Focus on Molecules: Human mucin MUC16

Perez, Beatriz H.; Gipson, Ilene K.

doi:10.1016/j.exer.2007.12.008

Cited by 63 publications

(36 citation statements)

References 4 publications

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“…FUT1 is an epithelial cell-surface receptor for pathogenic strains of E. coli and changes in its expression are thought to modulate pathogen attachment to epithelial cells (Yan et al, 2003;Wang et al, 2012) as is the expression of SERPINE2 (Luo et al, 2011). MUC16 which was highly elevated in this study is a glycosylated matrix protein known to provide a protective role in epithelial tissues (Perez and Gipson, 2008). PARD6B is one of a group of genes responsible for attachment and polarity of epithelial cells to basolateral membranes (Suzuki et al, 2001).…”

Section: Gene Expression and Pathway Analysismentioning

confidence: 96%

“…As such, they prevent the infiltration of potentially pathogenic bacteria into the deeper epithelial layers. Mucous layers are known lubricating barriers in epithelial cells and are a necessary component in the prevention of pathogen attachment (Perez and Gipson, 2008). FUT1 is an epithelial cell-surface receptor for pathogenic strains of E. coli and changes in its expression are thought to modulate pathogen attachment to epithelial cells (Yan et al, 2003;Wang et al, 2012) as is the expression of SERPINE2 (Luo et al, 2011).…”

Section: Gene Expression and Pathway Analysismentioning

confidence: 99%

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Butyrate-Mediated Genomic Changes Involved in Non-Specific Host Defenses, Matrix Remodeling and the Immune Response in the Rumen Epithelium of Cows Afflicted With Subacute Ruminal Acidosis

Dionissopoulos

Laarman

AlZahal

et al. 2013

American Journal of Animal and Veterinary Sciences

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Subacute Ruminal Acidosis (SARA) is a disorder in cattle which can lead to chronic inflammation in the rumen epithelium, known as rumenitis. Butyrate has been shown to attenuate some of the detrimental effects of inflammatory gastroenteral disorders but the molecular mechanisms mediated by butyrate have not been defined. The objective of this study was to define the inflammatory-related genomic changes responsible for the beneficial effects of butyrate. Experimentally, 16 fistulated dairy cows at mid-lactation were fed a SARA-inducing (45% non-fiber carbohydrate) diet beginning 2 days before the beginning of treatment and continuing throughout the experiment. Cows were then evenly divided into treatment groups where a carrier with (n = 8) or without (n = 8) supplemental butyrate (2.5% initial DM intake) was deposited into the rumen daily for 7 days. The minimum rumen pH was higher in cows with supplemental butyrate (4.96±0.09 to 5.20±0.05, p = 0.040), but mean pH, maximum pH and the duration for which rumen pH was below 5.6 was unaffected. Free plasma Lipopolysaccharide (LPS) concentration was unaffected by treatment as was the concentration of Serum Amyloid A (SAA), although the LPS Binding Protein (LBP) concentration was increased by the addition of butyrate to the rumen (6.91±0.29 to 7.93±0.29 µg mL −1 , p = 0.024). Of the rumen Short Chain Fatty Acids (SCFA) tested, only butyrate showed a pronounced treatment effect, rising from 8.60±0.94 to 21.60±0.94 mM (p≤0.0001). Plasma Beta-Hydroxybutyrate (BHBA) concentration also increased (799.50±265.24 to 3261.63±265.24 µM, p≤0.001). Butyrate infusion did not affect milk parameters (total fat, lactose, total protein and LOS); however, when related to dry matter intake, milk production efficiency was increased (p = 0.035). Microarray and qRT-PCR analyses of rumen papillae biopsies collected on day 7 found that butyrate administration affected (p≤0.05) the expression of genes involved in Non-Specific Host Defense (NSHD), Remodeling or adaptation (RM) and Immune Response (IR). Of the 49 genes tested by qRT-PCR, 9 (LCN2, MMP1, MUC16, GPX2, CSTA, FUT1, SERPINE2, BCAM, RAC3) were upregulated, 20 (MTOR, AKIRIN2, NFKBIZ, NFKB2, ACVR2A, LAMB1, FRS2, PPARD, LBP, NEDD4L, SGK1, DEDD2, MAP3K8, PARD6B, PLIN2, ADA, HPGD, FMO5, BMP6, TCHH) were downregulated and 20 were unchanged due to butyrate administration in the proximal gastrointestinal tract. AJAVSThese results demonstrate the potential protective effect and molecular mechanisms involved in a novel butyrate treatment for inflammatory gastrointestinal conditions.

