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Collagens, the basic proteins of the human body

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Czarny-Ratajczak M., Latos-Bielenska L.-B. A., Latos-Bielenska A.

Journal of Applied Genetics

2000

vol. 41

issue 4

317-330

Collagens are structural elements of many tissues in the human body. The family of collagens can be divided into fibrillar and non-fibrillar collagens. The criterion of the classification is the structure of these proteins. Mutations in the genes encoding collagens cause a variety of human diseases that include osteogenesis imperfecta, some forms of osteoporosis, chondrodysplasias, some types of Ehlers-Danlos syndrome, arterial and intracranial aneurysms, epidermolysis bullosa and the renal disease known as Alport syndrome. The detection of mutations is important both scientifically and clinically. Defining the molecular defects underlying a disorder helps in the understanding of not only the properties of the mutated protein but also the function of the normal protein. Even though many mutations in the genes encoding collagens have been described, the pathogenic consequences of some of the mutations are not fully understood. The important rationale for mutation detection is the clinical use of molecular diagnostics in genetic counselling and differential diagnosis.

Only neutral polymorphisms found in the TIGR/myocilin gene of 45 Polish patients with primary open-angle glaucoma

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Krawczynski M. R., Czarny-Ratajczak M., Pecold K., Latos-Bielenska A.

Journal of Applied Genetics

2004

vol. 45

issue 2

275-279

The aim of the study was to identify mutations of the TIGR gene in Polish patients with primary open-angle glaucoma (POAG) and to define possible genotype-phenotype correlations. The study included 45 patients with a verified diagnosis of POAG. The PCR amplification of all three exons of the TIGR gene and screening for the sequence changes by CSGE analysis was done for every patient. The probes with identified heteroduplexes were sequenced. Altogether 315 PCR products were obtained. The CSGE analysis detected 60 possible changes of the sequence in 28 patients. 34 heteroduplexes were chosen for sequencing, including 29 unique changes and 5 changes representative of identical heteroduplexes. Direct sequencing enabled detection of only four different changes in the TIGR gene sequence. Three of them: 5?UTR ?83GA (in 14 patients), +227 exon 1 GA, Arg76Lys (in 14 patients) and +311 exon 3 TC, Tyr347Tyr (in 4 patients) have already been described in the literature as neutral polymorphisms of the gene. Only one change in the promoter, 5?UTR ?126TC (in 2 patients), has not been described in the literature to date. However, this change does not alter directly the sequence of amino acids in myocilin, so it is difficult to conclude on its pathogenetic role. Thus our study showed only neutral polymorphisms of the TIGR gene. This suggests that the patients probably have mutations in other genes, so other loci that predispose to POAG must be analyzed.

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2 Journal of Applied Genetics

1 2004

1 2000

2 Czarny-Ratajczak M.

2 Latos-Bielenska A.

1 Krawczynski M. R.

1 Latos-Bielenska L.-B. A.

1 Pecold K.

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Collagens, the basic proteins of the human body

Only neutral polymorphisms found in the TIGR/myocilin gene of 45 Polish patients with primary open-angle glaucoma