Identification of gallbladder mucin-bilirubin complex in human cholesterol gallstone matrix. Effects of reducing agents on in vitro dissolution of matrix and intact gallstones.

Smith, Bernard F.; LaMont, J. Thomas

doi:10.1172/jci111991

Cited by 103 publications

(27 citation statements)

References 37 publications

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“…Fibrosis also was more in cases with pigment calculi in our study. Mucins have been shown to be a structural component of gallstones [11,30]. Histochemical studies carried out on calculi have demonstrated presence of sulfomucins in them, especially in pigment stones [12].…”

Section: Discussionmentioning

confidence: 99%

A histopathological and histochemical study of cholecystitis

Anupama¹,

V.²,

Ramakrishnan³

et al. 2014

Int J Hepatobiliary Pancreat Dis

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histochemistry, composition of calculi and metaplasia, fibrosis and mucin histochemistry, fibrosis and stone composition indicated a decrease in intraepithelial total acid mucin content in chronic calculous cholecystitis. cases with severe inflammation showed the maximum decrease in sulfomucin, concomitant increase in sialomucin scores and a high incidence of gastric metaplasia. Intestinal metaplasia on other hand did not correlate with the degree of inflammation or sialomucin content. conclusion: this study concludes that normally gallbladder epithelium contains sulfated acid mucins with traces of neutral and sialomucins. the sulfomucin content decreases in chronic calculous cholecystitis and with severe inflammation, total acid mucin content decreases, neutral mucin increases, and there is a higher incidence of gastric metaplasia and pigment stones and correlating with pigment stones. this tends to have an association with severe inflammation, higher degree of fibrosis, gastric metaplasia and presence of sialomucin. Keywords: chronic calculous cholecystitis, Gallbladder stones, Metaplasia, Mucin histochemistryHow to cite this article Anupama P, Menon Nirmala V, Janaky R, Mohammed IL, Alingal MB, Sideeque NA. A histopathological and histochemical study of cholecystitis. Int J Hepatobiliary Pancreat Dis 2014;4:70-80.

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Section: Discussionmentioning

confidence: 99%

A histopathological and histochemical study of cholecystitis

Anupama¹,

V.²,

Ramakrishnan³

et al. 2014

Int J Hepatobiliary Pancreat Dis

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“…Moreover, a serumalbumin family signature with the consensus sequence YX 6 CCX 7 C has also been found between residues 658 and 682. As mucins are well known to bind various hydrophobic substances such as cholesterol, fatty acids, or bilirubin, this small region could be important in the formation of gallstones for example in which mucins have been described to be involved (8,9,48,49).…”

Section: Methodsmentioning

confidence: 99%

Genomic Organization of the 3′ Region of the Human Mucin GeneMUC5B

Desseyn¹,

Aubert²,

Seuningen³

et al. 1997

Journal of Biological Chemistry

115

102

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MUC5B, mapped clustered with MUC6, MUC2, and MUC5AC to chromosome 11p15.5, is a human mucin gene of which the genomic organization is being elucidated. We have recently published the sequence and the peptide organization of its huge central exon, 10,713 base pairs (bp) in length. We present here the genomic organization of its 3 region, which encompasses 10,690 bp. The genomic sequence has been completely determined. The 3 region of MUC5B is composed of 18 exons ranging in size from 32 to 781 bp, contrasting thus with the very large central exon. The sizes of the 18 introns range from 114 to 1118 bp. Some repetitive sequences were identified in four introns. The peptide deduced from the sequence of the 18 exons consists of an 808-amino acid peptide. This carboxyl-terminal region exhibits extensive sequence similarity to MUC2, MUC5AC, and von Willebrand factor, particularly the number and the positions of the cysteine residues, suggesting that this domain may be derived from a common ancestral gene. The presence in these components of a cystine knot also found in growth factors such as transforming growth factor-␤ is of particular interest. Moreover, one part of this peptide is identical to the 196-amino acid sequence deduced from the cDNA clone pSM2-1, which codes for a part of the high molecular weight mucin MG1 isolated from human sublingual gland. Considering the expression pattern of MUC5B and the origin of MG1, we can thus conclude that MUC5B encodes MG1.Mucus is the layer that covers, protects, and lubricates the luminal surfaces of epithelial respiratory, gastrointestinal, and reproductive tracts. These basic properties are due to the viscous and viscoelastic properties of mucins, the major glycoprotein components of mucus. Mucins constitute a family of high molecular mass glycoproteins synthesized by the goblet cells of the epithelia and in some cases by submucosal glands (for more complete reviews, see Refs. 1-3).Alterations of the biosynthesis of mucins affecting the protein core and/or the carbohydrate content linked to the peptide have been observed in numerous pathological situations such as various adenomas and carcinomas, inflammatory diseases such as cystic fibrosis, asthma, chronic bronchitis, or inflammatory bowel diseases (4 -7). Moreover, the hypersecretion of mucins and the presence of alternating hydrophobic and hydrophilic domains in mucins have been shown to play a central role in the pathogenesis of cholesterol gallstones (8, 9).All apomucins contain tandemly repeated sequences rich in threonine and/or serine. Due to the high carbohydrate content, the peptide moiety of mucins has been difficult to characterize. cDNA cloning has enabled researchers to approach the study of the mucins over the past decade. Today, the membrane-associated mucin MUC1 and the secreted MUC7 are the only mucins for which the full-length cDNA and the genomic organization have been reported (10 -13). Both were revealed to be, in fact, small mucins. A complete cDNA of the large secreted mucin MUC2 (14 -17) has been...

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“…This can explain the observations made using electron microscopy of bronchial mucins which have been shown to form complex entangled structures (41) or "bush-like" aggregates (42). The cysteine-rich domains may play a highly conserved role such as the packaging of the mucins or in mediating interactions with numerous other proteins such as, for example, the association with bilirubin in the gall bladder matrix (43). Further studies will be required to more adequately clarify the role of these domains.…”

Section: Determination Of Intron-exon Boundaries On Each Side Of the mentioning

confidence: 93%

Human Mucin Gene MUC5B, the 10.7-kb Large Central Exon Encodes Various Alternate Subdomains Resulting in a Super-repeat

Desseyn

Guyonnet‐Duperat

Porchet

et al. 1997

Journal of Biological Chemistry

157

149

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This latter subdomain has high sequence similarity to the cysteine-rich domains described in MUC2 and MUC5AC. Sequence data of these three genes, together with their clustered organization, lead us to suggest that they may be a part of a multigene family. The super-repeat present in MUC5B is the largest ever determined in mucin genes and the central exon of this gene is, by far, the largest reported for a vertebrate gene.

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Identification of gallbladder mucin-bilirubin complex in human cholesterol gallstone matrix. Effects of reducing agents on in vitro dissolution of matrix and intact gallstones.

Cited by 103 publications

References 37 publications

A histopathological and histochemical study of cholecystitis

A histopathological and histochemical study of cholecystitis

Genomic Organization of the 3′ Region of the Human Mucin GeneMUC5B

Human Mucin Gene MUC5B, the 10.7-kb Large Central Exon Encodes Various Alternate Subdomains Resulting in a Super-repeat

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