Expression of Estrogen Receptors α and β, Androgen Receptors and Progesterone Receptors in Human Cornea

Expression of Estrogen Receptors α and β, Androgen Receptors and Progesterone Receptors in Human Cornea

ABSTRACTS Abstracts of Published Articles in Nippon Ganka Gakkai Zasshi (Journal of the Japanese Ophthalmological Society) Expression of Estrogen Re...

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ABSTRACTS

Abstracts of Published Articles in Nippon Ganka Gakkai Zasshi (Journal of the Japanese Ophthalmological Society)

Expression of Estrogen Receptors  and , Androgen Receptors and Progesterone Receptors in Human Cornea

Immunohistochemical Study of the Extracellular Matrices Related to Accommodation in Monkeys

Purpose: Using immunohistochemical techniques and reverse transcription polymerase chain reaction (RT-PCR), we examined the localization of estrogen receptors  and  (ER, ), androgen receptor (AR), and progesterone receptor (PR) in human corneas. Materials and Methods: Using formalin-fixed donor human cornea, we did immunohistochemical staining after making transverse sections, and examined the localization of receptors. Also, we extracted mRNA from primary culture cells of the corneal epithelium and stroma as well as the endothelial cell layer and epithelial layer of the cornea, and we performed RT-PCR and examined the expression of each receptor. Results: Immunohistochemical staining revealed that ER was localized in corneal epithelial cells as well as in corneal stromal cells, and ER, AR and PR were localized in corneal epithelial, stromal, and endothelial cells. ER, ER, and AR mRNA expression was observed in cultured and in vivo epithelium and cultured stroma cells. PR mRNA was expressed not only in cultured and in vivo epithelium and in cultured stroma cells but also in endothelium Conclusions: We detected the localization of estrogen receptors  and , androgen receptors, and progesterone receptors in the human cornea. (J Jpn Opthalmol Soc 106:557–564, 2002)

Purpose: The mechanism of accommodation was studied by immunohistochemical staining of extracellular matrices in monkey eyes. Methods: Frozen sections from five pairs of postmortem eyes donated by physiologists were used. The antigens listed in Table 1 were selected, and a 2- or 3-step staining technique was used. Confocal laser microscopy was used to evaluate the staining and to take photographs. Many frames were reconstituted for the Figures. Results: a) The ciliary muscle was divided into circular and longitudinal portions by arrangement of -smooth muscle actin and surrounded by dense nets of -elastin at the inner border under pigmented ciliary epithelium. Elastin nets extended into the stroma of the ciliary processes. In the lens, elastin was observed in the equatorial and central subcapsular area. b) Zonules were heavily stained by fibrillin-1 as bundles. Continuous fibers connected the surface of ciliary processes with the lens capsule, and were also anchored along the ciliary epithelium toward the pars plana. Type IV collagen was seen in circumferential lens capsule and between the lens fibers, especially in the equator and central cortex. c) There was more -1A adrenoceptor in the longitudinal than in the circular portion of the ciliary muscle. Conclusion: Our results provide an argument against Helmholtz’s theory, but in favor or Tsherning’s theory. The accommodation to near might be accomplished by contraction of circular ciliary muscle held by elastin nets pulling the zonules centripetally. The zonular tension puts pressure on the equator and also pulls the lens capsule anterocentrally. This coordination of the matrices will shorten the equatorial plane of the lens and expand the inter-lens-fiber space, making the polar axis wider. In far accommodation, longitudinal muscle will pull the zonules pe-

Tsutomu Hadeyama,* Kiyoo Nakayasu, Ha NT and Shinji Nakamura *Department of Ophthalmology, Juntendo University School of Medicine; †Department of Pathology, Juntendo University School of Medicine PII S0021-5155(02)00705-0 Jpn J Ophthalmol 47, 226–231 (2003) © 2003 Japanese Ophthalmological Society Published by Elsevier Science Inc.

0021-5155/03/$–see front matter