The epithelial mucin, MUC1, of milk, mammary gland and other tissues

Patton, Stuart; Gendler, Sandra J.; Spicer, Andrew P.

doi:10.1016/0304-4157(95)00014-3

Cited by 254 publications

(202 citation statements)

References 95 publications

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“…MCKD1 (OMIM 174000) is characterized by a bland urinary sediment and no other associated features other than progressive CKD (3). Linkage of MCKD1-1q21 was first shown in the work by Christodoulou et al MUC1 is a membraneanchored mucoprotein expressed in the skin, breast, lung, gastrointestinal tract, salivary glands, and renal distal tubular cells (9). The mucoprotein provides a protective layer to cell surfaces and may be involved in signaling (10).…”

Section: Introductionmentioning

confidence: 99%

Variable Clinical Presentation of an MUC1 Mutation Causing Medullary Cystic Kidney Disease Type 1

Bleyer

Kmoch

Antignac

et al. 2014

Clinical Journal of the American Society of Nephrology

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Background and objectives The genetic cause of medullary cystic kidney disease type 1 was recently identified as a cytosine insertion in the variable number of tandem repeat region of MUC1 encoding mucoprotein-1 (MUC1), a protein that is present in skin, breast, and lung tissue, the gastrointestinal tract, and the distal tubules of the kidney. The purpose of this investigation was to analyze the clinical characteristics of families and individuals with this mutation.Design, setting, participants, & measurements Families with autosomal dominant interstitial kidney disease were referred for genetic analysis over a 14-year period. Families without UMOD or REN mutations prospectively underwent genotyping for the presence of the MUC1 mutation. Clinical characteristics were retrospectively evaluated in individuals with the MUC1 mutation and historically affected individuals (persons who were both related to genetically affected individuals in such a way that ensured that they could be genetically affected and had a history of CKD stage IV or kidney failure resulting in death, dialysis, or transplantation).Results Twenty-four families were identified with the MUC1 mutation. Of 186 family members undergoing MUC1 mutational analysis, the mutation was identified in 95 individuals, 91 individuals did not have the mutation, and111 individuals were identified as historically affected. Individuals with the MUC1 mutation suffered from chronic kidney failure with a widely variable age of onset of end stage kidney disease ranging from 16 to .80 years. Urinalyses revealed minimal protein and no blood. Ultrasounds of 35 individuals showed no medullary cysts. There were no clinical manifestations of the MUC1 mutation detected in the breasts, skin, respiratory system, or gastrointestinal tract.Conclusion MUC1 mutation results in progressive chronic kidney failure with a bland urinary sediment. The age of onset of end stage kidney disease is highly variable, suggesting that gene-gene or gene-environment interactions contribute to phenotypic variability.

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Section: Introductionmentioning

confidence: 99%

Variable Clinical Presentation of an MUC1 Mutation Causing Medullary Cystic Kidney Disease Type 1

Bleyer

Kmoch

Antignac

et al. 2014

Clinical Journal of the American Society of Nephrology

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“…The MUC1 gene encodes a transmembrane mucin expressed by almost all human glandular epithelial tissues and throughout all regions of the gastrointestinal tract (6). The MUC3 and MUC4 genes were initially thought to encode secreted mucins; however, it has recently been shown that these genes encode transmembrane mucins as their dominant isoforms (7,8).…”

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confidence: 99%

MUC13, a Novel Human Cell Surface Mucin Expressed by Epithelial and Hemopoietic Cells

