Meconium ileus in cystic fibrosis is not linked to central repetitive region length variation in MUC1, MUC2, and MUC5AC

Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
Journal of cystic fibrosis: official journal of the European Cystic Fibrosis Society (Impact Factor: 3.48). 06/2014; 13(6). DOI: 10.1016/j.jcf.2014.05.005
Source: PubMed


Mucins are excellent candidates for contributing to the presence of meconium ileus (MI) in cystic fibrosis (CF) due to their extensive genetic variation and known function in intestinal physiology. The length of variants in mucin central repetitive regions has not been explored as "risk" factors for MI in CF.

We investigated the length polymorphisms in the central repetitive regions of MUC1, MUC2, and MUC5AC by Southern blot and tested for association with MI in CF subjects.

No significant associations were found for the allele sizes of any of the genes with respect to the prevalence of MI (p values=0.33, 0.16, and 0.71 for MUC1, MUC2, and MUC5AC, respectively).

The genetic length variants in the central repetitive region of three MUC genes studied are not associated with MI in subjects with CF.

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    ABSTRACT: Mucins are major glycoprotein components of the mucus that coats the surfaces of cells lining the respiratory, digestive, gastrointestinal and urogenital tracts. They function to protect epithelial cells from infection, dehydration and physical or chemical injury, as well as to aid the passage of materials through a tract i.e., lubrication. They are also implicated in the pathogenesis of benign and malignant diseases of secretory epithelial cells. In Human there are two types of mucins, membrane-bound and secreted that are originated from mucous producing goblet cells localized in the epithelial cell layer or in mucous producing glands and encoded by MUC gene. Mucins belong to a heterogeneous family of high molecular weight proteins composed of a long peptidic chain with a large number of tandem repeats that form the so-called mucin domain. The molecular weight is generally high, ranging between 0.2 and 10 million Dalton and all mucins contain one or more domains which are highly glycosylated. The size and number of repeats vary between mucins and the genetic polymorphism represents number of repeats (VNTR polymorphisms), which means the size of individual mucins can differ substantially between individuals which can be used as markers. In human it is only MUC1 and MUC7 that have mucin domains with less than 40 % serine and threonine which in turn could reduce number of PTS domains. Mucins can be considered as powerful two-edged sword, as its normal function protects from unwanted substances and organisms at an arm's length while, malfunction of mucus may be an important factor in human diseases. In this review we have unearthed the current status of different mucin proteins in understanding its role and function in various non-communicable diseases in human with special reference to its organ specific locations. The findings described in this review may be of direct relevance to the major research area in biomedicine with reference to mucin and mucin associated diseases.
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