required for the formation of DHT from pregnenolone, dehydroepiandrosterone, and testosterone (31, 32). 5{alpha}-Reductase is the enzyme that converts testosterone into DHT. The two isozymes, types 1 and 2, are encoded by different genes, possess 60% homology, and show different optimal pH and sensitivity to finasteride inhibition (33, 34, 35). Although type 1 isozyme has been reported to be predominant in skin (6), we found both isozymes to be present, as did Mestayer et al. (36). However, we could not determine the response of type 1 isozyme to hCG treatment.

Incubation of skin specimens showed that hCG could modestly inhibit both 5{alpha}-reductase and androgen receptor protein levels. The responses were time dependent, occurring at 4 h; dose dependent, occurring at 0.05–0.1 ng/mL hCG; and hormone specific, and require the conformation of native hormone. The decreases caused by low concentrations were not further inhibited by higher hCG concentrations.

Whether hCG can potentiate the inhibitory effects of others such as 13-cis-retinoic acid (37) and whether skin receptors depend on circulating and/or locally produced gonadotropins are not known. Skin producing LH and/or hCG or LH/hCG-like peptides is theoretically possible because it has the functional equivalent of a hypothalamo-pituitary axis and is capable of producing several neuroendocrine peptides (30, 32, 38, 39).

Our preliminary data showed that hCG treatment had no effect on steady state mRNA levels of type 2 5{alpha}-reductase or androgen receptors, indicating that the effects of hCG are specific to proteins of these molecules. Whether the effects of hCG are mediated by decreasing the translation efficiency of the corresponding mRNAs and/or increasing the degradation of proteins of these molecules is not known.

By decreasing androgen receptors, hCG acts as an antiandrogen in human skin, as it does in rat granulosa cells (40) and human prostate cancer LNCaP cells (41). However, from the known association between skin changes and elevated LH levels in chronic anovulatory or postmenopausal women, one may expect LH and hCG to increase, not decrease, 5{alpha}-reductase and androgen receptor levels. Thus, these unexpected responses indicate that we have yet to understand the biological and clinical significance of regulation of skin functions by gonadotropins. We would like to point out that abdominal skin was used in the present studies, and we do not know whether skin from other areas of the body responds similarly to hCG.

In summary, we demonstrate that women’s skin, which contains LH/hCG receptors, responds to these hormones by a modest decrease in type 2 5{alpha}-reductase and androgen receptor protein levels. The biological and clinical importance of this regulation remains to be determined.


   Footnotes
 
1 Current address: Center for Reproductive Medicine and Fertility, 1815 Gunbarrell Road, Chattanooga, Tennessee 37421. Back

2 Current address: Department of Obstetrics and Gynecology, Allegheny University of the Health Sciences, 320 East North Avenue, Pittsburgh, Pennsylvania 15212. Back

Received November 14, 1997.

Revised December 12, 1997.

Accepted January 15, 1998.


   References
Top
 Abstract
 Introduction
 Materials and Methods
 Results
 Discussion
 References
 