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Section: Gene Expression and Pathway Analysismentioning

confidence: 96%

Section: Gene Expression and Pathway Analysismentioning

confidence: 99%

Butyrate-Mediated Genomic Changes Involved in Non-Specific Host Defenses, Matrix Remodeling and the Immune Response in the Rumen Epithelium of Cows Afflicted With Subacute Ruminal Acidosis

Dionissopoulos

Laarman

AlZahal

et al. 2013

American Journal of Animal and Veterinary Sciences

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“…as a mixture of low glycosylated proteins ranging from 97 kDa to well over 200 kDa, all supposed to originate from monomeric MUC16, which is estimated to be the largest member of the mucin family, having an amino acid moiety of 22156 AA (O'Brien et al, 2001Perez and Gipson, 2008). MUC16 can be cleaved between the N-and C-terminal fragments, possibly in the SEA (sea urchin sperm protein, enterokinase, and agrin) domain, with potential influence on immunoreactivity, since both epitopes for OC125 and M11-like antibodies contain parts of two consecutive SEA domains with a linker (Maeda et al, 2004;Blalock et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Analysis of CA125 antigen in normal human seminal plasma highlightsthe molecular heterogeneity of underlying glycosylated species

Mitić¹,

Milutinović²,

Janković³

2017

Turk J Biol

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led to its definition as a repeating peptide epitope on MUC16 (Yin et al., 2001). The epitope map of CA125 is, however, very complex and varies among mucin molecules expressed under different pathophysiological conditions and from different sources. This results in typical/unique patterns sharing some commonality (Nustad et al., 2002).Structural data obtained on CA125/MUC16 indicated extreme heterogeneity, probably due to the existence of molecular species differing in mass and glycosylation. CA125-immunoreactivity was associated with high molecular mass macromolecular moieties of 3-5 MDa mucin and 400 kDa-200 kDa precursors, but also with low molecular mass species at 55 and 40, down to 10-15 kDa (Hanisch et al., 1985;Nustad et al., 1998;Yin et al., 2001). As for glycosylation, the total glycan content varied from moderate, as in glycoproteins, to extremely high (more than 28%), as in mucins (Kui Wong et al., 2003). Relatively high abundance of N-glycans, not typical for other mucins and diverse O-glycan associated epitopes such as CA19-9 and sTn, have been reported (

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“…[233] Diverse Mucine, die in Körperflüssigkeiten vorkommen, z. B. das Epitop von CA125, [234] wurden auf ihre Eignung als Tumormarker getestet. Die Klonierung des Gens, das für CA125 kodiert, zeigte, dass es das MUC16-Gen ist.…”

Section: O-glycane In Den Mucinen Von Schleimhautgewebeunclassified

Das Tn‐Antigen – strukturell einfach und biologisch komplex

Otto

Cummings

2011

Angewandte Chemie

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Die Glycoproteine tierischer Zellen enthalten vielfältige Glycanstrukturen, die co‐ und/oder posttranslational an die Proteine angeheftet werden. Mehr als zwanzig verschiedene Bindungsarten von Glycanen an Proteine sind bekannt, doch sind N‐Glycane (gebunden an Asn) und O‐Glycane (gebunden an Ser/Thr) die häufigsten. Ein abnormes O‐Glycan, das bei Krebs und anderen menschlichen Erkrankungen auftritt, ist das Tn‐Antigen. Es hat eine einfache Struktur, bestehend aus einem N‐Acetyl‐D‐galactosamin, das α‐glycosidisch an einen Serin‐ oder Threoninrest gebunden ist. Das Tn‐Antigen war eines der ersten Glycokonjugate, die chemisch synthetisiert wurden. Es wird normalerweise von einer spezifischen Galactosyltransferase, der T‐Synthase, im Golgi‐Apparat modifiziert. Die Expression aktiver T‐Synthase hängt vom molekularen Chaperon Cosmc ab, dessen Gen auf dem X‐Chromosom liegt. Genmutationen, die die Funktion von T‐Synthase, Cosmc oder anderen an der O‐Glycosylierung beteiligten Faktoren beeinträchtigen, können zur Expression des Tn‐Antigens führen. Da dieses bei einer Reihe von Krankheiten auftritt, besteht großes Interesse, es für die Entwicklung von Impfstoffen und anderen therapeutischen Ansätzen zu nutzen.

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Focus on Molecules: Human mucin MUC16

Cited by 63 publications

References 4 publications

Butyrate-Mediated Genomic Changes Involved in Non-Specific Host Defenses, Matrix Remodeling and the Immune Response in the Rumen Epithelium of Cows Afflicted With Subacute Ruminal Acidosis

Butyrate-Mediated Genomic Changes Involved in Non-Specific Host Defenses, Matrix Remodeling and the Immune Response in the Rumen Epithelium of Cows Afflicted With Subacute Ruminal Acidosis

Analysis of CA125 antigen in normal human seminal plasma highlightsthe molecular heterogeneity of underlying glycosylated species

Das Tn‐Antigen – strukturell einfach und biologisch komplex

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