Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review
"Ant-egg" cataract revisited. / Clemmensen, Kåre; Enghild, Jan J; Ivarsen, Anders et al.
In: Graefe's Archive for Clinical and Experimental Ophthalmology, Vol. 255, No. 1, 2017, p. 119-125.Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review
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TY - JOUR
T1 - "Ant-egg" cataract revisited
AU - Clemmensen, Kåre
AU - Enghild, Jan J
AU - Ivarsen, Anders
AU - Riise, Ruth
AU - Vorum, Henrik
AU - Heegaard, Steffen
PY - 2017
Y1 - 2017
N2 - PURPOSE: Hereditary congenital cataract varies immensely concerning location and form of the lens opacities. A specific and very rare phenotype is called "ant-egg" cataract first described in 1900. "Ant-eggs" have previously been examined using light microscopy, backscattered electron imaging and X-ray scans and electron microscopy. The purpose of this study was to further characterize "ant-egg" cataract using modern technology and display the history of the "ant-eggs" after cataract extraction.METHODS: "Ant-eggs" were examined using Heidelberg SPECTRALIS Optical Coherence Tomography (OCT)(Heidelberg Engineering, Heidelberg, Germany). Ten "ant-eggs" were extracted; four of these as well as control tissue were analyzed by mass spectrometry (AB Sciex). Proteins were identified and their approximate abundances were determined. Immunohistochemical staining was carried out on the remaining "ant-eggs" for cytokeratin and S100.RESULTS: In anterior OCT-images, the "ant-egg" structures are localized on the iris. Comparative pictures showed that they stayed in the same location for more than 45 years. Mass spectrometry of "ant-eggs" yielded a proteome of 56 different proteins. Eighteen of the 56 "ant-egg" proteins (32 %) were neither present in our controls nor in a known fetal lens proteome. Among these were cytokeratin and Matrix-Gla protein. Immunohistochemical reactions were positive for cytokeratin and S100.CONCLUSIONS: This study demonstrates the previously unknown protein composition of the "ant-egg" structures in "ant-egg" cataract. Eighteen of these proteins are not natively found in the human lens. Moreover, "ant-eggs" do not vary over time, after cataract extraction, regarding size and location.
AB - PURPOSE: Hereditary congenital cataract varies immensely concerning location and form of the lens opacities. A specific and very rare phenotype is called "ant-egg" cataract first described in 1900. "Ant-eggs" have previously been examined using light microscopy, backscattered electron imaging and X-ray scans and electron microscopy. The purpose of this study was to further characterize "ant-egg" cataract using modern technology and display the history of the "ant-eggs" after cataract extraction.METHODS: "Ant-eggs" were examined using Heidelberg SPECTRALIS Optical Coherence Tomography (OCT)(Heidelberg Engineering, Heidelberg, Germany). Ten "ant-eggs" were extracted; four of these as well as control tissue were analyzed by mass spectrometry (AB Sciex). Proteins were identified and their approximate abundances were determined. Immunohistochemical staining was carried out on the remaining "ant-eggs" for cytokeratin and S100.RESULTS: In anterior OCT-images, the "ant-egg" structures are localized on the iris. Comparative pictures showed that they stayed in the same location for more than 45 years. Mass spectrometry of "ant-eggs" yielded a proteome of 56 different proteins. Eighteen of the 56 "ant-egg" proteins (32 %) were neither present in our controls nor in a known fetal lens proteome. Among these were cytokeratin and Matrix-Gla protein. Immunohistochemical reactions were positive for cytokeratin and S100.CONCLUSIONS: This study demonstrates the previously unknown protein composition of the "ant-egg" structures in "ant-egg" cataract. Eighteen of these proteins are not natively found in the human lens. Moreover, "ant-eggs" do not vary over time, after cataract extraction, regarding size and location.
U2 - 10.1007/s00417-016-3539-z
DO - 10.1007/s00417-016-3539-z
M3 - Journal article
C2 - 27817115
VL - 255
SP - 119
EP - 125
JO - Graefe's Archive for Clinical and Experimental Ophthalmology
JF - Graefe's Archive for Clinical and Experimental Ophthalmology
SN - 0721-832X
IS - 1
ER -