Biochemical analysis of membrane proteins from an early maturation stage of phagosomes

2007 ◽  
pp. 431-436
Author(s):  
Michael T. Maicher ◽  
Arno Tiedtke
Keyword(s):  
Membrane Proteins ◽  
Biochemical Analysis ◽  
Maturation Stage ◽  
Early Maturation

Gene Expression and Localization of Amelogenin in the Rat Incisor

1996 ◽  
Vol 10 (2) ◽  
pp. 201-207 ◽  
Author(s):  
T. Inage ◽  
H. Shimokawa ◽  
K. Wakao ◽  
S. Sasaki
Keyword(s):  
Gene Expression ◽  
Amino Acids ◽  
Maturation Stage ◽  
Enamel Matrix ◽  
Rat Incisor ◽  
Early Maturation ◽  
Incisal Edge ◽  
Enamel Epithelium ◽  
Developing Rat

Gene expression and localization of amelogenin were studied in the developing rat incisor by the methods of in situ hybridization and immunohistochemistry. ISH revealed the first expression of amelogenin mRNA in the inner enamel epithelium of the cervical loop. The signals were clearly observed in pre-ameloblasts in the region bordering on predentin formation and became more intense toward the cells on the initial enamel matrix secretion. The maximal signals were found in the cytoplasm of secretory ameloblasts. From the terminal secretion zone, the signals then became gradually weaker toward the incisal edge but were still evident in the cytoplasm of shortening, transitional ameloblasts and those at the early maturation stage. No signals were found in the cells of the stratum intermedium and stellate reticulum throughout amelogenesis. Immunohistochemistry by means of an antibody against amelogenin C-telopeptide consisting of 12 amino acids revealed immunoreaction in the secretory ameloblasts reacting to the ISH. When a polyclonal antibody against amelogenin was used, immunoreaction was found in the distal ends of ruffle-ended ameloblasts (RA) in the maturation zone. Those results indicated that amelogenin is synthesized by ameloblastic cells from the inner enamel epithelium to the early maturation stage and is then resorbed by the RA.

Cadherin-related Neuronal Receptors in Incisor Development

2003 ◽  
Vol 82 (1) ◽  
pp. 17-22 ◽  
Author(s):  
E. Fukumoto ◽  
H. Sakai ◽  
S. Fukumoto ◽  
T. Yagi ◽  
O. Takagi ◽  
...  
Keyword(s):  
Early Phase ◽  
Late Phase ◽  
Maturation Stage ◽  
Early Maturation ◽  
Cell Matrix ◽  
Maturation Stages ◽  
Cell Matrix Interactions ◽  
Late Maturation ◽  
Dentin Formation

Cadherins are cell adhesion molecules that are critical for tissue development. In this report, we identified members of the cadherin family cadherin-related neuronal receptors (CNRs) 1 and 5 expressed in rat incisors by the differential display method. Quantitative RT-PCR revealed that CNR1 mRNA is expressed in the secretory stage but reduced in the early-maturation stage, while CNR5 mRNA is expressed in both these stages. In situ hybridization showed that strong expression of CNR1 is strong in the secretory stage, but reduced in the early phase and diminished in the late phase of the early-maturation stage. CNR5 mRNA is expressed almost at the same levels in the secretory and in the early phase of the early-maturation stages but is absent in the late phase of the early-maturation stage. Both CNR1 and 5 mRNA are continuously expressed in odontoblasts. Immunohistology showed that CNR proteins are expressed in the secretory and early-maturation stages of ameloblasts, but no protein expression at the late-maturation stage was observed. CNR proteins were continuously expressed in odontoblasts. We found that recombinant CNR1 binds dental epithelial and mesenchymal cells through N-terminal domain EC1 in vitro. These results suggest that CNR1 and CNR5 may play an important role in enamel and dentin formation, probably through cell-cell and/or cell-matrix interactions.

scholarly journals Cytochemical and biochemical characterization of glycoproteins in forming and maturing enamel of the rat incisor.

