Dataset Information

Goat's eye integrated with a human cataractous lens: A training model for phacoemulsification.

ABSTRACT: A relatively simple and inexpensive technique to train surgeons in phacoemulsification using a goat's eye integrated with a human cataractous nucleus is described. The goat's eye is placed on a bed of cotton within the lumen of a cylindrical container. This is then mounted on a rectangular thermocol so that the limbus is presented at the surgical field. After making a clear corneal entry with a keratome, the trainer makes a 5-5.5 mm continuous curvilinear capsulorhexis in the anterior lens capsule, creates a crater of adequate depth in the cortex and inserts the human nucleus within this crater in the goat's capsular bag. The surgical wound is sutured, and the goat's eye is ready for training. Creating the capsulorhexis with precision and making the crater of adequate depth to snugly accommodate the human nucleus are the most important steps to prevent excessive wobbling of the nucleus while training.

SUBMITTER: Sengupta S

PROVIDER: S-EPMC4448247 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Goat's eye integrated with a human cataractous lens: A training model for phacoemulsification.

Sengupta Sabyasachi S Dhanapal Praveen P Nath Manas M Haripriya Aravind A Venkatesh Rengaraj R

Indian journal of ophthalmology 20150301 3

A relatively simple and inexpensive technique to train surgeons in phacoemulsification using a goat's eye integrated with a human cataractous nucleus is described. The goat's eye is placed on a bed of cotton within the lumen of a cylindrical container. This is then mounted on a rectangular thermocol so that the limbus is presented at the surgical field. After making a clear corneal entry with a keratome, the trainer makes a 5-5.5 mm continuous curvilinear capsulorhexis in the anterior lens capsu ...[more]

PMID: 25971179

Similar Datasets

Project description:PURPOSE: Post-translational modification (PTM) of lens proteins is believed to play various roles in age-related lens function and development. Among the different types of PTM, phosphorylation is most noteworthy to play a major role in the regulation of various biosignaling pathways in relation to metabolic processes and cellular functions. The present study reported the quantitative analysis of the in vivo phosphoproteomics profiles of human normal and cataractous lenses with the aim of identifying specific phosphorylation sites which may provide insights into the physiologic significance of phosphorylation in relation to cataract formation. METHODS: To improve detection sensitivity of low abundant proteins, we first adopted SDS-gel electrophoresis fractionation of lens extracts to identify and compare the protein compositions between normal and cataractous lenses, followed by tryptic digestion, enrichment of phosphopeptides by immobilized metal affinity chromatography (IMAC) and nano-liquid chromatography coupled tandem mass spectrometry (nanoLC-MS/MS) analysis. RESULTS: By comprehensively screening of the phosphoproteome in normal and cataractous lenses, we identified 32 phosphoproteins and 73 phosphorylated sites. The most abundantly phosphorylated proteins are two subunits of ?-crystallin, i.e., ?B1-crystallin (12%) and ?B2-crystallin (12%). Moreover, serine was found to be the most abundantly phosphorylated residue (72%) in comparison with threonine (24%) and tyrosine (4%) in the lens phosphoproteome. The quantitative analysis revealed significant and distinct changes of 19 phosphoproteins corresponding to 28 phosphorylated sites between these two types of human lenses, including 20 newly discovered novel phosphorylation sites on lens proteins. CONCLUSIONS: The shotgun phosphoproteomics approach to characterize protein phosphorylation may be adapted and extended to the comprehensive analysis of other types of post-translational modification of lens proteins in vivo. The identification of these novel phosphorylation sites in lens proteins that showed differential expression in the cataractous lens may bear some unknown physiologic significance and provide insights into phosphorylation-related human eye diseases, which warrant further investigation in the future.

Dataset Information

Goat's eye integrated with a human cataractous lens: A training model for phacoemulsification.

Publications

Goat's eye integrated with a human cataractous lens: A training model for phacoemulsification.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets