Changes of lectin staining patterns in the Golgi stack during cell differentiation were examined in the ameloblasts of developing rat molar tooth germs, using HRP-labeled lectins: Canavalia ensiformis (Con A), Griffonia simplicifolia I (GS-I), Glycine max (SBA), Ulex europeus I (UEA-I), Triticum vulgaris (WGA), and Arachis hypogaea (PNA). The Golgi stacks of the inner enamel epithelial cells and the presecretory ameloblasts were stained with the lectins, although the staining strength and pattern varied among the stacks with each lectin. In some cases, the reaction products for the lectins were observed in most or all saccules of the Golgi stack. In the secretory ameloblasts, however, discrete staining patterns of the Golgi stack were found for each lectin. The reaction products deposited in definite saccules of the Golgi stack of the secretory ameloblast, especially for UEA-I and PNA which stained only the trans Golgi saccules of the stack. The reaction-positive saccules distributed more extensively in the Golgi stack of the inner enamel epithelial cell and the presecretory ameloblast than in the secretory ameloblast. These findings suggest that the Golgi stack is not fully compartmentalized in the inner enamel epithelial cell and the presecretory ameloblast. It is proposed that, in the differentiating ameloblast, various glycosyltransferases may coexist in most saccules of the Golgi stack.

Download full-text PDF

Source
http://dx.doi.org/10.1002/ar.1092360209DOI Listing

Publication Analysis

Top Keywords

golgi stack
32
inner enamel
12
enamel epithelial
12
saccules golgi
12
golgi
10
stack
9
changes lectin
8
lectin staining
8
developing rat
8
rat molar
8

Similar Publications

Golgi abnormalities have been linked to aging and age-related diseases, yet the underlying causes and functional consequences remain poorly understood. This study identifies the interaction between age-associated zinc deficiency and Golgi stress as a critical factor in cellular aging. Senescent Golgi bodies from human fibroblasts show a fragmented Golgi structure, associated with a decreased interaction of the zinc-dependent Golgi-stacking protein complex Golgin45-GRASP55.

View Article and Find Full Text PDF

Electroacupuncture pretreatment ameliorates Golgi stress and the inflammation response against endotoxin-induced lung injury.

Int Immunopharmacol

December 2024

Tianjin Nankai Hospital, Tianjin Medical University, Tianjin, China; Institute of Integrative Medicine for Acute Abdominal Diseases, Tianjin, China; Tianjin Key Laboratory of Acute Abdomen Disease Associated Organ Injury and ITCWM Repair, Tianjin, China. Electronic address:

Background: Sepsis is a life-threatening condition involving organ dysfunction characterized by a generalized inflammatory syndrome, and the associated mortality rate is high. Electroacupuncture (EA) exerts benefits in endotoxemia-induced lung injury, mainly through lung inflammation reduction and cellular homeostasis, although the anti-inflammatory mechanisms underlying these benefits remain to be completely understood.

Methods: Mice were pretreated with EA or sham EA therapy 5 days prior to the induction of endotoxemia through the administration of lipopolysaccharide (LPS) and cecal ligation and puncture (CLP).

View Article and Find Full Text PDF

RudLOV is an optically synchronized cargo transport method revealing unexpected effects of dynasore.

EMBO Rep

December 2024

Program of Life and Environmental Science, Graduate School of Integral Science for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, 739-8521, Japan.

Live imaging of secretory cargoes is a powerful method for understanding the mechanisms of membrane trafficking. Inducing the synchronous release of cargoes from an organelle is key for enhancing microscopic observation. We developed an optical cargo-releasing method, 'retention using dark state of LOV2' (RudLOV), which enables precise spatial, temporal, and quantity control during cargo release.

View Article and Find Full Text PDF

Alcohol misuse increases infections and cancer fatalities, but mechanisms underlying its toxicity are ill-defined. We show that alcohol treatment of human tracheobronchial epithelial cells leads to inactivation of giantin-mediated Golgi targeting of glycosylation enzymes. Loss of core 2 N-acetylglucosaminyltransferase 1, which uses only giantin for Golgi targeting, coupled with shifted targeting of other glycosylation enzymes to Golgi matrix protein 130-Golgi reassembly stacking protein 65, the site normally used by core 1 enzyme, results in loss of sialyl Lewis x and increase of sialyl Lewis a and α2-6sialo mucin O-glycans.

View Article and Find Full Text PDF

The Golgi apparatus plays a crucial role in the delivery of lysosomal enzymes. Golgi Reassembly Stacking Proteins, GRASP55 and GRASP65, are vital for maintaining Golgi structure and function. GRASP55 depletion results in the missorting and secretion of the lysosomal enzyme Cathepsin D (Xiang .

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!