Two-hybrid analysis of human salivary mucin MUC7 interactions

Bruno, Lucila S; Li, Xiaojing; Wang, Li; Soares, Rodrigo Villamarim; Siqueira, Camille C.; Oppenheim, Frank G.; Troxler, Robert F.; Offner, Gwynneth D.

doi:10.1016/j.bbamcr.2005.08.007

Cited by 46 publications

(47 citation statements)

References 43 publications

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“…We have examined MG2 from subjects on Western blots probed with anti-MG2 antibodies [31][32][33] and typically, MG2 appeared as a single polydisperse band of approximately 180 kDa. One exception was a subject where MG2 appeared as a doublet with immunoreactive bands of approximately 180 kDa and 125 kDa.…”

Section: Discussionmentioning

confidence: 99%

An unusual glycoform of human salivary mucin MG2

et al. 2011

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Since in a previous study we encountered a subject with an unusual split MG2 banding pattern, the aim of this study was to investigate the molecular basis of this observation. Submandibular/sublingual secretion was collected under resting and stimulated conditions and examined on Western blots probed with anti-MG2 antibodies or on gels stained with periodic acid-Schiff reagent. Genomic DNA was isolated and the N-, tandem repeat (TR), and C-terminal regions of MUC7 were amplified by PCR since MG2 is known to display a genetic polymorphism. Although the typical appearance of MG2 on blots and gels is a single 180 kDa band, salivary secretions from the subject exhibited doublet immunoreactive bands of approximately 180 and 125 kDa. Additionally, under resting conditions the 180 kDa band was predominant whereas upon stimulation the 125 kDa band became predominant. Genomic DNA analysis showed that MUC7 in the individual with split MG2 bands was not truncated and that the MUC7 genotype in this individual was (6/6) where both alleles encoded six TRs. The MG2 split banding pattern observed in this subject was not derived from proteolytic degradation of this salivary mucin in whole saliva or from genetic polymorphism. The expression of two isoforms of MG2 could in principle improve or reduce the activity of this key component of the oral host defense system.

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Section: Discussionmentioning

confidence: 99%

An unusual glycoform of human salivary mucin MG2

et al. 2011

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“…MUC19 encodes probably a gelforming mucin highly expressed in SMGs [37] which could not be detected in human saliva thus far [38]. MUC7 represents a low molecular weight mucin with antimicrobial activity, which interacts with many saliva components, such as amylase, statherin, and histatin-1 [39]. The site of MUC7 synthesis is controversial.…”

Section: Muc7 Muc19 and Fcgbp Are Predominantly Expressed In Mucousmentioning

confidence: 99%

Expression Analysis of Human Salivary Glands by Laser Microdissection: Differences Between Submandibular and Labial Glands

Kouznetsova

Gerlach

Zahl

et al. 2010

Cell Physiol Biochem

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Both the major and minor salivary glands are the sources of saliva, a fluid vital for the maintenance of a healthy oral cavity. Here, the expression profiles of human submandibular (SMG) and labial glands (LG) were compared by RT-PCR analysis of laser microdissected mucous and serous cells, respectively. The focus was on trefoil factor family (TFF) genes, but also other genes encoding secretory proteins (mucins, lysozyme, amylase, statherin, and histatins) or aquaporin 5 were included. Immunofluorescence studies concerning TFF1-3, FCGBP, amylase, and lysozyme are also presented. It was shown that LGs clearly contain serous cells and that these cells differ in their expression profiles from serous SMG cells. Furthermore, all three TFF peptides, together with MUC5B, MUC7, MUC19, and FCGBP, were clearly detectable in mucous acini of both LGs and SMGs. In contrast, lysozyme was differentially expressed in LGs and SMGs. It can be expected that labial saliva may play a particularly important role for protecting the teeth.

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“…Mucin-binding partners are found in the extracellular space in different tissues, most of them being detected in saliva. 61,62 However, as carbohydrate binding proteins, galectins are so far the only known extracellularly located mucin-binding partners of non-salivary origin. 63 Several biochemical studies have provided direct evidence of interaction between mucins and galectins.…”

Section: Mucins and Galectin-1mentioning

confidence: 99%

Interaction of extravillous trophoblast galectin-1 and mucin(s)—Is there a functional relevance?

Bojić‐Trbojević

Krivokuća

Kolundžić

et al. 2016

Cell Adhesion & Migration

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In the course of embryo implantation extensive interaction of the trophoblast with uterine tissue is crucial for adequate trophoblast invasion. This interaction is highly controlled, and it has been pointed out that a specific glycocode and changes in glycosylation may be important for successful implantation and maintenance of pregnancy. Both uterine and trophoblast cells have been shown to express cell surface glycoconjugates and sugar binding proteins, such as mucins (MUC) and galectins (gals). An increasing number of studies have investigated potential candidates interacting in this process. However, knowledge about the biochemical nature of the interactions and their importance for trophoblast cell function, and, consequently, for pregnancy outcome are still lacking. This review is aimed at deliberating the possibility that mucins, as heavily glycosylated proteins, might be among the functionally relevant galectin ligands in human trophoblast, based on both published data and our original research.

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Two-hybrid analysis of human salivary mucin MUC7 interactions

Cited by 46 publications

References 43 publications

An unusual glycoform of human salivary mucin MG2

An unusual glycoform of human salivary mucin MG2

Expression Analysis of Human Salivary Glands by Laser Microdissection: Differences Between Submandibular and Labial Glands

Interaction of extravillous trophoblast galectin-1 and mucin(s)—Is there a functional relevance?

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