  1. Pierce JG, Parsons TF. 1981 Glycoprotein hormones: structure and function. Annu Rev Biochem. 50:466–495.
  2. Loosfelt H, Misrahi M, Atger M, et al. 1989 Cloning and sequencing of porcine LH/hCG receptor cDNA: variants lacking transmembrane domain. Science. 245:525–528.[Abstract/Free Full Text]
  3. Rao ChV. 1996 The beginning of a new era in reproductive biology and medicine: expression of low levels of functional luteinizing hormone/human chorionic gonadotropin receptors in nongonadal tissues. J Physiol Pharmacol. 47(Suppl 1):41–53.
  4. Pabon JE, Bird JS, Li X, et al. 1996 Human skin contains luteinizing hormone/chorionic gonadotropin receptors. J Clin Endocrinol Metab. 81:2738–2741.[Abstract]
  5. Thigpen AE, Silver RI, Guileyardo JM, Casey ML, McConnell JD, Russell DW. 1993 Tissue distribution and ontogeny of steroid 5{alpha}-reductase isozyme expression. J Clin Invest. 92:903–910.
  6. Luu-The V, Sugimoto Y, Puy L, et al. 1994 Characterization, expression, and immunohistochemical localization of 5{alpha}-reductase in human skin. J Invest Dermatol. 102:221–226.[CrossRef][Medline]
  7. Bläuer M, Vaalasti A, Pauli SL, Ylikomi T, Joensuu T, Tuohimaa P. 1991 Location of androgen receptor in human skin. J Invest Dermatol. 97:264–268.[CrossRef][Medline]
  8. Liang T, Hoyer S, Yu R, et al. 1993 Immunocytochemical localization of androgen receptors in human skin using monoclonal antibodies against the androgen receptor. J Invest Dermatol. 100:663–666.[CrossRef][Medline]
  9. Choudhry R, Hodgins MB, Van der Kwast TH, Brinkmann AO, Boersma WJA. 1992 Localization of androgen receptors in human skin by immunohistochemistry: implications for the hormonal regulation of hair growth, sebaceous glands and sweat glands. J Endocrinol. 133:467–475.[Abstract]
  10. Ebling FJ. 1957 The action of testosterone on the sebaceous glands and epidermis in castrated and hypophysectomized male rats. J Endocrinol. 15:297–306.[Medline]
  11. Strauss LS, Kligman AR, Pochi PE. 1962 The effect of androgens and estrogens on human sebaceous glands. J Invest Dermatol. 39:139–143.[Medline]
  12. Sansone G, Reisner RM. 1971 Differential rates of conversion of testosterone to dihydrotestosterone in acne and in normal human skin: a possible pathogenic factor in acne. J Invest Dermatol. 56:366–372.[CrossRef][Medline]
  13. Hay JB, Hodgins MB. 1974 Metabolism of androgens by human skin in acne. Br J Dermatol. 91:123–133.[CrossRef][Medline]
  14. Pochi PE, Strauss JS. 1974 Endocrinologic control of the development and activity of the human sebaceous gland. J Invest Dermatol. 62:191–201.[CrossRef][Medline]
  15. Thomas JP, Oake RJ. 1974 Androgen metabolism in the skin of hirsute women. J Clin Endocrinol Metab. 38:19–22.[Medline]
  16. Lookingbill DP, Horton R, Demers LM, Egan N, Marks JG, Santen RJ. 1985 Tissue production of androgens in women with acne. J Am Acad Dermatol. 12:481–487.[Medline]
  17. Ebling FJ. 1990 The hormonal control of hair growth. In: Orfanos CE, Happle R, eds. Hair and hair diseases. Berlin: Springer-Verlag; 267–299.
  18. Reshef E, Lei ZM, Rao ChV, Pridham D, Chegini N, Luborsky JL. 1990 The presence of gonadotropin receptors in nonpregnant human uterus, human placenta, fetal membranes, and decidua. J Clin Endocrinol Metab. 70:421–430.[Abstract]
  19. Dunn SD. 1986 Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on Western blots by monoclonal antibodies. Anal Biochem. 157:144–153.[CrossRef][Medline]
  20. Steel RGD, Torrie JH. 1960 Principles and procedures of statistics, with special reference to the biological sciences. New York: McGraw-Hill.
  21. Ellis DL, Danzo BJ. 1989 Identification of an androgen receptor in the adult chicken oviduct. J Steroid Biochem. 33:1081–1086.[CrossRef][Medline]
  22. Kovacs WJ, Turney MK. 1988 High efficiency covalent radio labeling of the human androgen receptor. J Clin Invest. 81:342–348.
