Mac-2 binding protein and galectin-3 expression in mucinous tumours of the ovary: an annealing control primer system and immunohistochemical study

Pathology ◽  
2009 ◽  
Vol 41 (3) ◽  
pp. 229-233 ◽  
Author(s):  
Ju-Han Lee ◽  
Xianglan Zhang ◽  
Bong Kyung Shin ◽  
Eung Seok Lee ◽  
Insun Kim
2021 ◽  
Vol 12 ◽  
Author(s):  
Shihan Zhen ◽  
Ruoxin Cai ◽  
Xuelian Yang ◽  
Yanan Ma ◽  
Deliang Wen

BackgroundGalectin-3-binding protein (GAL-3BP) is a ubiquitous and multifunctional secreted glycoprotein, which functions in innate immunity and has been highlighted as a potential mediator of adipose inflammation in obesity. In this study, we aimed to identify whether GAL-3BP is a novel biological marker for metabolic syndrome (MetS).MethodsThe biochemical and anthropometric variables of the 570 participants in this study were evaluated using standard procedures. Their serum GAL-3BP levels were measured using enzyme-linked immunosorbent assay (ELISA), while the association between the glycoprotein and MetS was analyzed using multiple logistic regression analyses. Moreover, an experimental MetS model was established. The expression of GAL-3BP in serum and adipose tissue was measured using ELISA and western blotting. Lipid accumulation was determined with the use of immunohistochemistry and immunofluorescent staining.ResultsThe serum GAL-3BP level was found to be positively associated with MetS. The logistic regression analyses demonstrated that participants expressing the upper levels of GAL-3BP were more likely to develop MetS than those expressing less of the glycoprotein (OR = 2.39, 95%CI: 1.49, 3.83). The association between the serum GAL-3BP level and MetS was found preferentially in postmenopausal women (OR = 2.30, 95%CI: 1.31, 4.05). In addition, GAL-3BP was increased in the serum and visceral adipose tissue (VAT) of high fat diet (HFD) mice. Moreover, GAL-3BP was highly expressed in VAT macrophages.ConclusionsThis study confirmed serum GAL-3BP to be positively associated with MetS, highlighting it as a useful biological marker of MetS in Chinese participants.


2010 ◽  
Vol 7 (2) ◽  
pp. 888-895 ◽  
Author(s):  
Stefan Ückert ◽  
Eginhard S. Waldkirch ◽  
Knut Albrecht ◽  
Julia Sonnenberg ◽  
Kristina Langnäse ◽  
...  

2019 ◽  
Vol 36 (2) ◽  
pp. 177-183
Author(s):  
Ibrahim Halil Yavuz ◽  
Goknur Ozaydin-Yavuz ◽  
Erdem Çokluk ◽  
Zehra Kurtoğlu ◽  
Serap Gunes Bilgili

2017 ◽  
Vol 114 (50) ◽  
pp. E10687-E10696 ◽  
Author(s):  
Habib Bouguenina ◽  
Danièle Salaun ◽  
Aurélie Mangon ◽  
Leslie Muller ◽  
Emilie Baudelet ◽  
...  

Control of microtubule dynamics underlies several fundamental processes such as cell polarity, cell division, and cell motility. To gain insights into the mechanisms that control microtubule dynamics during cell motility, we investigated the interactome of the microtubule plus-end–binding protein end-binding 1 (EB1). Via molecular mapping and cross-linking mass spectrometry we identified and characterized a large complex associating a specific isoform of myomegalin termed “SMYLE” (for short myomegalin-like EB1 binding protein), the PKA scaffolding protein AKAP9, and the pericentrosomal protein CDK5RAP2. SMYLE was associated through an evolutionarily conserved N-terminal domain with AKAP9, which in turn was anchored at the centrosome via CDK5RAP2. SMYLE connected the pericentrosomal complex to the microtubule-nucleating complex (γ-TuRC) via Galectin-3–binding protein. SMYLE associated with nascent centrosomal microtubules to promote microtubule assembly and acetylation. Disruption of SMYLE interaction with EB1 or AKAP9 prevented microtubule nucleation and their stabilization at the leading edge of migrating cells. In addition, SMYLE depletion led to defective astral microtubules and abnormal orientation of the mitotic spindle and triggered G1 cell-cycle arrest, which might be due to defective centrosome integrity. As a consequence, SMYLE loss of function had a profound impact on tumor cell motility and proliferation, suggesting that SMYLE might be an important player in tumor progression.


2003 ◽  
Vol 48 (10) ◽  
pp. 2788-2795 ◽  
Author(s):  
Shiro Ohshima ◽  
Stefan Kuchen ◽  
Christian A. Seemayer ◽  
Diego Kyburz ◽  
Astrid Hirt ◽  
...  

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