Williams

Wreschner

Tran

et al. 2001

Journal of Biological Chemistry

278

246

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Transmembrane mucins are glycoproteins involved in barrier function in epithelial tissues. To identify novel transmembrane mucin genes, we performed a tblastn search of the GenBank EST data bases with a serine/ threonine-rich search string, and a rodent gene expressed in bone marrow was identified. We determined the cDNA sequence of the human orthologue of this gene, MUC13, which localizes to chromosome band 3q13.3 and generates 3.2-kilobase pair transcripts encoding a 512-amino acid protein comprised of an N-terminal mucin repeat domain, three epidermal growth factor-like sequences, a SEA module, a transmembrane domain, and a cytoplasmic tail (GenBank accession no. AF286113). MUC13 mRNA is expressed most highly in the large intestine and trachea, and at moderate levels in the kidney, small intestine, appendix, and stomach. In situ hybridization in murine tissues revealed expression in intestinal epithelial and lymphoid cells. Immunohistochemistry demonstrated the human MUC13 protein on the apical membrane of both columnar and goblet cells in the gastrointestinal tract, as well as within goblet cell thecae, indicative of secretion in addition to presence on the cell surface. MUC13 is cleaved, and the ␤-subunit containing the cytoplasmic tail undergoes homodimerization. Including MUC13, there are at least five cell surface mucins expressed in the gastrointestinal tract.

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“…From the result of identification, HMWP glycosyls contained NeuNAc, which could combine and inhibit bacteria and virus. For example, Patton et al (1995) reported that NeuNAc of mucin in milk could combine rotavirus that resulted in infant gastroenteritis. Our results showed HMWP also has antibacterial activity.…”

Section: Discussionmentioning

confidence: 99%

“…The results suggested HMWP was a monomer, not dimer or polymer. Various lectins can combine specific glycosyls in glycoprotein (Hurley et al, 1993;Patton et al, 1995). On base of this principle, Western blots of lectins were used to identify the kinds of carbohydrate residues attached to HMWP qualitatively.…”

Section: Isolation Of Hmwpmentioning

confidence: 99%

Isolation and identification of a high molecular weight protein in sow milk

Qin

et al. 2015

Animal

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A high molecular weight protein (HMWP) was isolated and purified from sow milk, and some of its biochemical characteristics and biological functions were identified. The origin of HMWP was also investigated. The molecular weight of HMWP was determined to be about 115 000 and 114 800 by SDS-PAGE and gel filtration, respectively. The sequence of 10 amino acids in N-terminal of HMWP was Ala-Leu-Val-Gln-Ser-Cys-Leu-Asn-Leu-Val. The sequence was blasted against GenBank. No protein showed significant similarity with this sequence suggesting the HMWP may be novel. The result of liquid chromatography mass spectrometry (LC-MS) also proved HMWP could be a novel protein. By amino acid assay, HMWP was rich in glutamate (including glutamine), cysteine, glycine, aspartic acid (including asparagines) and proline. The content of hydrophobic amino acids (Ala, Val, Leu, Ile, Met, Phe and Pro) was lower at 18.59% of the total amino acids suggesting HMWP has high solubility in water. Western blots of lectins were used to identify the kinds of carbohydrate residues attached to HMWP qualitatively. The result showed that HMWP was a kind of glycoprotein containing N-acetylneuraminic acid (NeuNAc), mannose (Man) and/or N-acetylglucosamine (GlcNAc). By isoelectric focusing, HMWP pI was found to be 5.1. Compared with milk fat globule membrane protein (MFGMP) isolated from the sow milk in SDS-PAGE, MFGMP did not contain HMWP. HMWP was assumed to be a secretory milk protein. HMWP was not found in bovine, goat, rabbit or human milk in SDS-PAGE gel suggesting HMWP may be unique to sow milk. By Western blot, HMWP could be detected in sow milk, not in sow serum, which suggests it is synthesized and secreted by the mammary gland. HMWP concentrations in sows milk were the lowest in the first day of lactation, rose significantly during lactation 1 to 7 days. The HMWP content of sows milk remained relatively constant ((1.95 ± 0.13) g/l) during lactation 7 to 20 days. HMWP significantly inhibited Escherichia coli in a dose related manner in vitro. Overall, HMWP could be a novel sow milk protein with implications for the mammary gland and the piglet.

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The epithelial mucin, MUC1, of milk, mammary gland and other tissues

Cited by 254 publications

References 95 publications

Variable Clinical Presentation of an MUC1 Mutation Causing Medullary Cystic Kidney Disease Type 1

Variable Clinical Presentation of an MUC1 Mutation Causing Medullary Cystic Kidney Disease Type 1

MUC13, a Novel Human Cell Surface Mucin Expressed by Epithelial and Hemopoietic Cells

Isolation and identification of a high molecular weight protein in sow milk

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