  23. De SK, Wohlenberg CR, Marinos NJ, Doodnaugh D, Bryant JL, Notkins AL. 1997 Human chorionic gonadotropin hormone prevents wasting syndrome and death in HIV-1 transgenic mice. J Clin Invest. 99:1484–1491.[Medline]
  24. Kachra Z, Guo W-X, Sairam MR, Antakly T. 1997 Low molecular weight components but not dimeric hCG inhibit growth and down-regulate AP-1 transcription factor in Kaposi’s sarcoma cells. Endocrinology. 138:4038–4041.[Abstract/Free Full Text]
  25. Lunardi-Iskandar Y, Bryant JL, Zeman RA, et al. 1995 Tumorigenesis and metastasis of neoplastic Kaposi’s sarcoma cell line in immunodeficient mice blocked by a human pregnancy hormone. Nature. 375:64–68.[CrossRef][Medline]
  26. Gill PS, Lunardi-Iskandar Y, Louie S, et al. 1996 The effects of preparations of human chorionic gonadotropin on AIDS-related Kaposi’s sarcoma. N Engl J Med. 335:1261–1269.[Abstract/Free Full Text]
  27. Milstone LM, Edelson RL. 1988 Endocrine, metabolic and immunologic functions of keratinocytes. New York: New York Academy of Science.
  28. Bos JD. 1993 Skin immune system (SIS). Boca Raton: CRC Press.
  29. Slominski A, Paus R, Wortsman J. 1993 On the potential role of proopiomelanocortin in skin physiology and pathology. Mol Cell Endocrinol 93:C1–C6.
  30. Bhardwaj R, Luger TA. 1994 Proopiomelanocortin production by epidermal cells: evidence for an immune neuroendocrine network in the epidermis. Arch Dematol Res. 287:85–90.
  31. Dumont M, Luu-The V, Dupond E, Pelletier G, Labrie F. 1992 Characterization, expression and immunohistochemical localization of 3ß-hydroxysteroid dehydrogenase/{Delta}5-{Delta}4 isomerase in human skin. J Invest Dermatol. 99:415–421.[CrossRef][Medline]
  32. Slominski A, Ermak G, Mihm M. 1996 ACTH receptor, CYP11A1, CYP17 and CYP21A2 genes are expressed in skin. J Clin Endocrinol Metab. 81:2746–2749.[Abstract]
  33. Andersson S, Bishop RW, Russell DW. 1989 Expression cloning and regulation of steroid 5{alpha}-reductase, an enzyme essential for male sexual differentiation. J Biol Chem. 264:16249–16255.[Abstract/Free Full Text]
  34. Jenkins EP, Andersson S, Imperato-McGinley J, Wilson JD, Russell DW. 1992 Genetic and pharmacological evidence for more than one human steroid 5{alpha}-reductase. J Clin Invest89 :293–300.
  35. Thigpen AE, Russell DW. 1992 Four-amino acid segment in steroid 5{alpha}-reductase 1 confers sensitivity to finasteride, a competitive inhibitor. J Biol Chem. 267:8577–8583.[Abstract/Free Full Text]
  36. Mestayer CH, Berthaut I, Portois M-C, et al. 1996 Predominant expression of 5{alpha}-reductase type 1 in pubic skin from normal subjects and hirsute patients. J Clin Endocrinol Metab. 81:1989–1993.[Abstract]
  37. Boudou P, Chivot M, Vexiau P, et al. 1994 Evidence for decreased androgen 5{alpha}-reduction in skin and liver of men with severe acne after 13-cis-retinoic acid treatment. J Clin Endocrinol Metab. 78:1064–1069.[Abstract]
  38. Slominski A, Ermak G, Hwang J, Chakraborty A, Mazurkiewicz J, Mihm M. 1995 Proopiomelanocortin, corticotropin releasing hormone and corticotropin releasing hormone receptor genes are expressed in human skin. FEBS Lett. 374:113–116.[CrossRef][Medline]
  39. Slominski A, Ermak G, Hwang J, Mazurkiewicz J, Corliss D, Eastman A. 1996 The expression of proopiomelanocortin (POMC) and of corticotropin releasing hormone receptor (CRH-R) genes in mouse skin. Biochim Biophys Acta 1289:247–251.
  40. Tetsuka M, Whitelaw PF, Bremner WJ, Millar MR, Smyth CD, Hillier SG. 1995 Developmental regulation of androgen receptor in rat ovary. J Endocrinol. 145:535–543.[Abstract]
  41. Bao S, Lei ZM, Rao ChV. The presence of functional luteinizing hormone/chorionic gonadotropin receptors in human prostate cell lines. Proc of the 79th Annual Meet of The Endocrine Soc. 1997; P3–403.



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