Human CRYBB1 (Crystallin Beta B1) gene mutation and application thereof

Abstract

The invention relates to human CRYBB1 (Crystallin Beta B1) gene mutation and relevancy thereof to cataract, provides a method for detecting the human CRYBB1 gene mutation, and provides a related detection kit. In the method, whether C (Cytosine)-to-T (Thymine) mutation exists is detected by determining nucleotide at a 18458th site in a sequence shown as SEQ ID NO: 1. Research finds that C-to-T single nucleotide polymorphism exists in the nucleotide at the 18458th site in the sequence shown as the SEQ ID NO: 1, in the human CRYBB1 gene; and when the C-to-T mutation occurs, Q227X in an amino acid sequence SEQ ID NO: 2 of beta B1 crystallin is caused, and truncated beta B1 crystallin protein is formed and is related to morbidity of genetic cataract. The method can be used for aided diagnosis of the cataract for finding out a potential carrier of the genetic cataract, so that a basis is provided for the prevention of the disease.

Description

technical field

[0001] The present invention relates to a gene mutation of human CRYBB1 and a method for analyzing the mutation of human CRYBB1 gene, as well as the use of the mutation in assisting diagnosis in cataract. Background technique

[0002] Crystallin was first described in 1893 by Find[ C.T., Untersuchungen der. Protein substanzen in den lichtbrechenden Medien des Auges. Z. Physiol. Chem. 1893; 18:61-106]. It is the main structural protein of the vertebrate lens, accounting for 90% of the total lens protein. Crystallin has a special spatial structure, which plays a very important role in maintaining the transparency of the lens. Crystallins can be divided into α-, β-, γ-crystallins according to molecular weight from large to small.

[0003] β-crystallin (Beta crystallin, CRYB) can be divided into acidic protein (βA) and basic protein (βB) two subgroups, each subgroup is encoded by three genes (CRYBA1, 2, 3; CRYBB1, 2 , 3) [Jochen Graw. Genetics of crystalli...

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