1989 ◽  
Vol 37 (11) ◽  
pp. 1619-1633 ◽  
Author(s):  
A Nanci ◽  
J P Ahluwalia ◽  
S Zalzal ◽  
C E Smith
Keyword(s):  
Secretory Granules ◽  
Helix Pomatia ◽  
Extracellular Proteins ◽  
Maturation Stage ◽  
Variable Degree ◽  
Rat Incisor ◽  
Double Labeling ◽  
Early Maturation ◽  
Enamel Proteins ◽  
Lowicryl K4m

Biochemical and histochemical studies have shown the presence of various carbohydrates in enamel. Using lectin-gold cytochemistry, we have examined the distribution of glycoconjugates containing N-acetyl-D-galactosamine (GalNAc) and/or N-acetyl-glucosamine (GlcNAc)/N-acetyl-neuraminic acid (NeuNAc) residues in rat incisor ameloblasts and in forming and maturing enamel embedded in Lowicryl K4M, LR Gold, and LR White resins. The enamel proteins that contain these carbohydrate moieties were further characterized by lectin blotting. All three resins allowed, albeit to a variable degree, detection of the binding sites for Helix pomatia agglutinin (HPA) and wheat germ agglutinin (WGA) GalNAc, and GlcNAc/NeuNAc, respectively. In general, Lowicryl K4M permitted more intense reactions with both lectins. Lectin binding was observed over the rough endoplasmic reticulum (weak labeling with WGA), the Golgi apparatus, lysosomes, secretory granules, and the enamel matrix. These compartments were shown by double labeling with WGA and anti-amelogenin antibody, and by previous immunocytochemical studies, to contain enamel proteins. Furthermore, WGA binding was more concentrated at the growth sites of enamel. Lectin blotting showed that several proteins in the amelogenin group were glycosylated and contained the sugars GalNAc and GlcNAc/NeuNAc. Fewer proteins were stained by HPA than by WGA, and the staining pattern suggested that the extracellular proteins recognized by these two lectins are processed differently. The HPA-reactive proteins were lost by or during the early maturation stage, whereas many of the WGA-reactive proteins persisted into the mid maturation stage. The heterogeneous staining of certain protein bands observed with WGA suggests that they contain more than one component. Two distinct glycoproteins containing GlcNAc/NeuNAc also appeared during the maturation stage. These results are consistent with the notion that ameloblasts produce an extracellular matrix composed mainly of glycosylated amelogenins which are differently processed throughout amelogenesis.

scholarly journals Getting on target: The archaeal signal recognition particle

Archaea ◽  
2002 ◽  
Vol 1 (1) ◽  
pp. 27-34 ◽  
Author(s):  
Christian Zwieb ◽  
Jerry Eichler
Keyword(s):  
Membrane Proteins ◽  
Biochemical Analysis ◽  
Protein Targeting ◽  
Polypeptide Chain ◽  
Protein Translocation ◽  
Signal Recognition Particle ◽  
Evolutionary Significance ◽  
Signal Recognition ◽  
Functional Behavior ◽  
Translocation Pathway

Protein translocation begins with the efficient targeting of secreted and membrane proteins to complexes embedded within the membrane. In Eukarya and Bacteria, this is achieved through the interaction of the signal recognition particle (SRP) with the nascent polypeptide chain. In Archaea, homologs of eukaryal and bacterial SRP-mediated translocation pathway components have been identified. Biochemical analysis has revealed that although the archaeal system incorporates various facets of the eukaryal and bacterial targeting systems, numerous aspects of the archaeal system are unique to this domain of life. Moreover, it is becoming increasingly clear that elucidation of the archaeal SRP pathway will provide answers to basic questions about protein targeting that cannot be obtained from examination of eukaryal or bacterial models. In this review, recent data regarding the molecular composition, functional behavior and evolutionary significance of the archaeal signal recognition particle pathway are discussed.

scholarly journals Biochemical analysis of ligand-induced receptor patching and capping using a novel immunolactoperoxidase iodination technique.

1979 ◽  
Vol 83 (3) ◽  
pp. 649-656 ◽  
Author(s):  
L Y Bourguignon
Keyword(s):  
Membrane Proteins ◽  
Biochemical Analysis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Histocompatibility Antigen ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Cytochemical Analysis ◽  
Novel Approach ◽  
Surface Receptor ◽  
Specific Ligand

A novel approach for the analysis of membrane proteins involved in ligand-induced surface receptor patching and capping is described. The technique is based on the use of immunolactoperoxidase (immuno-LPO) conjugates which catalyze the iodination of those surface proteins with available tyrosine groups that are located in the immediate vicinity of the patch or cap of a particular antigen. We have used the patching and capping of the H-2 (histocompatibility) antigen on mouse thymocytes to illustrate this method. However, this technique should be generally applicable to any cell surface proteins which can be induced to form patches or caps by a specific ligand. Cytochemical analysis indicates that the immuno-LPO conjugates induce the same patching and capping of the H-2 antigen as does the unconjugated antibody. Biochemical analysis of the 125I-labeled proteins by SDS polyacrylamide gel electrophoresis indicates that a large membrane protein (mol wt of approximately 200,000 daltons) is closely associated with H-2 patches and caps. Since a number of other prominent membrane proteins are not labeled by this procedure, selective redistribution of certain surface proteins must be occurring during H-2 antibody-induced patching and capping.

Ultrastructure of granular materials in rat incisor enamel organ at early maturation stage

1984 ◽  
Vol 29 (2) ◽  
pp. 157-159 ◽  
Author(s):  
K. Yamamoto ◽  
S. Matsuo ◽  
T. Nishimoto ◽  
S. Wakisaka ◽  
H. Ichikawa ◽  
...  
Keyword(s):  
Granular Materials ◽  
Enamel Organ ◽  
Maturation Stage ◽  
Rat Incisor ◽  
Early Maturation

scholarly journals Biochemical composition and fatty acid profile of gonads from wild and cultured Shortfin corvina (Cynoscion parvipinnis) during the early maturation stage

2017 ◽  
Vol 69 (3) ◽  
pp. 491-501 ◽  
Author(s):  
Mayra González-Félix ◽  
Perla Urquidez-Bejarano ◽  
Martin Perez-Velazquez ◽  
Reina Castro-Longoria ◽  
Celia Vazquez-Boucard
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Profile ◽  
Biochemical Composition ◽  
Gulf Of California ◽  
Gonadosomatic Index ◽  
Wild Fish ◽  
Maturation Stage ◽  
Human Consumption ◽  
Early Maturation ◽  
Cultured Fish

Cynoscion parvipinnis is an important fisheries resource of the Gulf of California used locally for human consumption. Its aquaculture potential has recently been demonstrated, and cultured organisms are already available. In this study, the gonadal developmental stage, proximate composition, fatty acid profile and other biochemical and biological indices of wild and cultured fish were characterized. A total of 80 fish, 30 cultured (15 female and 15 male) and 50 wild (31 female and 19 male), captured in November at Santa Rosa, Sonora, Mexico, were analyzed. Histological analyses of the gonads showed that 100% of the wild and cultured fish were at an early maturation stage. Wild fish had greater body weight, total length and gonadosomatic index. Cultured female fish (19.64%) possessed a slightly higher protein content in their gonads than wild females (17.11%), whereas males had similar values (14.00 and 14.83%). Cultured females (10.85%) and males (20.48%) had a significantly greater crude fat content than wild fish (female: 2.05%, male: 11.05%). Palmitic acid was the most abundant fatty acid (FA), ranging from 128.58-164.84 mg of 16:0 g-1 of gonad wet weight. After 16:0, highly unsaturated FAs like DHA, ARA and EPA were the major FA in gonadal tissue; n-3 FAs were quantitatively higher than n-6 FAs, while the n-3/n-6 ratios ranged from 2.08-2.81. In general, the biochemical composition of the gonad of wild and cultured organisms at an early maturation stage was quite similar. These data may serve as indicators of dietary requirements for a maturation diet for broodstock culture.

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